Journal articles: 'Hogu'

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Yu, Zutao, Mengting Ai, Soumen K. Samanta, Fumitaka Hashiya, Junichi Taniguchi, Sefan Asamitsu, Shuji Ikeda, et al. "A synthetic transcription factor pair mimic for precise recruitment of an epigenetic modifier to the targeted DNA locus." Chemical Communications 56, no. 15 (2020): 2296–99. http://dx.doi.org/10.1039/c9cc09608f.

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Yu, Zutao, Chuanxin Guo, Yulei Wei, Kaori Hashiya, Toshikazu Bando, and Hiroshi Sugiyama. "Pip-HoGu: An Artificial Assembly with Cooperative DNA Recognition Capable of Mimicking Transcription Factor Pairs." Journal of the American Chemical Society 140, no. 7 (February 8, 2018): 2426–29. http://dx.doi.org/10.1021/jacs.7b13275.

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한성주. "Hogu Materials of Lee Gwi-jae's family in Samcheok area in the 18~19th century and their meaning." 古文書硏究 52, no. ll (February 2018): 115–44. http://dx.doi.org/10.21027/manusc.2018.52..005.

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byung gyung kim. "The Effects of Taekwondo Globalness on Nation Brand Image Creation through Users Experience of Electronic Hogu: Moderation Effect of Players' Ethnocentrism." TAEKWONDO JOURNAL OF KUKKIWON 8, no. 4 (December 2017): 311–34. http://dx.doi.org/10.24881/tjk.2017.8.4.311.

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Tandy, Kisha. "Julie Rodrigues Widholm, Barbara Jones-Hogu: Resist, Relate, Unite, 1968–1975. Chicago: DePaul University Art Museum, 2018. Pp. 104. $60.00 (cloth)." Journal of African American History 106, no. 1 (January 1, 2021): 163–64. http://dx.doi.org/10.1086/712010.

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Kim, Bong-Gyung. "A Study on the Relationship between Taekwondo Perceived Quality, User Attitude, and Reuse Intention of Electronic Hogu: Moderation Effect of Players’ Ethnocentrism." Korean Journal of Sports Science 28, no. 4 (August 31, 2019): 613–25. http://dx.doi.org/10.35159/kjss.2019.08.28.4.613.

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Urcola, Hernán A., and Scott H. Irwin. "Hog Options: Contract Redesign and Market Efficiency." Journal of Agricultural and Applied Economics 42, no. 4 (November 2010): 773–90. http://dx.doi.org/10.1017/s1074070800003953.

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This article tests the efficiency of the hog options market and assesses the impact of the 1996 contract redesign on efficiency. We find that the hog options market is efficient, but some options yielded excess returns during the live hogs period but not during the lean hogs period. Our findings indicate that the hog options market is efficient and is consistent with the new contract improving the efficiency of the market. However, other market conditions such as lower transaction costs during the lean hogs period can also contribute to reduce expected option returns during the latter period.

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Winkler, Astrid, Christopher Arkind, Christopher P. Mattison, Anne Burkholder, Kathryn Knoche, and Irene Ota. "Heat Stress Activates the Yeast High-Osmolarity Glycerol Mitogen-Activated Protein Kinase Pathway, and Protein Tyrosine Phosphatases Are Essential under Heat Stress." Eukaryotic Cell 1, no. 2 (April 2002): 163–73. http://dx.doi.org/10.1128/ec.1.2.163-173.2002.

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ABSTRACT The yeast high-osmolarity glycerol (HOG) mitogen-activated protein kinase (MAPK) pathway has been characterized as being activated solely by osmotic stress. In this work, we show that the Hog1 MAPK is also activated by heat stress and that Sho1, previously identified as a membrane-bound osmosensor, is required for heat stress activation of Hog1. The two-component signaling protein, Sln1, the second osmosensor in the HOG pathway, was not involved in heat stress activation of Hog1, suggesting that the Sho1 and Sln1 sensors discriminate between stresses. The possible function of Hog1 activation during heat stress was examined, and it was found that the hog1Δ strain does not recover as rapidly from heat stress as well as the wild type. It was also found that protein tyrosine phosphatases (PTPs) Ptp2 and Ptp3, which inactivate Hog1, have two functions during heat stress. First, they are essential for survival at elevated temperatures, preventing lethality due to Hog1 hyperactivation. Second, they block inappropriate cross talk between the HOG and the cell wall integrity MAPK pathways, suggesting that PTPs are important for maintaining specificity in MAPK signaling pathways.

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Westfall, Patrick J., and Jeremy Thorner. "Analysis of Mitogen-Activated Protein Kinase Signaling Specificity in Response to Hyperosmotic Stress: Use of an Analog-Sensitive HOG1 Allele." Eukaryotic Cell 5, no. 8 (August 2006): 1215–28. http://dx.doi.org/10.1128/ec.00037-06.

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ABSTRACT When confronted with a marked increase in external osmolarity, budding yeast (Saccharomyces cerevisiae) cells utilize a conserved mitogen-activated protein kinase (MAPK) signaling cascade (the high-osmolarity glycerol or HOG pathway) to elicit cellular responses necessary to permit continued growth. One input that stimulates the HOG pathway requires the integral membrane protein and putative osmosensor Sho1, which recruits and enables activation of the MAPK kinase kinase Ste11. In mutants that lack the downstream MAPK kinase (pbs2Δ) or the MAPK (hog1Δ) of the HOG pathway, Ste11 activated by hyperosmotic stress is able to inappropriately stimulate the pheromone response pathway. This loss of signaling specificity is known as cross talk. To determine whether it is the Hog1 polypeptide per se or its kinase activity that is necessary to prevent cross talk, we constructed a fully functional analog-sensitive allele of HOG1 to permit acute inhibition of this enzyme without other detectable perturbations of the cell. We found that the catalytic activity of Hog1 is required continuously to prevent cross talk between the HOG pathway and both the pheromone response and invasive growth pathways. Moreover, contrary to previous reports, we found that the kinase activity of Hog1 is necessary for its stress-induced nuclear import. Finally, our results demonstrate a role for active Hog1 in maintaining signaling specificity under conditions of persistently high external osmolarity.

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O'Rourke, Sean M., and Ira Herskowitz. "Unique and Redundant Roles for HOG MAPK Pathway Components as Revealed by Whole-Genome Expression Analysis." Molecular Biology of the Cell 15, no. 2 (February 2004): 532–42. http://dx.doi.org/10.1091/mbc.e03-07-0521.

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The Saccharomyces cerevisiae high osmolarity glycerol (HOG) mitogen-activated protein kinase pathway is required for osmoadaptation and contains two branches that activate a mitogen-activated protein kinase (Hog1) via a mitogen-activated protein kinase kinase (Pbs2). We have characterized the roles of common pathway components (Hog1 and Pbs2) and components in the two upstream branches (Ste11, Sho1, and Ssk1) in response to elevated osmolarity by using whole-genome expression profiling. Several new features of the HOG pathway were revealed. First, Hog1 functions during gene induction and repression, cross talk inhibition, and in governing the regulatory period. Second, the phenotypes of pbs2 and hog1 mutants are identical, indicating that the sole role of Pbs2 is to activate Hog1. Third, the existence of genes whose induction is dependent on Hog1 and Pbs2 but not on Ste11 and Ssk1 suggests that there are additional inputs into Pbs2 under our inducing conditions. Fourth, the two upstream pathway branches are not redundant: the Sln1-Ssk1 branch has a much more prominent role than the Sho1-Ste11 branch for activation of Pbs2 by modest osmolarity. Finally, the general stress response pathway and both branches of the HOG pathway all function at high osmolarity. These studies demonstrate that cells respond to increased osmolarity by using different signal transduction machinery under different conditions.

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Lipscomb, Donald J. "Impacts of Feral Hogs on Longleaf Pine Regeneration." Southern Journal of Applied Forestry 13, no. 4 (November 1, 1989): 177–81. http://dx.doi.org/10.1093/sjaf/13.4.177.

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Abstract Moderate to heavy populations of feral hogs (Sus scrofa domesticus) were fenced out of 32 tenth-acre plots in a natural regeneration area for longleaf pine (Pinus palustris Mill.) After two growing seasons the fenced areas contained the equivalent of 500 fire-resistant longleaf pineseedlings per acre while corresponding unfenced areas contained only 8 fire-resistant seedlings per acre. Thus free ranging feral hogs caused a crop failure in these natural regeneration stands of longleaf pine. There was evidence that feral hogs selected the larger seedlings. Thus longleafpine seedling crops that survive feral hog depredation will be progressively less competitive and vigorous. Areas with feral hog problems may need to control the hog population by trapping, hunting, or fencing. South. J. Appl. For. 13(4):177-181.

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Franken, Jason R. V., and Joe L. Parcell. "Evaluation of Market Thinness for Hogs and Pork." Journal of Agricultural and Applied Economics 44, no. 4 (November 2012): 461–75. http://dx.doi.org/10.1017/s1074070800024044.

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We investigate thinness of hog and pork markets in terms of quantity and representativeness of negotiated transactions. Transactional volume imparts marginally greater confidence in pricing precision for Iowa-Southern Minnesota negotiated hogs than for the national carcass cut-out, suggesting that contracts tying prices to the former rather than the latter may be more representative of industry conditions. Extending mandatory price reporting to pork may remedy this discrepancy. Despite declining volume, terminal hog markets may price accurately off of Iowa-Southern Minnesota prices. Hog quality differentials across procurement methods are documented, and quality of negotiated hogs is shown to decline with declining volume.

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Albertyn, J., S. Hohmann, J. M. Thevelein, and B. A. Prior. "GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high-osmolarity glycerol response pathway." Molecular and Cellular Biology 14, no. 6 (June 1994): 4135–44. http://dx.doi.org/10.1128/mcb.14.6.4135.

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The yeast Saccharomyces cerevisiae responds to osmotic stress, i.e., an increase in osmolarity of the growth medium, by enhanced production and intracellular accumulation of glycerol as a compatible solute. We have cloned a gene encoding the key enzyme of glycerol synthesis, the NADH-dependent cytosolic glycerol-3-phosphate dehydrogenase, and we named it GPD1. gpd1 delta mutants produced very little glycerol, and they were sensitive to osmotic stress. Thus, glycerol production is indeed essential for the growth of yeast cells during reduced water availability. hog1 delta mutants lacking a protein kinase involved in osmostress-induced signal transduction (the high-osmolarity glycerol response [HOG] pathway) failed to increase glycerol-3-phosphate dehydrogenase activity and mRNA levels when osmotic stress was imposed. Thus, expression of GPD1 is regulated through the HOG pathway. However, there may be Hog1-independent mechanisms mediating osmostress-induced glycerol accumulation, since a hog1 delta strain could still enhance its glycerol content, although less than the wild type. hog1 delta mutants are more sensitive to osmotic stress than isogenic gpd1 delta strains, and gpd1 delta hog1 delta double mutants are even more sensitive than either single mutant. Thus, the HOG pathway most probably has additional targets in the mechanism of adaptation to hypertonic medium.

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Albertyn, J., S. Hohmann, J. M. Thevelein, and B. A. Prior. "GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high-osmolarity glycerol response pathway." Molecular and Cellular Biology 14, no. 6 (June 1994): 4135–44. http://dx.doi.org/10.1128/mcb.14.6.4135-4144.1994.

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The yeast Saccharomyces cerevisiae responds to osmotic stress, i.e., an increase in osmolarity of the growth medium, by enhanced production and intracellular accumulation of glycerol as a compatible solute. We have cloned a gene encoding the key enzyme of glycerol synthesis, the NADH-dependent cytosolic glycerol-3-phosphate dehydrogenase, and we named it GPD1. gpd1 delta mutants produced very little glycerol, and they were sensitive to osmotic stress. Thus, glycerol production is indeed essential for the growth of yeast cells during reduced water availability. hog1 delta mutants lacking a protein kinase involved in osmostress-induced signal transduction (the high-osmolarity glycerol response [HOG] pathway) failed to increase glycerol-3-phosphate dehydrogenase activity and mRNA levels when osmotic stress was imposed. Thus, expression of GPD1 is regulated through the HOG pathway. However, there may be Hog1-independent mechanisms mediating osmostress-induced glycerol accumulation, since a hog1 delta strain could still enhance its glycerol content, although less than the wild type. hog1 delta mutants are more sensitive to osmotic stress than isogenic gpd1 delta strains, and gpd1 delta hog1 delta double mutants are even more sensitive than either single mutant. Thus, the HOG pathway most probably has additional targets in the mechanism of adaptation to hypertonic medium.

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Train, Clément-Marie, Miguel Pignatelli, Adrian Altenhoff, and Christophe Dessimoz. "iHam and pyHam: visualizing and processing hierarchical orthologous groups." Bioinformatics 35, no. 14 (December 3, 2018): 2504–6. http://dx.doi.org/10.1093/bioinformatics/bty994.

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Abstract Summary The evolutionary history of gene families can be complex due to duplications and losses. This complexity is compounded by the large number of genomes simultaneously considered in contemporary comparative genomic analyses. As provided by several orthology databases, hierarchical orthologous groups (HOGs) are sets of genes that are inferred to have descended from a common ancestral gene within a species clade. This implies that the set of HOGs defined for a particular clade correspond to the ancestral genes found in its last common ancestor. Furthermore, by keeping track of HOG composition along the species tree, it is possible to infer the emergence, duplications and losses of genes within a gene family of interest. However, the lack of tools to manipulate and analyse HOGs has made it difficult to extract, display and interpret this type of information. To address this, we introduce interactive HOG analysis method, an interactive JavaScript widget to visualize and explore gene family history encoded in HOGs and python HOG analysis method, a python library for programmatic processing of genes families. These complementary open source tools greatly ease adoption of HOGs as a scalable and interpretable concept to relate genes across multiple species. Availability and implementation iHam’s code is available at https://github.com/DessimozLab/iHam or can be loaded dynamically. pyHam’s code is available at https://github.com/DessimozLab/pyHam and or via the pip package ‘pyham’.

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Okoro, C. K., B. S. Wilson, J. Lorenzo-Morales, and R. D. Robinson. "Gastrointestinal helminths of wild hogs and their potential livestock and public health significance in Jamaica." Journal of Helminthology 90, no. 2 (January 9, 2015): 139–43. http://dx.doi.org/10.1017/s0022149x14000881.

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AbstractAn investigation into the potential for transmission of gastrointestinal helminths from wild hogs to livestock and humans was prompted by concerns of recreational wild-hog hunting in the Caribbean region and the recent practice, by livestock farmers in Jamaica, of co-rearing wild and domesticated swine. Thirty-one wild hogs from the Hellshire Hills, a dry limestone forest in southern Jamaica, were necropsied during the period June 2004 to August 2006. Thirteen of the captured animals were male and 18 female. Four species of adult helminths were recovered from the gastrointestinal tracts of the wild hogs: Hyostrongylus rubidus (77%), Globocephalus urosubulatus (48%), Oesophagostomum dentatum (42%) and Macroacanthorhynchus hirudinaceus (77%). Two (6.2%), ten (32.2%) and 18 (58.0%) hogs harboured one, two and three species of helminths, respectively. Mean infection intensities varied from 8.1 for M. hirudinaceus, to 115.5 for O. dentatum. There was no association between any of the recovered helminths and sex of the host; however, a multivariate analysis indicated a positive association between the prevalence of G. urosubulatus and host age (odds ratio (OR) = 6.517). Domesticated hogs co-reared with wild hogs are potentially at risk of infection with all four helminths, while wild-hog hunters and pig farmers may be exposed to M. hirudinaceus.

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Warmka, Janel, Jennifer Hanneman, Ji Lee, Dipesh Amin, and Irene Ota. "Ptc1, a Type 2C Ser/Thr Phosphatase, Inactivates the HOG Pathway by Dephosphorylating the Mitogen-Activated Protein Kinase Hog1." Molecular and Cellular Biology 21, no. 1 (January 1, 2001): 51–60. http://dx.doi.org/10.1128/mcb.21.1.51-60.2001.

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ABSTRACT The HOG (high-osmolarity glycerol) mitogen-activated protein kinase (MAPK) pathway regulates the osmotic stress response in the yeast Saccharomyces cerevisiae. Three type 2C Ser/Thr phosphatases (PTCs), Ptc1, Ptc2, and Ptc3, have been isolated as negative regulators of this pathway. Previously, multicopy expression of PTC1 and PTC3 was shown to suppress lethality of the sln1Δ strain due to hyperactivation of the HOG pathway. In this work, we show thatPTC2 also suppresses sln1Δ lethality. Furthermore, the phosphatase activity of these PTCs was needed for suppression, as mutation of a conserved Asp residue, likely to coordinate a metal ion, inactivated PTCs. Further analysis of Ptc1 function in vivo showed that it inactivates the MAPK, Hog1, but not the MEK, Pbs2. In the wild type, Hog1 kinase activity increased transiently, ∼12-fold in response to osmotic stress, while overexpression of PTC1 limited activation to ∼3-fold. In contrast, overexpression of PTC1 did not inhibit phosphorylation of Hog1 Tyr in the phosphorylation lip, suggesting that Ptc1 does not act on Pbs2. Deletion of PTC1 also strongly affected Hog1, leading to high basal Hog1 activity and sustained Hog1 activity in response to osmotic stress, the latter being consistent with a role for Ptc1 in adaptation. In vitro, Ptc1 but not the metal binding site mutant, Ptc1D58N, inactivated Hog1 by dephosphorylating the phosphothreonine but not the phosphotyrosine residue in the phosphorylation lip. Consistent with its role as a negative regulator of Hog1, which accumulates in the nucleus upon activation, Ptc1 was found in both the nucleus and the cytoplasm. Thus, one function of Ptc1 is to inactivate Hog1.

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Zhao, Yunying, Shiyun Li, Jing Wang, Yingli Liu, and Yu Deng. "Roles of High Osmolarity Glycerol and Cell Wall Integrity Pathways in Cadmium Toxicity in Saccharomyces cerevisiae." International Journal of Molecular Sciences 22, no. 12 (June 8, 2021): 6169. http://dx.doi.org/10.3390/ijms22126169.

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Cadmium is a carcinogen that can induce ER stress, DNA damage, oxidative stress and cell death. The yeast mitogen-activated protein kinase (MAPK) signalling pathways paly crucial roles in response to various stresses. Here, we demonstrate that the unfolded protein response (UPR) pathway, the high osmolarity glycerol (HOG) pathway and the cell wall integrity (CWI) pathway are all essential for yeast cells to defend against the cadmium-induced toxicity, including the elevated ROS and cell death levels induced by cadmium. We show that the UPR pathway is required for the cadmium-induced phosphorylation of HOG_MAPK Hog1 but not for CWI_MAPK Slt2, while Slt2 but not Hog1 is required for the activation of the UPR pathway through the transcription factors of Swi6 and Rlm1. Moreover, deletion of HAC1 and IRE1 could promote the nuclear accumulation of Hog1, and increase the cytosolic and bud neck localisation of Slt2, indicating crucial roles of Hog1 and Slt2 in regulating the cellular process in the absence of UPR pathway. Altogether, our findings highlight the significance of these two MAPK pathways of HOG and CWI and their interrelationship with the UPR pathway in responding to cadmium-induced toxicity in budding yeast.

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Gillespie, Jeffrey M., and Vernon R. Eidman. "The Effect of Risk and Autonomy on Independent Hog Producers' Contracting Decisions." Journal of Agricultural and Applied Economics 30, no. 1 (July 1998): 175–88. http://dx.doi.org/10.1017/s1074070800008154.

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AbstractThe introduction of vertical coordination in the hog industry has provided producers with new business arrangements for raising hogs. While some researchers have elicited utility functions for hog producers on the basis of income risk, none have addressed autonomy, a factor which appears to be important in business arrangement selection for independent family hog operations. In this study, a method is developed for eliciting a multi-attribute function with attributes of income and autonomy. Utility functions are elicited for a group of Minnesota farrow-to-finish hog producers. For these producers, autonomy dominated risk as the most important attribute in business arrangement selection.

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Conde, Cristina, Daniela Moctezuma, Isaac Martín De Diego, and Enrique Cabello. "HoGG: Gabor and HoG-based human detection for surveillance in non-controlled environments." Neurocomputing 100 (January 2013): 19–30. http://dx.doi.org/10.1016/j.neucom.2011.12.037.

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Colling, Phil L., and Scott H. Irwin. "The Reaction of Live Hog Futures Prices to USDA Hogs and Pigs Reports." American Journal of Agricultural Economics 72, no. 1 (February 1990): 84–94. http://dx.doi.org/10.2307/1243147.

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Migdal, Iwona, Yulia Ilina, Markus J. Tamás, and Robert Wysocki. "Mitogen-Activated Protein Kinase Hog1 Mediates Adaptation to G1 Checkpoint Arrest during Arsenite and Hyperosmotic Stress." Eukaryotic Cell 7, no. 8 (June 13, 2008): 1309–17. http://dx.doi.org/10.1128/ec.00038-08.

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ABSTRACT Cells slow down cell cycle progression in order to adapt to unfavorable stress conditions. Yeast (Saccharomyces cerevisiae) responds to osmotic stress by triggering G1 and G2 checkpoint delays that are dependent on the mitogen-activated protein kinase (MAPK) Hog1. The high-osmolarity glycerol (HOG) pathway is also activated by arsenite, and the hog1Δ mutant is highly sensitive to arsenite, partly due to increased arsenite influx into hog1Δ cells. Yeast cell cycle regulation in response to arsenite and the role of Hog1 in this process have not yet been analyzed. Here, we found that long-term exposure to arsenite led to transient G1 and G2 delays in wild-type cells, whereas cells that lack the HOG1 gene or are defective in Hog1 kinase activity displayed persistent G1 cell cycle arrest. Elevated levels of intracellular arsenite and “cross talk” between the HOG and pheromone response pathways, observed in arsenite-treated hog1Δ cells, prolonged the G1 delay but did not cause a persistent G1 arrest. In contrast, deletion of the SIC1 gene encoding a cyclin-dependent kinase inhibitor fully suppressed the observed block of G1 exit in hog1Δ cells. Moreover, the Sic1 protein was stabilized in arsenite-treated hog1Δ cells. Interestingly, Sic1-dependent persistent G1 arrest was also observed in hog1Δ cells during hyperosmotic stress. Taken together, our data point to an important role of the Hog1 kinase in adaptation to stress-induced G1 cell cycle arrest.

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Rodríguez-Pupo, Eya Caridad, Yordanis Pérez-Llano, José Raunel Tinoco-Valencia, Norma Silvia Sánchez, Francisco Padilla-Garfias, Martha Calahorra, Nilda del C. Sánchez, et al. "Osmolyte Signatures for the Protection of Aspergillus sydowii Cells under Halophilic Conditions and Osmotic Shock." Journal of Fungi 7, no. 6 (May 26, 2021): 414. http://dx.doi.org/10.3390/jof7060414.

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Aspergillus sydowii is a moderate halophile fungus extensively studied for its biotechnological potential and halophile responses, which has also been reported as a coral reef pathogen. In a recent publication, the transcriptomic analysis of this fungus, when growing on wheat straw, showed that genes related to cell wall modification and cation transporters were upregulated under hypersaline conditions but not under 0.5 M NaCl, the optimal salinity for growth in this strain. This led us to study osmolyte accumulation as a mechanism to withstand moderate salinity. In this work, we show that A. sydowii accumulates trehalose, arabitol, mannitol, and glycerol with different temporal dynamics, which depend on whether the fungus is exposed to hypo- or hyperosmotic stress. The transcripts coding for enzymes responsible for polyalcohol synthesis were regulated in a stress-dependent manner. Interestingly, A. sydowii contains three homologs (Hog1, Hog2 and MpkC) of the Hog1 MAPK, the master regulator of hyperosmotic stress response in S. cerevisiae and other fungi. We show a differential regulation of these MAPKs under different salinity conditions, including sustained basal Hog1/Hog2 phosphorylation levels in the absence of NaCl or in the presence of 2.0 M NaCl, in contrast to what is observed in S. cerevisiae. These findings indicate that halophilic fungi such as A. sydowii utilize different osmoadaptation mechanisms to hypersaline conditions.

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Reiser, Vladimı́r, Helmut Ruis, and Gustav Ammerer. "Kinase Activity-dependent Nuclear Export Opposes Stress-induced Nuclear Accumulation and Retention of Hog1 Mitogen-activated Protein Kinase in the Budding Yeast Saccharomyces cerevisiae." Molecular Biology of the Cell 10, no. 4 (April 1999): 1147–61. http://dx.doi.org/10.1091/mbc.10.4.1147.

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Budding yeast adjusts to increases in external osmolarity via a specific mitogen-activated protein kinase signal pathway, the high-osmolarity glycerol response (HOG) pathway. Studies with a functional Hog1–green fluorescent protein (GFP) fusion reveal that even under nonstress conditions the mitogen-activated protein kinase Hog1 cycles between cytoplasmic and nuclear compartments. The basal distribution of the protein seems independent of its activator, Pbs2, and independent of its phosphorylation status. Upon osmotic challenge, the Hog1–GFP fusion becomes rapidly concentrated in the nucleus from which it is reexported after return to an iso-osmotic environment or after adaptation to high osmolarity. The preconditions and kinetics of increased nuclear localization correlate with those found for the dual phosphorylation of Hog1–GFP. The duration of Hog1 nuclear residence is modulated by the presence of the general stress activators Msn2 and Msn4. Reexport of Hog1 to the cytoplasm does not require de novo protein synthesis but depends on Hog1 kinase activity. Thus, at least three different mechanisms contribute to the intracellular distribution pattern of Hog1: phosphorylation-dependent nuclear accumulation, retention by nuclear targets, and a kinase-induced export.

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Vylkova, Slavena, Woong Sik Jang, Wansheng Li, Namrata Nayyar, and Mira Edgerton. "Histatin 5 Initiates Osmotic Stress Response in Candida albicans via Activation of the Hog1 Mitogen-Activated Protein Kinase Pathway." Eukaryotic Cell 6, no. 10 (August 22, 2007): 1876–88. http://dx.doi.org/10.1128/ec.00039-07.

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ABSTRACT Histatin 5 (Hst 5) is a salivary cationic peptide that has toxicity for Candida albicans by inducing rapid cellular ion imbalance and cell volume loss. Microarray analyses of peptide-treated cells were used to evaluate global gene responses elicited by Hst 5. The major transcriptional response of C. albicans to Hst 5 was expression of genes involved in adaptation to osmotic stress, including production of glycerol (RHR2, SKO1, and PDC11) and the general stress response (CTA1 and HSP70). The oxidative-stress genes AHP1, TRX1, and GPX1 were mildly induced by Hst 5. Cell defense against Hst 5 was dependent on the Hog1 mitogen-activated protein kinase (MAPK) pathway, since C. albicans hog1/hog1 mutants were significantly hypersensitive to Hst 5 but not to Mkc1 MAPK or Cek1 MAPK mutants. Activation of the high-osmolarity glycerol (HOG) pathway was demonstrated by phosphorylation of Hog1 MAPK as well as by glycerol production following Hst 5 treatment in a dose-dependent manner. C. albicans cells prestressed with sorbitol were less sensitive to subsequent Hst 5 treatment; however, cells treated concurrently with osmotic stress and Hst 5 were hypersensitive to Hst 5. In contrast, cells subjected to oxidative stress had no difference in sensitivity to Hst 5. These results suggest a common underlying cellular response to osmotic stress and Hst 5. The HOG stress response pathway likely represents a significant and effective challenge to physiological levels of Hst 5 and other toxic peptides in fungal cells.

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Hall, J. P., V. Cherkasova, E. Elion, M. C. Gustin, and E. Winter. "The osmoregulatory pathway represses mating pathway activity in Saccharomyces cerevisiae: isolation of a FUS3 mutant that is insensitive to the repression mechanism." Molecular and Cellular Biology 16, no. 12 (December 1996): 6715–23. http://dx.doi.org/10.1128/mcb.16.12.6715.

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Mitogen-activated protein (MAP) kinase cascades are conserved signal transduction pathways that are required for eukaryotic cells to respond to a variety of stimuli. Multiple MAP kinase pathways can function within a single cell type; therefore, mechanisms that insulate one MAP kinase pathway from adventitious activations by parallel pathways may exist. We have studied interactions between the mating pheromone response and the osmoregulatory (high-osmolarity glycerol response [HOG]) pathways in Saccharomyces cerevisiae which utilize the MAP kinases Fus3p and Hog1p, respectively. Inactivating mutations in HOG pathway kinases cause an increase in the phosphotyrosine content of Fus3p, greater expression of pheromone-responsive genes, and increased sensitivity to growth arrest by pheromone. Therefore, the HOG pathway represses mating pathway activity. In a HOG1+ strain, Fus3p phosphotyrosine increases modestly and transiently following an increase in the extracellular osmolarity; however, it increases to a greater extent and for a sustained duration in a hog1-delta strain. Thus, the HOG-mediated repression of mating pathway activity may insulate the mating pathway from activation by osmotic stress. A FUS3 allele whose gene product is resistant to the HOG-mediated repression of its phosphotyrosine content has been isolated. This mutant encodes an amino acid substitution in the highly conserved DPXDEP motif in subdomain XI. Other investigators have shown that the corresponding amino acid is also mutated in a gain-of-function allele of the MAP kinase encoded by the rolled locus in Drosophila melanogaster. These data suggest that the DPXDEP motif plays a role in the negative regulation of MAP kinases.

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Alonso-Monge, Rebeca, Sara Carvaihlo, Cesar Nombela, Eduardo Rial, and Jesús Pla. "The Hog1 MAP kinase controls respiratory metabolism in the fungal pathogen Candida albicans." Microbiology 155, no. 2 (February 1, 2009): 413–23. http://dx.doi.org/10.1099/mic.0.023309-0.

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Signal transduction pathways mediated by mitogen-activated protein kinases (MAPKs) play crucial roles in eukaryotic cells. In the pathogenic fungus Candida albicans the HOG MAPK pathway regulates the response to external stresses (osmotic and oxidative among others) and is involved in morphogenesis and virulence. We show here that the lack of the Hog1 MAPK increases the sensitivity of this fungus to inhibitors of the respiratory chain. hog1 mutants also show an enhanced basal respiratory rate compared to parental strains, and higher levels of intracellular reactive oxygen species despite an increased expression of detoxifying enzymes. We also demonstrate that although oxidative phosphorylation is essentially unaffected, hog1 mutants have an altered mitochondrial membrane potential. Data indicate that hog1-defective mutants are more dependent on mitochondrial ATP synthesis, probably due to an increased cellular ATP demand. Our results therefore link a MAPK pathway with respiratory metabolism in pathogenic fungi.

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Su, Chang, Yang Lu, and Haoping Liu. "Reduced TOR signaling sustains hyphal development inCandida albicansby lowering Hog1 basal activity." Molecular Biology of the Cell 24, no. 3 (February 2013): 385–97. http://dx.doi.org/10.1091/mbc.e12-06-0477.

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Candida albicans is able to undergo reversible morphological changes between yeast and hyphal forms in response to environmental cues. This morphological plasticity is essential for its pathogenesis. Hyphal development requires two temporally linked changes in promoter chromatin, which is sequentially regulated by temporarily clearing the transcription inhibitor Nrg1 upon activation of cAMP/protein kinase A and promoter recruitment of the histone deacetylase Hda1 under reduced target of rapamycin (Tor1) signaling. The GATA family transcription factor Brg1 recruits Hda1 to promoters for sustained hyphal development, and BRG1 expression is a readout of reduced Tor1 signaling. How Tor1 regulates BRG1 expression is not clear. Using a forward genetic screen for mutants that can sustain hyphal elongation in rich media, we found hog1, ssk2, and pbs2 mutants of the HOG mitogen-activated protein kinase pathway to express BRG1 irrespective of rapamycin. Furthermore, rapamycin lowers the basal activity of Hog1 through the functions of the two Hog1 tyrosine phosphatases Ptp2 and Ptp3. Active Hog1 represses the expression of BRG1 via the transcriptional repressor Sko1 as Sko1 disassociates from the promoter of BRG1 in the hog1 mutant or in rapamycin. Our data suggest that reduced Tor1 signaling lowers Hog1 basal activity via Hog1 phosphatases to activate BRG1 expression for hyphal elongation.

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Schroeder, Ted C., J. R. Mintert, and John M. Blair. "The reaction of slaughter hog cash and futures prices to USDA hogs and pigs reports." Kansas Agricultural Experiment Station Research Reports, no. 10 (January 1, 1989): 166–70. http://dx.doi.org/10.4148/2378-5977.6222.

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Argimón, Silvia, Saranna Fanning, Jill R. Blankenship, and Aaron P. Mitchell. "Interaction between the Candida albicans High-Osmolarity Glycerol (HOG) Pathway and the Response to Human β-Defensins 2 and 3." Eukaryotic Cell 10, no. 2 (December 3, 2010): 272–75. http://dx.doi.org/10.1128/ec.00133-10.

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ABSTRACT Human β-defensins 2 and 3 are small cationic peptides with antimicrobial activity against the fungal pathogen Candida albicans . We found that hog1 and pbs2 mutants were hypersensitive to treatment with these peptides, pointing to a role of the high-osmolarity glycerol (HOG) pathway in the response to defensin-induced cell injury.

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Lee, Kyung-Tae, Hyo-Jeong Byun, Kwang-Woo Jung, Joohyeon Hong, Eunji Cheong, and Yong-Sun Bahn. "Distinct and Redundant Roles of Protein Tyrosine Phosphatases Ptp1 and Ptp2 in Governing the Differentiation and Pathogenicity of Cryptococcus neoformans." Eukaryotic Cell 13, no. 6 (April 11, 2014): 796–812. http://dx.doi.org/10.1128/ec.00069-14.

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ABSTRACTProtein tyrosine phosphatases (PTPs) serve as key negative-feedback regulators of mitogen-activated protein kinase (MAPK) signaling cascades. However, their roles and regulatory mechanisms in human fungal pathogens remain elusive. In this study, we characterized the functions of two PTPs, Ptp1 and Ptp2, inCryptococcus neoformans, which causes fatal meningoencephalitis.PTP1andPTP2were found to be stress-inducible genes, which were controlled by the MAPK Hog1 and the transcription factor Atf1. Ptp2 suppressed the hyperphosphorylation of Hog1 and was involved in mediating vegetative growth, sexual differentiation, stress responses, antifungal drug resistance, and virulence factor regulation through the negative-feedback loop of the HOG pathway. In contrast, Ptp1 was not essential for Hog1 regulation, despite its Hog1-dependent induction. However, in the absence of Ptp2, Ptp1 served as a complementary PTP to control some stress responses. In differentiation, Ptp1 acted as a negative regulator, but in a Hog1- and Cpk1-independent manner. Additionally, Ptp1 and Ptp2 localized to the cytosol but were enriched in the nucleus during the stress response, affecting the transient nuclear localization of Hog1. Finally, Ptp1 and Ptp2 played minor and major roles, respectively, in the virulence ofC. neoformans. Taken together, our data suggested that PTPs could be exploited as novel antifungal targets.

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Jones, Kelly C., Thomas A. Gorman, Brandon K. Rincon, John Allen, Carola A. Haas, and Richard M. Engeman. "Feral swine Sus scrofa: a new threat to the remaining breeding wetlands of the Vulnerable reticulated flatwoods salamander Ambystoma bishopi." Oryx 52, no. 4 (February 27, 2017): 669–76. http://dx.doi.org/10.1017/s0030605316001253.

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AbstractFeral swine Sus scrofa have been implicated as a major threat to sensitive habitats and ecosystems as well as threatened wildlife. Nevertheless, direct and indirect impacts on threatened species (especially small, fossorial species) are not well documented. The decline of the U.S. federally endangered reticulated flatwoods salamander Ambystoma bishopi, categorized as Vulnerable on the IUCN Red List, has been rapid and there are few remaining breeding locations for this species. The flatwoods salamander depends on complex herbaceous vegetation in all life stages, including eggs, larvae and adults. Historically sets of hog tracks have been observed only occasionally in the vicinity of monitored reticulated flatwoods salamander breeding wetlands, and damage to the wetlands had never been recorded. However, during the autumn–winter breeding season of 2013–2014 we observed a large increase in hog sign, including extensive rooting damage, in known flatwoods salamander breeding wetlands. Our objective was to assess the amount of hog sign and damage in these wetlands and to take corrective management actions to curb additional impacts. Of 28 wetlands surveyed for hog sign, presence was recorded at 68%, and damage at 54%. Of the 11 sites known to be occupied by flatwoods salamanders in 2013–2014, 64% had presence, and 55% had damage. We found that regular monitoring of disturbance in wetland habitats was a valuable tool to determine when intervention was needed and to assess the effectiveness of intervention. Habitat damage caused by feral hogs poses a potentially serious threat to the salamanders, which needs to be mitigated using methods to control and exclude hogs from this sensitive habitat.

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Reynolds, Todd B., B. Diane Hopkins, Matthew R. Lyons, and Todd R. Graham. "The High Osmolarity Glycerol Response (HOG) MAP Kinase Pathway Controls Localization of a Yeast Golgi Glycosyltransferase." Journal of Cell Biology 143, no. 4 (November 16, 1998): 935–46. http://dx.doi.org/10.1083/jcb.143.4.935.

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The yeast α-1,3-mannosyltransferase (Mnn1p) is localized to the Golgi by independent transmembrane and lumenal domain signals. The lumenal domain is localized to the Golgi complex when expressed as a soluble form (Mnn1-s) by exchange of its transmembrane domain for a cleavable signal sequence (Graham, T. R., and V. A. Krasnov. 1995. Mol. Biol. Cell. 6:809–824). Mutants that failed to retain the lumenal domain in the Golgi complex, called lumenal domain retention (ldr) mutants, were isolated by screening mutagenized yeast colonies for those that secreted Mnn1-s. Two genes were identified by this screen, HOG1, a gene encoding a mitogen-activated protein kinase (MAPK) that functions in the high osmolarity glycerol (HOG) pathway, and LDR1. We have found that basal signaling through the HOG pathway is required to localize Mnn1-s to the Golgi in standard osmotic conditions. Mutations in HOG1 and LDR1 also perturb localization of intact Mnn1p, resulting in its loss from early Golgi compartments and a concomitant increase of Mnn1p in later Golgi compartments.

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Alonso-Monge, Rebeca, José P. Guirao-Abad, Ruth Sánchez-Fresneda, Jesús Pla, Genoveva Yagüe, and Juan Carlos Argüelles. "The Fungicidal Action of Micafungin is Independent on Both Oxidative Stress Generation and HOG Pathway Signaling in Candida albicans." Microorganisms 8, no. 12 (November 26, 2020): 1867. http://dx.doi.org/10.3390/microorganisms8121867.

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In fungi, the Mitogen-Activated Protein kinase (MAPK) pathways sense a wide variety of environmental stimuli, leading to cell adaptation and survival. The HOG pathway plays an essential role in the pathobiology of Candida albicans, including the colonization of the gastrointestinal tract in a mouse model, virulence, and response to stress. Here, we examined the role of Hog1 in the C. albicans response to the clinically relevant antifungal Micafungin (MF), whose minimum inhibitory concentration (MIC) was identical in the parental strain (RM100) and in the isogenic homozygous mutant hog1 (0.016 mg/L). The cell viability was impaired without significant differences between the parental strain, the isogenic hog1 mutant, and the Hog1+ reintegrant. This phenotype was quite similar in a collection of hog1 mutants constructed in a different C. albicans background. MF-treated cells failed to induce a relevant increase of both reactive oxygen species (ROS) formation and activation of the mitochondrial membrane potential in parental and hog1 cells. MF was also unable to trigger any significant activation of the genes coding for the antioxidant activities catalase (CAT1) and superoxide dismutase (SOD2), as well as on the corresponding enzymatic activities, whereas a clear induction was observed in the presence of Amphotericin B (AMB), introduced as a positive control of Hog1 signaling. Furthermore, Hog1 was not phosphorylated by the addition of MF, but, notably, this echinocandin caused Mkc1 phosphorylation. Our results strongly suggest that the toxic effect of MF on C. albicans cells is not mediated by the Hog1 MAPK and is independent of the generation of an internal oxidative stress in C. albicans.

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Igbalajobi, Olumuyiwa, Jia Gao, and Reinhard Fischer. "The HOG Pathway Plays Different Roles in Conidia and Hyphae During Virulence of Alternaria alternata." Molecular Plant-Microbe Interactions® 33, no. 12 (December 2020): 1405–10. http://dx.doi.org/10.1094/mpmi-06-20-0165-r.

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The black mold Alternaria alternata causes dramatic losses in agriculture due to postharvest colonization and mycotoxin formation and is a weak pathogen on living plants. Fungal signaling processes are crucial for successful colonization of a host plant. Because the mitogen-activated protein kinase HogA is important for the expression of stress-associated genes, we tested a ∆hogA-deletion strain for pathogenicity. When conidia were used as inoculum, the ∆hogA-deletion strain was largely impaired in colonizing tomato and apple. In comparison, hyphae as inoculum colonized the fruit very well. Hence, HogA appears to be important only in the initial stages of plant colonization. A similar difference between conidial inoculum and hyphal inoculum was observed on artificial medium in the presence of different stress agents. Whereas wild-type conidia adapted well to different stresses, the ∆hogA-deletion strain failed to grow under the same conditions. With hyphae as inoculum, the wild type and the ∆hogA-deletion strain grew in a very similar way. At the molecular level, we observed upregulation of several catalase (catA, -B, and -D) and superoxide dismutase (sodA, -B, and -E) genes in germlings but not in hyphae after exposure to 4 mM hydrogen peroxide. The upregulation required the high osmolarity glycerol (HOG) pathway. In contrast, in mycelia, catD, sodA, sodB, and sodE were upregulated upon stress in the absence of HogA. Several other stress-related genes behaved in a similar way.

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Hogeweg, Lotte, and Richard van Gerrevink. "The acquisition of the Dutch discourse particle wel." Nederlandse Taalkunde 20, no. 2 (September 1, 2015): 187–213. http://dx.doi.org/10.5117/nedtaa2015.2.hoge.

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Hogeterp, A. L. A. "Eschatologisch Schriftgebruik in het Nieuwe Testament in het licht van de rollen van de Dode Zee." NTT Journal for Theology and the Study of Religion 62, no. 2 (May 18, 2008): 140–54. http://dx.doi.org/10.5117/ntt2008.62.140.hoge.

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This article reviews eschatological interpretations of Isaiah, Psalms, and Daniel in the New Testament in light of the Dead Sea Scrolls. Q 7:18-23 and 4Q521 attest to a horizon of expectation that an anointed messenger (Isa. 61:1) and divine miracles (e.g. Isa. 26:19) confirm hope in the Lord ‐ hope that the Jesus-movement identified with Jesus as Lord. The Davidic messianism that exegesis of Ps. 110:1 in Mrk. 12:35-37a par. counters is partly informed by accents of Davidic messianism in 11QPsa. Mark 13:26-27 par., that alludes to Dan. 7:13-14, shares with 4QpsDana ar 24 2 the motif of the gathering of the elect.

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Hogervorst, Susan, and Kees Ribbens. "Tijdschrift voor Geschiedenis gedigitaliseerd, 1886-2008." Tijdschrift voor geschiedenis 131, no. 2 (June 1, 2018): 309–25. http://dx.doi.org/10.5117/tvgesch2018.2.hoge.

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Hogervorst, Susan. "Discussiedossier Inleiding: oral history en geschiedenisonderwijs." Tijdschrift voor geschiedenis 131, no. 4 (December 1, 2018): 631–35. http://dx.doi.org/10.5117/tvgesch2018.4.004.hoge.

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Hogervorst, Susan. "‘Echte oorlogsgeschiedenis’." Tijdschrift voor geschiedenis 131, no. 4 (December 1, 2018): 647–51. http://dx.doi.org/10.5117/tvgesch2018.4.007.hoge.

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Hogervorst, Susan, and Kees Ribbens. "Herdenken is nadenken in de nieuwe vaste tentoonstelling in Nationaal Monument Kamp Vught : 32.000 verhalen en zeven seizoenen." Tijdschrift voor geschiedenis 133, no. 1 (June 1, 2020): 105–11. http://dx.doi.org/10.5117/tvgesch2020.1.007.hoge.

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Hogervorst, Susan. "Schriftelijke geschiedenis? Een vrijmoedig pleidooi voor het structureel werken met mondelinge bronnen." Tijdschrift voor Geschiedenis 134, no. 2 (August 1, 2021): 185–86. http://dx.doi.org/10.5117/tvg2021.2.001.hoge.

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Lee, Jongmin, and David E. Levin. "Methylated metabolite of arsenite blocks glycerol production in yeast by inhibition of glycerol-3-phosphate dehydrogenase." Molecular Biology of the Cell 30, no. 17 (August 2019): 2134–40. http://dx.doi.org/10.1091/mbc.e19-04-0228.

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The yeast high-osmolarity glycerol (HOG) stress-activated protein kinase Hog1 is activated in response to hyperosmotic stress, inducing the production and retention of glycerol to restore osmotic balance. Hog1 promotes retention of glycerol through closure of the plasma-membrane glycerol channel Fps1. Treatment of yeast with the toxic trivalent metalloid arsenite (As(III)) also activates Hog1 as part of a protective response in which Hog1 closes Fps1, the main entry port for As(III). In this study, we investigated how cells treated with As(III) avoid creating a new stress caused by the accumulation of glycerol in the absence of hyperosmotic stress conditions. We found that As(III) treatment did not induce glycerol accumulation and, in fact, blocked the accumulation of glycerol induced by constitutive Hog1 activity. We demonstrated that As(III) blocks glycerol production indirectly after its metabolic activation to methylarsenite (MAs(III)), which is a potent inhibitor of glycerol-3-phosphate dehydrogenase. Finally, we used a biotinylated arsenic probe to establish that Cys306 of yeast Gpd1, a highly conserved residue within the active site, is the key target of MAs(III). Conservative mutations at this residue greatly diminished Gpd1 activity. This study offers insight into mechanisms by which SAPK outputs are tailored to specific stressors.

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García-Rodriguez, L. J., A. Durán, and C. Roncero. "Calcofluor Antifungal Action Depends on Chitin and a Functional High-Osmolarity Glycerol Response (HOG) Pathway: Evidence for a Physiological Role of the Saccharomyces cerevisiae HOG Pathway under Noninducing Conditions." Journal of Bacteriology 182, no. 9 (May 1, 2000): 2428–37. http://dx.doi.org/10.1128/jb.182.9.2428-2437.2000.

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ABSTRACT We have isolated several Saccharomyces cerevisiaemutants resistant to calcofluor that contain mutations in thePBS2 or HOG1 genes, which encode the mitogen-activated protein kinase (MAPK) and MAP kinases, respectively, of the high-osmolarity glycerol response (HOG) pathway. We report that blockage of either of the two activation branches of the pathway, namely, SHO1 and SLN1, leads to partial resistance to calcofluor, while simultaneous disruption significantly increases resistance. However, chitin biosynthesis is independent of the HOG pathway. Calcofluor treatment also induces an increase in salt tolerance and glycerol accumulation, although no activation of the HOG pathway is detected. Our results indicate that the antifungal effect of calcofluor depends on its binding to cell wall chitin but also on the presence of a functional HOG pathway. Characterization of one of the mutants isolated, pbs2-14, revealed that resistance to calcofluor and HOG-dependent osmoadaptation are two different physiological processes. Sensitivity to calcofluor depends on the constitutive functionality of the HOG pathway; when this is altered, the cells become calcofluor resistant but also show very low levels of basal salt tolerance. Characterization of some multicopy suppressors of the calcofluor resistance phenotype indicated that constitutive HOG functionality participates in the maintenance of cell wall architecture, a conclusion supported by the antagonism observed between the protein kinase and HOG signal transduction pathways.

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BUTLER, KELLY M., and RICHARD FRANK. "Pentachlorophenol Residues in Porcine Tissue Following Preslaughter Exposure to Treated Wood Shavings." Journal of Food Protection 54, no. 6 (June 1, 1991): 448–50. http://dx.doi.org/10.4315/0362-028x-54.6.448.

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Sixty market hogs originating from one producer and finished in a concrete and steel facility were divided into two groups of 30 and housed for approximately 60 h on either straw (control group) or pentachlorophenol (PCP) treated wood shavings (test group). Feed, straw, and shavings were analyzed for PCP residues. Both feed and straw yielded nondetectable levels of PCP residues, while shavings ranged from 0.03 to 12.0 ppm. The hogs were shipped to slaughter without bedding, and liver, fat and muscle (muscle from the test group only) samples were collected postmortem. The mean level of PCP residue in control (straw) hog livers was 0.037 ppm, while that of livers of hogs bedded with contaminated shavings was 0.342 ppm, a highly significant difference. The t-value using Welch's approximation equalled 9.77 using 28.5 degrees of freedom, indicating the mean PCP residue level was higher for the treated than the control group at a 0.01% level of significance.

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Román, Elvira, Fabien Cottier, Joachim F. Ernst, and Jesús Pla. "Msb2 Signaling Mucin Controls Activation of Cek1 Mitogen-Activated Protein Kinase in Candida albicans." Eukaryotic Cell 8, no. 8 (June 19, 2009): 1235–49. http://dx.doi.org/10.1128/ec.00081-09.

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ABSTRACT We have characterized the role that the Msb2 protein plays in the fungal pathogen Candida albicans by the use of mutants defective in the putative upstream components of the HOG pathway. Msb2, in cooperation with Sho1, controls the activation of the Cek1 mitogen-activated protein kinase under conditions that damage the cell wall, thus defining Msb2 as a signaling element of this pathway in the fungus. msb2 mutants display altered sensitivity to Congo red, caspofungin, zymolyase, or tunicamycin, indicating that this protein is involved in cell wall biogenesis. Msb2 (as well as Sho1 and Hst7) is involved in the transmission of the signal toward Cek1 mediated by the Cdc42 GTPase, as revealed by the use of activated alleles (Cdc42G12V) of this protein. msb2 mutants have a stronger defective invasion phenotype than sho1 mutants when tested on certain solid media that use mannitol or sucrose as a carbon source or under hypoxia. Interestingly, Msb2 contributes to growth under conditions of high osmolarity when both branches of the HOG pathway are altered, as triple ssk1 msb2 sho1 mutants (but not any single or double mutant) are osmosensitive. However, this phenomenon is independent of the presence of Hog1, as Hog1 phosphorylation, Hog1 translocation to the nucleus, and glycerol accumulation are not affected in this mutant following an osmotic shock. These results reveal essential functions in morphogenesis, invasion, cell wall biogenesis, and growth under conditions of high osmolarity for Msb2 in C. albicans and suggest the divergence and specialization of this signaling pathway in filamentous fungi.

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Eisman, B., R. Alonso-Monge, E. Román, D. Arana, C. Nombela, and J. Pla. "The Cek1 and Hog1 Mitogen-Activated Protein Kinases Play Complementary Roles in Cell Wall Biogenesis and Chlamydospore Formation in the Fungal Pathogen Candida albicans." Eukaryotic Cell 5, no. 2 (February 2006): 347–58. http://dx.doi.org/10.1128/ec.5.2.347-358.2006.

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ABSTRACT The Hog1 mitogen-activated protein (MAP) kinase mediates an adaptive response to both osmotic and oxidative stress in the fungal pathogen Candida albicans. This protein also participates in two distinct morphogenetic processes, namely the yeast-to-hypha transition (as a repressor) and chlamydospore formation (as an inducer). We show here that repression of filamentous growth occurs both under serum limitation and under other partially inducing conditions, such as low temperature, low pH, or nitrogen starvation. To understand the relationship of the HOG pathway to other MAP kinase cascades that also play a role in morphological transitions, we have constructed and characterized a set of double mutants in which we deleted both the HOG1 gene and other signaling elements (the CST20, CLA4, and HST7 kinases, the CPH1 and EFG1 transcription factors, and the CPP1 protein phosphatase). We also show that Hog1 prevents the yeast-to-hypha switch independent of all the elements analyzed and that the inability of the hog1 mutants to form chlamydospores is suppressed when additional elements of the CEK1 pathway (CST20 or HST7) are altered. Finally, we report that Hog1 represses the activation of the Cek1 MAP kinase under basal conditions and that Cek1 activation correlates with resistance to certain cell wall inhibitors (such as Congo red), demonstrating a role for this pathway in cell wall biogenesis.

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Rafkind, Jon, and Matthew Flatt. "Honu." ACM SIGPLAN Notices 48, no. 3 (April 10, 2013): 122–31. http://dx.doi.org/10.1145/2480361.2371420.

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O'Rourke, Sean M., and Ira Herskowitz. "A Third Osmosensing Branch in Saccharomyces cerevisiae Requires the Msb2 Protein and Functions in Parallel with the Sho1 Branch." Molecular and Cellular Biology 22, no. 13 (July 1, 2002): 4739–49. http://dx.doi.org/10.1128/mcb.22.13.4739-4749.2002.

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ABSTRACT Two Saccharomyces cerevisiae plasma membrane-spanning proteins, Sho1 and Sln1, function during increased osmolarity to activate a mitogen-activated protein (MAP) kinase cascade. One of these proteins, Sho1, utilizes the MAP kinase kinase kinase Ste11 to activate Pbs2. We previously used the FUS1 gene of the pheromone response pathway as a reporter to monitor cross talk in hog1 mutants. Cross talk requires the Sho1-Ste11 branch of the HOG pathway, but some residual signaling, which is STE11 dependent, still occurs in the absence of Sho1. These observations led us to propose the existence of another osmosensor upstream of Ste11. To identify such an osmosensor, we screened for mutants in which the residual signaling in a hog1 sho1 mutant was further reduced. We identified the MSB2 gene, which encodes a protein with a single membrane-spanning domain and a large presumptive extracellular domain. Assay of the FUS1-lacZ reporter (in a hog1 mutant background) showed that sho1 and msb2 mutations both reduced the expression of the reporter partially and that the hog1 sho1 msb2 mutant was severely defective in the expression of the reporter. The use of DNA microarrays to monitor gene expression revealed that Sho1 and Msb2 regulate identical gene sets in hog1 mutants. A role for MSB2 in HOG1 strains was also seen in strains defective in the two known branches that activate Pbs2: an ssk1 sho1 msb2 strain was more osmosensitive than an ssk1 sho1 MSB2 strain. These observations indicate that Msb2 is partially redundant with the Sho1 osmosensing branch for the activation of Ste11.

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Hernández-Elvira, Mariana, Ricardo Martínez-Gómez, Eunice Domínguez-Martin, Akram Méndez, Laura Kawasaki, Laura Ongay-Larios, and Roberto Coria. "Tunicamycin Sensitivity-Suppression by High Gene Dosage Reveals New Functions of the Yeast Hog1 MAP Kinase." Cells 8, no. 7 (July 12, 2019): 710. http://dx.doi.org/10.3390/cells8070710.

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In the yeast Saccharomyces cerevisiae, components of the High Osmolarity Glycerol (HOG) pathway are important for the response to diverse stresses including response to endoplasmic reticulum stress (ER stress), which is produced by the accumulation of unfolded proteins in the lumen of this organelle. Accumulation of unfolded proteins may be due to the inhibition of protein N-glycosylation, which can be achieved by treatment with the antibiotic tunicamycin (Tn). In this work we were interested in finding proteins involved in the ER stress response regulated by Hog1, the mitogen activated protein kinase (MAPK) of the HOG pathway. A high gene dosage suppression screening allowed us to identify genes that suppressed the sensitivity to Tn shown by a hog1Δ mutant. The suppressors participate in a limited number of cellular processes, including lipid/carbohydrate biosynthesis and protein glycosylation, vesicle-mediated transport and exocytosis, cell wall organization and biogenesis, and cell detoxification processes. The finding of suppressors Rer2 and Srt1, which participate in the dolichol biosynthesis pathway revealed that the hog1Δ strain has a defective polyprenol metabolism. This work uncovers new genetic and functional interactors of Hog1 and contributes to a better understanding of the participation of this MAPK in the ER stress response.

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Journal articles on the topic 'Hogu'

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