Journal articles: 'Far1'

1

Kemp, Hilary A., and George F. Sprague,. "Far3 and Five Interacting Proteins Prevent Premature Recovery from Pheromone Arrest in the Budding Yeast Saccharomyces cerevisiae." Molecular and Cellular Biology 23, no. 5 (March 1, 2003): 1750–63. http://dx.doi.org/10.1128/mcb.23.5.1750-1763.2003.

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ABSTRACT In budding yeast, diffusible mating pheromones initiate a signaling pathway that culminates in several responses, including cell cycle arrest. Only a handful of genes required for the interface between pheromone response and the cell cycle have been identified, among them FAR1 and FAR3; of these, only FAR1 has been extensively characterized. In an effort to learn about the mechanism by which Far3 acts, we used the two-hybrid method to identify interacting proteins. We identified five previously uncharacterized open reading frames, dubbed FAR7, FAR8, FAR9, FAR10, and FAR11, that cause a far3-like pheromone arrest defect when disrupted. Using two-hybrid and coimmunoprecipitation analysis, we found that all six Far proteins interact with each other. Moreover, velocity sedimentation experiments suggest that Far3 and Far7 to Far11 form a complex. The phenotype of a sextuple far3far7-far11 mutant is no more severe than any single mutant. Thus, FAR3 and FAR7 to FAR11 all participate in the same pathway leading to G1 arrest. These mutants initially arrest in response to pheromone but resume budding after 10 h. Under these conditions, wild-type cells fail to resume budding even after several days whereas far1 mutant cells resume budding within 1 h. We conclude that the FAR3-dependent arrest pathway is functionally distinct from that which employs FAR1.

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Alberghina, Lilia, Riccardo L. Rossi, Lorenzo Querin, Valeria Wanke, and Marco Vanoni. "A cell sizer network involving Cln3 and Far1 controls entrance into S phase in the mitotic cycle of budding yeast." Journal of Cell Biology 167, no. 3 (November 1, 2004): 433–43. http://dx.doi.org/10.1083/jcb.200405102.

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Saccharomyces cerevisiae must reach a carbon source-modulated critical cell size, protein content per cell at the onset of DNA replication (Ps), in order to enter S phase. Cells grown in glucose are larger than cells grown in ethanol. Here, we show that an increased level of the cyclin-dependent inhibitor Far1 increases cell size, whereas far1Δ cells start bud emergence and DNA replication at a smaller size than wild type. Cln3Δ, far1Δ, and strains overexpressing Far1 do not delay budding during an ethanol glucose shift-up as wild type does. Together, these findings indicate that Cln3 has to overcome Far1 to trigger Cln–Cdc28 activation, which then turns on SBF- and MBF-dependent transcription. We show that a second threshold is required together with the Cln3/Far1 threshold for carbon source modulation of Ps. A new molecular network accounting for the setting of Ps is proposed.

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McKinney, J. D., and F. R. Cross. "FAR1 and the G1 phase specificity of cell cycle arrest by mating factor in Saccharomyces cerevisiae." Molecular and Cellular Biology 15, no. 5 (May 1995): 2509–16. http://dx.doi.org/10.1128/mcb.15.5.2509.

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Significant accumulation of Far1p is restricted to the G1 phase of the Saccharomyces cerevisiae cell cycle. Here we demonstrate yeast cell cycle regulation of Far1p proteolysis. Deletions within the 50 N-terminal amino acids of Far1p increase stability and reduce cell cycle regulation of Far1p abundance. Whereas wild-type Far1p specifically and exclusively promotes G1 phase arrest in response to mating factor, stabilized Far1p promoted arrest both during and after G1. The loss of the G1 specificity of Far1p action requires elimination of FAR1 transcriptional regulation (by means of the GAL1 promoter) as well as N-terminal truncation. Thus, the cell cycle specificity of mating factor arrest may be largely due to cell cycle regulation of FAR1 transcription and protein stability.

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Wang, Jinwu, Xingyu Wang, Linzhen Xie, Wenhao Zheng, Hua Chen, and Leyi Cai. "Comparison of radiographs and CT features between posterior Pilon fracture and posterior malleolus fracture: a retrospective cohort study." British Journal of Radiology 93, no. 1110 (June 2020): 20191030. http://dx.doi.org/10.1259/bjr.20191030.

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Objectives: This study explored the morphological differences between posterior Pilon fracture and posterior malleolus fracture from radiographs and CT to provide detail for diagnosis and treatment of them. Methods: Radiographs and CT imaging data of 174 patients with distal posterior tibial fractures who were treated from January 2013 to January 2019 were retrospectively analyzed. Based on the operation and imaging examination, the fractures were classified into posterior Pilon fractures and posterior malleolus fractures. Radiographic parameters including the width, height, depth, α angle, β angle, γ angle, fragment area ratio 1 (FAR1), δ angle and fragment area ratio 2 (FAR2) of ankle mortise were measured. Results: There were 96 posterior Pilon fractures (Type I: 30, Type II: 22 and Type III: 44) and 78 posterior malleolus fractures (Type I: 40 and Type II: 38). The ankle depth, α angle, γ angle, FAR1 and FAR2 of posterior Pilon fractures were larger than these of posterior malleolus fractures (p < 0.05). In addition, FAR1 and FAR2 of Type II and Type III posterior Pilon fractures were significantly larger than these of Type I (p < 0.05). FAR1 and FAR2 of Type I posterior malleolus fractures were significantly smaller than these of Type II (p < 0.05). Conclusion: Radiographs combined with CT analysis is an effective method to accurately distinguish morphological features between posterior Pilon fracture and posterior malleolus fracture. Advances in knowledge: Radiographs combined with CT distinguished the fracture of posterior malleolus and posterior Pilon rapidly and accurately, instead of operation.

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Gartner, Anton, Alexandra Jovanović, Doo-Il Jeoung, Sarah Bourlat, Frederick R. Cross, and Gustav Ammerer. "Pheromone-Dependent G1 Cell Cycle Arrest Requires Far1 Phosphorylation, but May Not Involve Inhibition of Cdc28-Cln2 Kinase, In Vivo." Molecular and Cellular Biology 18, no. 7 (July 1, 1998): 3681–91. http://dx.doi.org/10.1128/mcb.18.7.3681.

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ABSTRACT In yeast, the pheromone α-factor acts as an antiproliferative factor that induces G1 arrest and cellular differentiation. Previous data have indicated that Far1, a factor dedicated to pheromone-induced cell cycle arrest, is under positive and negative posttranslational regulation. Phosphorylation by the pheromone-stimulated mitogen-activated protein (MAP) kinase Fus3 has been thought to enhance the binding of Far1 to G1-specific cyclin-dependent kinase (Cdk) complexes, thereby inhibiting their catalytic activity. Cdk-dependent phosphorylation events were invoked to account for the high instability of Far1 outside early G1 phase. To confirm any functional role of Far1 phosphorylation, we undertook a systematic mutational analysis of potential MAP kinase and Cdk recognition motifs. Two putative phosphorylation sites that strongly affect Far1 behavior were identified. A change of serine 87 to alanine prevents the cell cycle-dependent degradation of Far1, causing enhanced sensitivity to pheromone. In contrast, threonine 306 seems to be an important recipient of an activating modification, as substitutions at this position abolish the G1 arrest function of Far1. Only the phosphorylated wild-type Far1 protein, not the T306-to-A substitution product, can be found in stable association with the Cdc28-Cln2 complex. Surprisingly, Far1-associated Cdc28-Cln2 complexes are at best moderately inhibited in immunoprecipitation kinase assays, suggesting unconventional inhibitory mechanisms of Far1.

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Liu, Zhengjun, Chuanjing An, Yiqing Zhao, Yao Xiao, Lu Bao, Chunmei Gong, and Yuefang Gao. "Genome-Wide Identification and Characterization of the CsFHY3/FAR1 Gene Family and Expression Analysis under Biotic and Abiotic Stresses in Tea Plants (Camellia sinensis)." Plants 10, no. 3 (March 17, 2021): 570. http://dx.doi.org/10.3390/plants10030570.

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The FHY3/FAR1 transcription factor family, derived from transposases, plays important roles in light signal transduction, and in the growth and development of plants. However, the homologous genes in tea plants have not been studied. In this study, 25 CsFHY3/FAR1 genes were identified in the tea plant genome through a genome-wide study, and were classified into five subgroups based on their phylogenic relationships. Their potential regulatory roles in light signal transduction and photomorphogenesis, plant growth and development, and hormone responses were verified by the existence of the corresponding cis-acting elements. The transcriptome data showed that these genes could respond to salt stress and shading treatment. An expression analysis revealed that, in different tissues, especially in leaves, CsFHY3/FAR1s were strongly expressed, and most of these genes were positively expressed under salt stress (NaCl), and negatively expressed under low temperature (4 °C) stress. In addition, a potential interaction network demonstrated that PHYA, PHYC, PHYE, LHY, FHL, HY5, and other FRSs were directly or indirectly associated with CsFHY3/FAR1 members. These results will provide the foundation for functional studies of the CsFHY3/FAR1 family, and will contribute to the breeding of tea varieties with high light efficiency and strong stress resistance.

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7

Chang, F., and I. Herskowitz. "Phosphorylation of FAR1 in response to alpha-factor: a possible requirement for cell-cycle arrest." Molecular Biology of the Cell 3, no. 4 (April 1992): 445–50. http://dx.doi.org/10.1091/mbc.3.4.445.

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Exposure of yeast a cells to alpha-factor causes cells to arrest in the G1 phase of the cell cycle. The FAR1 gene is required for this cell-cycle arrest; its product is necessary for the inhibition of a G1 cyclin, CLN2. Earlier work demonstrated that alpha-factor caused an increase in the transcription of FAR1 severalfold over a measurable basal level. We now show that transcriptional induction of FAR1 from a heterologous promoter is not sufficient to inhibit CLN2 in the absence of alpha-factor. We also show that FAR1 is phosphorylated in response to alpha-factor and propose that this phosphorylation may be required for FAR1 activity.

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8

Oehlen, L. J., J. D. McKinney, and F. R. Cross. "Ste12 and Mcm1 regulate cell cycle-dependent transcription of FAR1." Molecular and Cellular Biology 16, no. 6 (June 1996): 2830–37. http://dx.doi.org/10.1128/mcb.16.6.2830.

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The transcripts of many genes involved in Saccharomyces cerevisiae mating were found to fluctuate during the cell cycle. In the absence of a functional Ste12 transcription factor, both the levels and the cell cycle pattern of expression of these genes were affected. FUS1 and AGA1 levels, which are maximally expressed only in G1-phase cells, were strongly reduced in ste12- cells. The cell cycle transcription pattern for FAR1 was changed in ste12- cells: the gene was still significantly expressed in G2/M, but transcript levels were strongly reduced in G1 phase, resulting in a lack of Far1 protein accumulation. G2/M transcription of FAR1 was dependent on the transcription factor Mcm1, and expression of a gene with Mcm1 fused to a strong transcriptional activation domain resulted in increased levels of FAR1 transcription. The pattern of cell cycle-regulated transcription of FAR1 could involve combinatorial control of Ste12 and Mcm1. Forced G1 expression of FAR1 from the GAL1 promoter resorted the ability to arrest in response to pheromone in ste12-cells. This indicates that transcription of FAR1 in the G1 phase is essential for accumulation of the protein and for pheromone-induced cell cycle arrest.

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9

Valdivieso, M. H., K. Sugimoto, K. Y. Jahng, P. M. Fernandes, and C. Wittenberg. "FAR1 is required for posttranscriptional regulation of CLN2 gene expression in response to mating pheromone." Molecular and Cellular Biology 13, no. 2 (February 1993): 1013–22. http://dx.doi.org/10.1128/mcb.13.2.1013-1022.1993.

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Yeast cells arrest during the G1 interval of the cell cycle in response to peptide mating pheromones. The FAR1 gene is required for cell cycle arrest but not for a number of other aspects of the pheromone response. Genetic evidence suggests that FAR1 is required specifically for inactivation of the G1 cyclin CLN2. From these observations, the FAR1 gene has been proposed to encode an element of the interface between the mating pheromone signal transduction pathway and the cell cycle regulatory apparatus. We show here that FAR1 is necessary for the decrease in CLN1 and CLN2 transcript accumulation observed in response to mating pheromone but is unnecessary for regulation of the same transcripts during vegetative growth. However, the defect in regulation of CLN1 expression is dependent upon CLN2. We show that pheromone regulates the abundance of Cln2 at a posttranscriptional level and that FAR1 is required for that regulation. From these observations, we suggest that FAR1 function is limited to posttranscriptional regulation of CLN2 expression by mating pheromone. The failure of mating pheromone to repress CLN2 transcript levels in far1 mutants can be explained by the stimulatory effect of the persistent Cln2 protein on CLN2 transcription via the CLN/CDC28-dependent feedback pathway.

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10

Valdivieso, M. H., K. Sugimoto, K. Y. Jahng, P. M. Fernandes, and C. Wittenberg. "FAR1 is required for posttranscriptional regulation of CLN2 gene expression in response to mating pheromone." Molecular and Cellular Biology 13, no. 2 (February 1993): 1013–22. http://dx.doi.org/10.1128/mcb.13.2.1013.

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Yeast cells arrest during the G1 interval of the cell cycle in response to peptide mating pheromones. The FAR1 gene is required for cell cycle arrest but not for a number of other aspects of the pheromone response. Genetic evidence suggests that FAR1 is required specifically for inactivation of the G1 cyclin CLN2. From these observations, the FAR1 gene has been proposed to encode an element of the interface between the mating pheromone signal transduction pathway and the cell cycle regulatory apparatus. We show here that FAR1 is necessary for the decrease in CLN1 and CLN2 transcript accumulation observed in response to mating pheromone but is unnecessary for regulation of the same transcripts during vegetative growth. However, the defect in regulation of CLN1 expression is dependent upon CLN2. We show that pheromone regulates the abundance of Cln2 at a posttranscriptional level and that FAR1 is required for that regulation. From these observations, we suggest that FAR1 function is limited to posttranscriptional regulation of CLN2 expression by mating pheromone. The failure of mating pheromone to repress CLN2 transcript levels in far1 mutants can be explained by the stimulatory effect of the persistent Cln2 protein on CLN2 transcription via the CLN/CDC28-dependent feedback pathway.

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11

Cui, Weiwei, Dong Liu, Wei Gu, and Bo Chu. "Peroxisome-driven ether-linked phospholipids biosynthesis is essential for ferroptosis." Cell Death & Differentiation 28, no. 8 (March 17, 2021): 2536–51. http://dx.doi.org/10.1038/s41418-021-00769-0.

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AbstractIt is well established that ferroptosis is primarily induced by peroxidation of long-chain poly-unsaturated fatty acid (PUFA) through nonenzymatic oxidation by free radicals or enzymatic stimulation of lipoxygenase. Although there is emerging evidence that long-chain saturated fatty acid (SFA) might be implicated in ferroptosis, it remains unclear whether and how SFA participates in the process of ferroptosis. Using endogenous metabolites and genome-wide CRISPR screening, we have identified FAR1 as a critical factor for SFA-mediated ferroptosis. FAR1 catalyzes the reduction of C16 or C18 saturated fatty acid to fatty alcohol, which is required for the synthesis of alkyl-ether lipids and plasmalogens. Inactivation of FAR1 diminishes SFA-dependent ferroptosis. Furthermore, FAR1-mediated ferroptosis is dependent on peroxisome-driven ether phospholipid biosynthesis. Strikingly, TMEM189, a newly identified gene which introduces vinyl-ether double bond into alkyl-ether lipids to generate plasmalogens abrogates FAR1-alkyl-ether lipids axis induced ferroptosis. Our study reveals a new FAR1-ether lipids-TMEM189 axis dependent ferroptosis pathway and suggests TMEM189 as a promising druggable target for anticancer therapy.

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Pope, Patricia A., and Peter M. Pryciak. "Functional overlap among distinct G1/S inhibitory pathways allows robust G1 arrest by yeast mating pheromones." Molecular Biology of the Cell 24, no. 23 (December 2013): 3675–88. http://dx.doi.org/10.1091/mbc.e13-07-0373.

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In budding yeast, mating pheromones arrest the cell cycle in G1 phase via a pheromone-activated Cdk-inhibitor (CKI) protein, Far1. Alternate pathways must also exist, however, because deleting the cyclin CLN2 restores pheromone arrest to far1∆ cells. Here we probe whether these alternate pathways require the G1/S transcriptional repressors Whi5 and Stb1 or the CKI protein Sic1, whose metazoan analogues (Rb or p27) antagonize cell cycle entry. Removing Whi5 and Stb1 allows partial escape from G1 arrest in far1∆ cln2∆ cells, along with partial derepression of G1/S genes, which implies a repressor-independent route for inhibiting G1/S transcription. This route likely involves pheromone-induced degradation of Tec1, a transcriptional activator of the cyclin CLN1, because Tec1 stabilization also causes partial G1 escape in far1∆ cln2∆ cells, and this is additive with Whi5/Stb1 removal. Deleting SIC1 alone strongly disrupts Far1-independent G1 arrest, revealing that inhibition of B-type cyclin-Cdk activity can empower weak arrest pathways. Of interest, although far1∆ cln2∆ sic1∆ cells escaped G1 arrest, they lost viability during pheromone exposure, indicating that G1 exit is deleterious if the arrest signal remains active. Overall our findings illustrate how multiple distinct G1/S-braking mechanisms help to prevent premature cell cycle commitment and ensure a robust signal-induced G1 arrest.

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Marsh, Kayleigh G., Adrian Arrieta, Donna J. Thuerauf, Erik A. Blackwood, Lauren MacDonnell, and Christopher C. Glembotski. "The peroxisomal enzyme, FAR1, is induced during ER stress in an ATF6-dependent manner in cardiac myocytes." American Journal of Physiology-Heart and Circulatory Physiology 320, no. 5 (May 1, 2021): H1813—H1821. http://dx.doi.org/10.1152/ajpheart.00999.2020.

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14

Valtz, N., M. Peter, and I. Herskowitz. "FAR1 is required for oriented polarization of yeast cells in response to mating pheromones." Journal of Cell Biology 131, no. 4 (November 15, 1995): 863–73. http://dx.doi.org/10.1083/jcb.131.4.863.

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Cell polarization involves specifying an area on the cell surface and organizing the cytoskeleton towards that landmark. The mechanisms by which external signals are translated into internal landmarks for polarization are poorly understood. The yeast Saccharomyces cerevisiae exhibits polarized growth during mating: the actin cytoskeleton of each cell polarizes towards its partner, presumably to allow efficient cell fusion. The external signal which determines the landmark for polarization is thought to be a gradient of peptide pheromone released by the mating partner. Here we described mutants that exhibit random polarization. Using two assays, including a direct microscope assay for orientation (Segall, J. 1993. Proc. Natl. Acad. Sci. USA. 90:8332-8337), we show that these mutants cannot locate the source of a pheromone gradient although they are able to organize their cytoskeleton. These mutants appear to be defective in mating because they are unable to locate the mating partner. They carry mutations of the FAR1 gene, denoted far1-s, and identify a new function for the Far1 protein. Its other known function is to promote cell cycle arrest during mating by inhibiting a cyclin-dependent kinase (Peter, M., and I. Herskowitz. 1994. Science (Wash. DC). 265:1228-1232). The far1-s mutants exhibit normal cell cycle arrest in response to pheromone, which suggests that Far1 protein plays two distinct roles in mating: one in cell cycle arrest and the other in orientation towards the mating partner.

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15

Zhang, Donghong, and Paul A. Lefebvre. "FAR1, a Negative Regulatory Locus Required for the Repression of the Nitrate Reductase Gene in Chlamydomonas reinhardtii." Genetics 146, no. 1 (May 1, 1997): 121–33. http://dx.doi.org/10.1093/genetics/146.1.121.

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In Chlamydomonas reinhardtii, the genes required for nitrate assimilation, including the gene encoding nitrate reductase (NIT1), are subject to repression by ammonia. To study the mechanism of ammonia repression, we employed two approaches to search for mutants with defective repression of NIT1 gene expression. (1) PF14, a gene required for flagellar function, was used as a reporter gene for expression from the NIT1 promoter. When introduced into a pf14 mutant host, the NZTl:PF14 chimeric construct produced a transformant (T10-10B) with a conditional swimming phenotype. Spontaneous mutants with defective ammonia repression of the NIT1 promoter were screened for by isolating cells that gained constitutive motility. (2) Insertional mutagenesis was performed, followed by screening for chlorate sensitivity in the presence of ammonia ion. One insertional mutant and six spontaneous mutants were allelic and defined a new gene, FAR1 (free from ammonia repression). FAR1 was mapped to Linkage Group I, 7.7 cM to the right of the centromere. The far1-1 mutant strain was used to clone DNA adjacent to the site of plasmid insertion, which was then used as a hybridization probe to clone the FAR1 gene from wild type.

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Elion, E. A., B. Satterberg, and J. E. Kranz. "FUS3 phosphorylates multiple components of the mating signal transduction cascade: evidence for STE12 and FAR1." Molecular Biology of the Cell 4, no. 5 (May 1993): 495–510. http://dx.doi.org/10.1091/mbc.4.5.495.

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The mitogen-activated protein (MAP) kinase homologue FUS3 mediates both transcription and G1 arrest in a pheromone-induced signal transduction cascade in Saccharomyces cerevisiae. We report an in vitro kinase assay for FUS3 and its use in identifying candidate substrates. The assay requires catalytically active FUS3 and pheromone induction. STE7, a MAP kinase kinase homologue, is needed for maximal activity. At least seven proteins that specifically associate with FUS3 are phosphorylated in the assay. Many of these substrates are physiologically relevant and are affected by in vivo levels of numerous signal transduction components. One substrate is likely to be the transcription factor STE12. A second is likely to be FAR1, a protein required for G1 arrest. FAR1 was isolated as a multicopy suppressor of a nonarresting fus3 mutant and interacts with FUS3 in a two hybrid system. Consistent with this FAR1 is a good substrate in vitro and generates a FUS3-associated substrate of expected size. These data support a model in which FUS3 mediates transcription and G1 arrest by direct activation of STE12 and FAR1 and phosphorylates many other proteins involved in the response to pheromone.

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17

Horecka, Joe, and George F. Sprague. "Identification and Characterization of FAR3, a Gene Required for Pheromone-Mediated G1 Arrest in Saccharomyces cerevisiae." Genetics 144, no. 3 (November 1, 1996): 905–21. http://dx.doi.org/10.1093/genetics/144.3.905.

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Abstract In haploid Saccharomyces cerevisiae cells, mating pheromones activate a signal transduction pathway that leads to cell cycle arrest in the G1 phase and to transcription induction of genes that promote conjugation. To identify genes that link the signal transduction pathway and the cell cycle machinery, we developed a selection strategy to isolate yeast mutants specifically defective for G1 arrest. Several of these mutants identified previously known genes, including CLN3, FUS3, and FAR1. In addition, a new gene, FAR3, was identified and characterized. FAR3 encodes a novel protein of 204 amino acid residues that is dispensable for viability. Northern blot experiments indicated that FAR3 expression is constitutive with respect to cell type, pheromone treatment, and cell cycle position. As a first step toward elucidating the mechanism by which Far3 promotes pheromone-mediated G1 arrest, we performed genetic and molecular experiments to test the possibility that Far3 participates in one of the heretofore characterized mechanisms, namely Fus3/Farl-mediated inhibition of Cdc28-Cln kinase activity, G1 cyclin gene repression, and G1, cyclin protein turnover. Our data indicate that Far3 effects G1 arrest by a mechanism distinct from those previously known.

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Domergue, Frédéric, Sollapura J. Vishwanath, Jérôme Joubès, Jasmine Ono, Jennifer A. Lee, Matthieu Bourdon, Reem Alhattab, et al. "Three Arabidopsis Fatty Acyl-Coenzyme A Reductases, FAR1, FAR4, and FAR5, Generate Primary Fatty Alcohols Associated with Suberin Deposition." Plant Physiology 153, no. 4 (June 22, 2010): 1539–54. http://dx.doi.org/10.1104/pp.110.158238.

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Pracheil, Tammy, and Zhengchang Liu. "Tiered Assembly of the Yeast Far3-7-8-9-10-11 Complex at the Endoplasmic Reticulum." Journal of Biological Chemistry 288, no. 23 (April 26, 2013): 16986–97. http://dx.doi.org/10.1074/jbc.m113.451674.

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Target of rapamycin signaling is a conserved, essential pathway integrating nutritional cues with cell growth and proliferation. The target of rapamycin kinase exists in two distinct complexes, TORC1 and TORC2. It has been reported that protein phosphatase 2A (PP2A) and the Far3-7-8-9-10-11 complex (Far complex) negatively regulate TORC2 signaling in yeast. The Far complex, originally identified as factors required for pheromone-induced cell cycle arrest, and PP2A form the yeast counterpart of the STRIPAK complex, which was first isolated in mammals. The cellular localization of the Far complex has yet to be fully characterized. Here, we show that the Far complex localizes to the endoplasmic reticulum (ER) by analyzing functional GFP-tagged Far proteins in vivo. We found that Far9 and Far10, two homologous proteins each with a tail-anchor domain, localize to the ER in mutant cells lacking the other Far complex components. Far3, Far7, and Far8 form a subcomplex, which is recruited to the ER by Far9/10. The Far3-7-8- complex in turn recruits Far11 to the ER. Finally, we show that the tail-anchor domain of Far9 is required for its optimal function in TORC2 signaling. Our study reveals tiered assembly of the yeast Far complex at the ER and a function for Far complex's ER localization in TORC2 signaling.

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Jeoung, Doo-Il, L. J. W. M. Oehlen, and Frederick R. Cross. "Cln3-Associated Kinase Activity inSaccharomyces cerevisiae Is Regulated by the Mating Factor Pathway." Molecular and Cellular Biology 18, no. 1 (January 1, 1998): 433–41. http://dx.doi.org/10.1128/mcb.18.1.433.

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ABSTRACT The Saccharomyces cerevisiae cell cycle is arrested in G1 phase by the mating factor pathway. Genetic evidence has suggested that the G1 cyclins Cln1, Cln2, and Cln3 are targets of this pathway whose inhibition results in G1 arrest. Inhibition of Cln1- and Cln2-associated kinase activity by the mating factor pathway acting through Far1 has been described. Here we report that Cln3-associated kinase activity is inhibited by mating factor treatment, with dose response and timing consistent with involvement in cell cycle arrest. No regulation of Cln3-associated kinase was observed in a fus3 kss1 strain deficient in mating factor pathway mitogen-activated protein (MAP) kinases. Inhibition occurs mainly at the level of specific activity of Cln3-Cdc28 complexes. Inhibition of the C-terminally truncated Cln3-1-associated kinase is not observed; such truncations were previously identified genetically as causing resistance to mating factor-induced cell cycle arrest. Regulation of Cln3-associated kinase specific activity by mating factor treatment requires Far1. Overexpression of Far1 restores inhibition of C-terminally truncated Cln3-1-associated kinase activity. G2/M-arrested cells are unable to regulate Cln3-associated kinase, possibly because of cell cycle regulation of Far1 abundance. Inhibition of Cln3-associated kinase activity by the mating factor pathway may allow this pathway to block the earliest step in normal cell cycle initiation, since Cln3 functions as the most upstream G1-acting cyclin, activating transcription of the G1 cyclins CLN1 and CLN2 as well as of the S-phase cyclins CLB5 and CLB6.

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Young Chae, Geun, Woo-Jong Hong, Min Jeong Jang, Ki-Hong Jung, and Seungill Kim. "Recurrent mutations promote widespread structural and functional divergence of MULE-derived genes in plants." Nucleic Acids Research 49, no. 20 (November 2, 2021): 11765–77. http://dx.doi.org/10.1093/nar/gkab932.

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Abstract Transposable element (TE)-derived genes are increasingly recognized as major sources conferring essential traits in agriculturally important crops but underlying evolutionary mechanisms remain obscure. We updated previous annotations and constructed 18,744 FAR-RED IMPAIRED RESPONSE1 (FAR1) genes, a transcription factor family derived from Mutator-like elements (MULEs), from 80 plant species, including 15,546 genes omitted in previous annotations. In-depth sequence comparison of the updated gene repertoire revealed that FAR1 genes underwent continuous structural divergence via frameshift and nonsense mutations that caused premature translation termination or specific domain truncations. CRISPR/Cas9-based genome editing and transcriptome analysis determined a novel gene involved in fertility-regulating transcription of rice pollen, denoting the functional capacity of our re-annotated gene models especially in monocots which had the highest copy numbers. Genomic evidence showed that the functional gene adapted by obtaining a shortened form through a frameshift mutation caused by a tandem duplication of a 79-bp sequence resulting in premature translation termination. Our findings provide improved resources for comprehensive studies of FAR1 genes with beneficial agricultural traits and unveil novel evolutionary mechanisms generating structural divergence and subsequent adaptation of TE-derived genes in plants.

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Honsho, Masanori, Fabian Dorninger, Yuichi Abe, Daiki Setoyama, Ryohei Ohgi, Takeshi Uchiumi, Dongchon Kang, Johannes Berger, and Yukio Fujiki. "Impaired plasmalogen synthesis dysregulates liver X receptor-dependent transcription in cerebellum." Journal of Biochemistry 166, no. 4 (May 28, 2019): 353–61. http://dx.doi.org/10.1093/jb/mvz043.

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Abstract Synthesis of ethanolamine plasmalogen (PlsEtn) is regulated by modulating the stability of fatty acyl-CoA reductase 1 (Far1) on peroxisomal membrane, a rate-limiting enzyme in plasmalogen synthesis. Dysregulation of plasmalogen homeostasis impairs cholesterol biosynthesis in cultured cells by altering the stability of squalene epoxidase (SQLE). However, regulation of PlsEtn synthesis and physiological consequences of plasmalogen homeostasis in tissues remain unknown. In the present study, we found that the protein but not the transcription level of Far1 in the cerebellum of the Pex14 mutant mouse expressing Pex14p lacking its C-terminal region (Pex14ΔC/ΔC) is higher than that from wild-type mouse, suggesting that Far1 is stabilized by the lowered level of PlsEtn. The protein level of SQLE was increased, whereas the transcriptional activity of the liver X receptors (LXRs), ligand-activated transcription factors of the nuclear receptor superfamily, is lowered in the cerebellum of Pex14ΔC/ΔC and the mice deficient in dihydroxyacetonephosphate acyltransferase, the initial enzyme for the synthesis of PlsEtn. These results suggest that the reduction of plasmalogens in the cerebellum more likely compromises the cholesterol homeostasis, thereby reducing the transcriptional activities of LXRs, master regulators of cholesterol homeostasis.

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Chelimsky, E., D. Cordray, and L. e. Datta. "Federal Evaluation: the Pendulum Has Swung Too Far1." American Journal of Evaluation 10, no. 2 (May 1, 1989): 25–29. http://dx.doi.org/10.1177/109821408901000204.

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Chelimsky, Eleanor, David Cordray, and Lois-ellin Datta. "Federal evaluation: The pendulum has swung too far1." Evaluation Practice 10, no. 2 (May 1989): 25–30. http://dx.doi.org/10.1016/s0886-1633(89)80050-9.

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25

Dorer, R., P. M. Pryciak, and L. H. Hartwell. "Saccharomyces cerevisiae cells execute a default pathway to select a mate in the absence of pheromone gradients." Journal of Cell Biology 131, no. 4 (November 15, 1995): 845–61. http://dx.doi.org/10.1083/jcb.131.4.845.

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During conjugation, haploid S. cerevisiae cells find one another by polarizing their growth toward each other along gradients of pheromone (chemotropism). We demonstrate that yeast cells exhibit a second mating behavior: when their receptors are saturated with pheromone, wild-type a cells execute a default pathway and select a mate at random. These matings are less efficient than chemotropic matings, are induced by the same dose of pheromone that induces shmoo formation, and appear to use a site near the incipient bud site for polarization. We show that the SPA2 gene is specifically required for the default pathway: spa2 delta mutants cannot mate if pheromone concentrations are high and gradients are absent, but can mate if gradients are present. ste2 delta, sst2 delta, and far1 delta mutants are chemotropism-defective and therefore must choose a mate by using a default pathway; consistent with this deduction, these strains require SPA2 to mate. In addition, our results suggest that far1 mutants are chemotropism-defective because their mating polarity is fixed at the incipient bud site, suggesting that the FAR1 gene is required for inhibiting the use of the incipient bud site during chemotropic mating. These observations reveal a molecular relationship between the mating and budding polarity pathways.

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Tyers, M., and B. Futcher. "Far1 and Fus3 link the mating pheromone signal transduction pathway to three G1-phase Cdc28 kinase complexes." Molecular and Cellular Biology 13, no. 9 (September 1993): 5659–69. http://dx.doi.org/10.1128/mcb.13.9.5659-5669.1993.

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In the yeast Saccharomyces cerevisiae, the Cdc28 protein kinase controls commitment to cell division at Start, but no biologically relevant G1-phase substrates have been identified. We have studied the kinase complexes formed between Cdc28 and each of the G1 cyclins Cln1, Cln2, and Cln3. Each complex has a specific array of coprecipitated in vitro substrates. We identify one of these as Far1, a protein required for pheromone-induced arrest at Start. Treatment with alpha-factor induces a preferential association and/or phosphorylation of Far1 by the Cln1, Cln2, and Cln3 kinase complexes. This induced interaction depends upon the Fus3 protein kinase, a mitogen-activated protein kinase homolog that functions near the bottom of the alpha-factor signal transduction pathway. Thus, we trace a path through which a mitogen-activated protein kinase regulates a Cdc2 kinase.

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Tyers, M., and B. Futcher. "Far1 and Fus3 link the mating pheromone signal transduction pathway to three G1-phase Cdc28 kinase complexes." Molecular and Cellular Biology 13, no. 9 (September 1993): 5659–69. http://dx.doi.org/10.1128/mcb.13.9.5659.

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In the yeast Saccharomyces cerevisiae, the Cdc28 protein kinase controls commitment to cell division at Start, but no biologically relevant G1-phase substrates have been identified. We have studied the kinase complexes formed between Cdc28 and each of the G1 cyclins Cln1, Cln2, and Cln3. Each complex has a specific array of coprecipitated in vitro substrates. We identify one of these as Far1, a protein required for pheromone-induced arrest at Start. Treatment with alpha-factor induces a preferential association and/or phosphorylation of Far1 by the Cln1, Cln2, and Cln3 kinase complexes. This induced interaction depends upon the Fus3 protein kinase, a mitogen-activated protein kinase homolog that functions near the bottom of the alpha-factor signal transduction pathway. Thus, we trace a path through which a mitogen-activated protein kinase regulates a Cdc2 kinase.

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Nern, Aljoscha, and Robert A. Arkowitz. "A Cdc24p-Far1p-Gβγ Protein Complex Required for Yeast Orientation during Mating." Journal of Cell Biology 144, no. 6 (March 22, 1999): 1187–202. http://dx.doi.org/10.1083/jcb.144.6.1187.

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Oriented cell growth requires the specification of a site for polarized growth and subsequent orientation of the cytoskeleton towards this site. During mating, haploid Saccharomyces cerevisiae cells orient their growth in response to a pheromone gradient overriding an internal landmark for polarized growth, the bud site. This response requires Cdc24p, Far1p, and a heterotrimeric G-protein. Here we show that a two- hybrid interaction between Cdc24p and Gβ requires Far1p but not pheromone-dependent MAP-kinase signaling, indicating Far1p has a role in regulating the association of Cdc24p and Gβ. Binding experiments demonstrate that Cdc24p, Far1p, and Gβ form a complex in which pairwise interactions can occur in the absence of the third protein. Cdc24p localizes to sites of polarized growth suggesting that this complex is localized. In the absence of CDC24-FAR1-mediated chemotropism, a bud site selection protein, Bud1p/Rsr1p, is essential for morphological changes in response to pheromone. These results suggest that formation of a Cdc24p-Far1p-Gβγ complex functions as a landmark for orientation of the cytoskeleton during growth towards an external signal.

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van Drogen, Frank, Ranjan Mishra, Fabian Rudolf, Michal J. Walczak, Sung Sik Lee, Wolfgang Reiter, Björn Hegemann, et al. "Mechanical stress impairs pheromone signaling via Pkc1-mediated regulation of the MAPK scaffold Ste5." Journal of Cell Biology 218, no. 9 (July 17, 2019): 3117–33. http://dx.doi.org/10.1083/jcb.201808161.

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Cells continuously adapt cellular processes by integrating external and internal signals. In yeast, multiple stress signals regulate pheromone signaling to prevent mating under unfavorable conditions. However, the underlying crosstalk mechanisms remain poorly understood. Here, we show that mechanical stress activates Pkc1, which prevents lysis of pheromone-treated cells by inhibiting polarized growth. In vitro Pkc1 phosphorylates conserved residues within the RING-H2 domains of the scaffold proteins Far1 and Ste5, which are also phosphorylated in vivo. Interestingly, Pkc1 triggers dispersal of Ste5 from mating projections upon mechanically induced stress and during cell–cell fusion, leading to inhibition of the MAPK Fus3. Indeed, RING phosphorylation interferes with Ste5 membrane association by preventing binding to the receptor-linked Gβγ protein. Cells expressing nonphosphorylatable Ste5 undergo increased lysis upon mechanical stress and exhibit defects in cell–cell fusion during mating, which is exacerbated by simultaneous expression of nonphosphorylatable Far1. These results uncover a mechanical stress–triggered crosstalk mechanism modulating pheromone signaling, polarized growth, and cell–cell fusion during mating.

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Busti, Stefano, Laura Gotti, Chiara Balestrieri, Lorenzo Querin, Guido Drovandi, Giovanni Felici, Gabriella Mavelli, Paola Bertolazzi, Lilia Alberghina, and Marco Vanoni. "Overexpression of Far1, a cyclin-dependent kinase inhibitor, induces a large transcriptional reprogramming in which RNA synthesis senses Far1 in a Sfp1-mediated way." Biotechnology Advances 30, no. 1 (January 2012): 185–201. http://dx.doi.org/10.1016/j.biotechadv.2011.09.007.

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31

Wang, Hai, and Haiyang Wang. "Multifaceted roles of FHY3 and FAR1 in light signaling and beyond." Trends in Plant Science 20, no. 7 (July 2015): 453–61. http://dx.doi.org/10.1016/j.tplants.2015.04.003.

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Atir-Lande, Avigail, Tsvia Gildor, and Daniel Kornitzer. "Role for the SCFCDC4Ubiquitin Ligase inCandida albicansMorphogenesis." Molecular Biology of the Cell 16, no. 6 (June 2005): 2772–85. http://dx.doi.org/10.1091/mbc.e05-01-0079.

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The ability of Candida albicans, a major fungal pathogen, to switch between a yeast form, and a hyphal (mold) form is recognized as being important for the ability of the organism to invade the host and cause disease. We found that a C. albicans mutant deleted for CaCDC4, a homologue of the Saccharomyces cerevisiae F-box protein component of the SCFCDC4ubiquitin ligase, is viable and displays constitutive filamentous, mostly hyphal, growth. The phenotype of the Cacdc4–/– mutant suggests that ubiquitin-mediated protein degradation is involved in the regulation of the dimorphic switch of C. albicans and that one or more regulators of the yeast-to-mold switch are among the substrates of SCFCaCDC4. Epistasis analysis indicates that the Cacdc4–/– phenotype is largely independent of the filamentation-inducing transcription factors Efg1 and Cph1. We identify C. albicans Far1 and Sol1, homologues of the S. cerevisiae SCFCDC4substrates Far1 and Sic1, and show that Sol1 is a substrate of C. albicans Cdc4. Neither protein is essential for the hyphal phenotype of the Cacdc4–/– mutant. However, ectopic expression and deletion of SOL1 indicate a role for this gene in C. albicans morphogenesis.

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bin Yusof, Mohammad Termizi, Michael J. Kershaw, Darren M. Soanes, and Nicholas J. Talbot. "FAR1 and FAR2 Regulate the Expression of Genes Associated with Lipid Metabolism in the Rice Blast Fungus Magnaporthe oryzae." PLoS ONE 9, no. 6 (June 20, 2014): e99760. http://dx.doi.org/10.1371/journal.pone.0099760.

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34

Peter, M., and I. Herskowitz. "Direct inhibition of the yeast cyclin-dependent kinase Cdc28-Cln by Far1." Science 265, no. 5176 (August 26, 1994): 1228–31. http://dx.doi.org/10.1126/science.8066461.

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35

McKinney, J. D., F. Chang, N. Heintz, and F. R. Cross. "Negative regulation of FAR1 at the Start of the yeast cell cycle." Genes & Development 7, no. 5 (May 1, 1993): 833–43. http://dx.doi.org/10.1101/gad.7.5.833.

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36

Devlin, Paul F., and Hamad Siddiqui. "FHY3 and FAR1 mediate red light input to the Arabidopsis circadian clock." Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology 153, no. 2 (June 2009): S207. http://dx.doi.org/10.1016/j.cbpa.2009.04.475.

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37

de Silva, Nayana D. G., Jhadeswar Murmu, Denise Chabot, Keith Hubbard, Peter Ryser, Isabel Molina, and Owen Rowland. "Root Suberin Plays Important Roles in Reducing Water Loss and Sodium Uptake in Arabidopsis thaliana." Metabolites 11, no. 11 (October 27, 2021): 735. http://dx.doi.org/10.3390/metabo11110735.

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Suberin is a cell-wall-associated hetero-polymer deposited in specific plant tissues. The precise role of its composition and lamellae structure in protecting plants against abiotic stresses is unclear. In Arabidopsis thaliana, we tested the biochemical and physiological responses to water deficiency and NaCl treatment in mutants that are differentially affected in suberin composition and lamellae structure. Chronic drought stress increased suberin and suberin-associated waxes in wild-type plants. Suberin-deficient mutants were not more susceptible than the wild-type to the chronic drought stress imposed in this study. Nonetheless, the cyp86a1-1 cyp86b1-1 mutant, which had a severely altered suberin composition and lamellae structure, exhibited increased water loss through the root periderm. Cyp86a1-1 cyp86b1-1 also recorded lower relative water content in leaves. The abcg2-1 abcg6-1 abcg20-1 mutant, which has altered suberin composition and lamellae, was very sensitive to NaCl treatment. Furthermore, cyp86a1-1 cyp86b1-1 recorded a significant drop in the leaf K/Na ratio, indicating salt sensitivity. The far1-2 far4-1 far5-1 mutant, which did not show structural defects in the suberin lamellae, had similar responses to drought and NaCl treatments as the wild-type. Our results provide evidence that the suberin amount and lamellae structure are key features in the barrier function of suberin in reducing water loss and reducing sodium uptake through roots for better performance under drought and salt stresses.

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38

Hudson, M., C. Ringli, M. T. Boylan, and P. H. Quail. "The FAR1 locus encodes a novel nuclear protein specific to phytochrome A signaling." Genes & Development 13, no. 15 (August 1, 1999): 2017–27. http://dx.doi.org/10.1101/gad.13.15.2017.

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39

Peter, Matthias, Anton Gartner, Joe Horecka, Gustav Ammerer, and Ira Herskowitz. "FAR1 links the signal transduction pathway to the cell cycle machinery in yeast." Cell 73, no. 4 (May 1993): 747–60. http://dx.doi.org/10.1016/0092-8674(93)90254-n.

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40

Peter, M., A. Gartner, J. Horecka, G. Ammerer, and I. Herskowitz. "FAR1 links the signal transduction pathway to the cell cycle machinery in yeast." Trends in Cell Biology 3, no. 8 (August 1993): 256. http://dx.doi.org/10.1016/0962-8924(93)90048-6.

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41

Honsho, Masanori, Shunsuke Asaoku, and Yukio Fujiki. "Posttranslational Regulation of Fatty Acyl-CoA Reductase 1, Far1, Controls Ether Glycerophospholipid Synthesis." Journal of Biological Chemistry 285, no. 12 (January 13, 2010): 8537–42. http://dx.doi.org/10.1074/jbc.m109.083311.

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42

Cherkasova, Vera, David M. Lyons, and Elaine A. Elion. "Fus3p and Kss1p Control G1 Arrest in Saccharomyces cerevisiae Through a Balance of Distinct Arrest and Proliferative Functions That Operate in Parallel With Far1p." Genetics 151, no. 3 (March 1, 1999): 989–1004. http://dx.doi.org/10.1093/genetics/151.3.989.

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AbstractIn Saccharomyces cerevisiae, mating pheromones activate two MAP kinases (MAPKs), Fus3p and Kss1p, to induce G1 arrest prior to mating. Fus3p is known to promote G1 arrest by activating Far1p, which inhibits three Clnp/Cdc28p kinases. To analyze the contribution of Fus3p and Kss1p to G1 arrest that is independent of Far1p, we constructed far1 CLN strains that undergo G1 arrest from increased activation of the mating MAP kinase pathway. We find that Fus3p and Kss1p both control G1 arrest through multiple functions that operate in parallel with Far1p. Fus3p and Kss1p together promote G1 arrest by repressing transcription of G1/S cyclin genes (CLN1, CLN2, CLB5) by a mechanism that blocks their activation by Cln3p/Cdc28p kinase. In addition, Fus3p and Kss1p counteract G1 arrest through overlapping and distinct functions. Fus3p and Kss1p together increase the expression of CLN3 and PCL2 genes that promote budding, and Kss1p inhibits the MAP kinase cascade. Strikingly, Fus3p promotes proliferation by a novel function that is not linked to reduced Ste12p activity or increased levels of Cln2p/Cdc28p kinase. Genetic analysis suggests that Fus3p promotes proliferation through activation of Mcm1p transcription factor that upregulates numerous genes in G1 phase. Thus, Fus3p and Kss1p control G1 arrest through a balance of arrest functions that inhibit the Cdc28p machinery and proliferative functions that bypass this inhibition.

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43

Udo, Edet E., and Eiman Sarkhoo. "Genetic analysis of high-level mupirocin resistance in the ST80 clone of community-associated meticillin-resistant Staphylococcus aureus." Journal of Medical Microbiology 59, no. 2 (February 1, 2010): 193–99. http://dx.doi.org/10.1099/jmm.0.013268-0.

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Four community-associated meticillin-resistant Staphylococcus aureus (CA-MRSA) isolates expressing high-level mupirocin resistance (MIC >1024 mg l−1) were isolated from four sites of a diabetic patient and characterized for the genetic location of their resistance determinants and typed using PFGE, staphylococcal cassette chromosome mec (SCCmec), the coagulase gene and multilocus sequence typing to ascertain their relatedness. The presence of genes for resistance to high-level mupirocin (mupA), tetracycline (tetK) and fusidic acid (far1), Panton–Valentine leukocidin (PVL), accessory gene regulators (agr) and capsular polysaccharide (cap) were detected in PCR assays. The isolates were resistant to kanamycin, streptomycin, tetracycline, fusidic acid and cadmium acetate, and harboured mupA, tetK, far1, PVL, agr3 and cap8. They had identical PFGE patterns and coagulase gene type, possessed the type IV SCCmec element and belonged to sequence type 80 (ST80). However, they had three different plasmid profiles: (i) 28.0 and 26.0 kb; (ii) 28.0, 21.0 and 4.0 kb; and (iii) 41.0 and 4.0 kb. Genetic studies located the resistance to tetracycline, fusidic acid and cadmium acetate on the 28 kb plasmid and mupA on the related non-conjugative 26 and 21 kb plasmids. One of the 21 kb mupirocin-resistance plasmids was derived from the ∼41 kb plasmid during transfer experiments. The emergence of high-level mupirocin resistance in the ST80-SCCmec IV MRSA clone demonstrates the increasing capacity of CA-MRSA clones to acquire resistance to multiple antibacterial agents. The presence of different plasmid profiles in genetically identical isolates creates difficulty in the interpretation of typing results and highlights the weakness of using plasmid analysis as the sole method for strain typing.

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Wells, Amy Stuart, Jennifer Jellison Holme, Awo Korantemaa Atanda, and Anita Tijerina Revilla. "Tackling Racial Segregation One Policy at a Time: Why School Desegregation Only Went So Far1." Teachers College Record 107, no. 9 (September 2005): 2141–77. http://dx.doi.org/10.1111/j.1467-9620.2005.00587.x.

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Wang, Haiyang, and Xing Wang Deng. "ArabidopsisFHY3 defines a key phytochrome A signaling component directly interacting with its homologous partner FAR1." EMBO Journal 21, no. 6 (March 15, 2002): 1339–49. http://dx.doi.org/10.1093/emboj/21.6.1339.

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Liu, Yang, Hongbin Wei, Mengdi Ma, Quanquan Li, Dexin Kong, Juan Sun, Xiaojing Ma, et al. "Arabidopsis FHY3 and FAR1 Regulate the Balance between Growth and Defense Responses under Shade Conditions." Plant Cell 31, no. 9 (July 16, 2019): 2089–106. http://dx.doi.org/10.1105/tpc.18.00991.

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Liu, Yang, Mengdi Ma, Gang Li, Li Yuan, Yurong Xie, Hongbin Wei, Xiaojing Ma, et al. "Transcription Factors FHY3 and FAR1 Regulate Light-Induced CIRCADIAN CLOCK ASSOCIATED1 Gene Expression in Arabidopsis." Plant Cell 32, no. 5 (March 9, 2020): 1464–78. http://dx.doi.org/10.1105/tpc.19.00981.

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Shimada, Yukiko, Marie-Pierre Gulli, and Matthias Peter. "Nuclear sequestration of the exchange factor Cdc24 by Far1 regulates cell polarity during yeast mating." Nature Cell Biology 2, no. 2 (January 17, 2000): 117–24. http://dx.doi.org/10.1038/35000073.

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Esch, R. Keith, Yuqi Wang, and Beverly Errede. "Pheromone-Induced Degradation of Ste12 Contributes to Signal Attenuation and the Specificity of Developmental Fate." Eukaryotic Cell 5, no. 12 (October 13, 2006): 2147–60. http://dx.doi.org/10.1128/ec.00270-06.

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ABSTRACT The Ste12 transcription factor of Saccharomyces cerevisiae regulates transcription programs controlling two different developmental fates. One is differentiation into a mating-competent form that occurs in response to mating pheromone. The other is the transition to a filamentous-growth form that occurs in response to nutrient deprivation. These two distinct roles for Ste12 make it a focus for studies into regulatory mechanisms that impart biological specificity. The transient signal characteristic of mating differentiation led us to test the hypothesis that regulation of Ste12 turnover might contribute to attenuation of the mating-specific transcription program and restrict activation of the filamentation program. We show that prolonged pheromone induction leads to ubiquitin-mediated destabilization and decreased amounts of Ste12. This depletion in pheromone-stimulated cultures is dependent on the mating-pathway-dedicated mitogen-activated protein kinase Fus3 and its target Cdc28 inhibitor, Far1. Attenuation of pheromone-induced mating-specific gene transcription (FUS1) temporally correlates with Ste12 depletion. This attenuation is abrogated in the deletion backgrounds (fus3Δ or far1Δ) where Ste12 is found to persist. Additionally, pheromone induces haploid invasion and filamentous-like growth instead of mating differentiation when Ste12 levels remain high. These observations indicate that loss of Ste12 reinforces the adaptive response to pheromone and contributes to the curtailing of a filamentation response.

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Wang, Wanqing, Weijiang Tang, Tingting Ma, De Niu, Jing Bo Jin, Haiyang Wang, and Rongcheng Lin. "A pair of light signaling factors FHY3 and FAR1 regulates plant immunity by modulating chlorophyll biosynthesis." Journal of Integrative Plant Biology 58, no. 1 (July 24, 2015): 91–103. http://dx.doi.org/10.1111/jipb.12369.

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Journal articles on the topic 'Far1'

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