Relevant bibliographies by topics / Rag GTPase

Academic literature on the topic 'Rag GTPase'

Author: Grafiati
Published: 9 March 2023

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Journal articles on the topic "Rag GTPase"

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Shen, Kuang, and David M. Sabatini. "Ragulator and SLC38A9 activate the Rag GTPases through noncanonical GEF mechanisms." Proceedings of the National Academy of Sciences 115, no. 38 (September 4, 2018): 9545–50. http://dx.doi.org/10.1073/pnas.1811727115.

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The mechanistic target of rapamycin complex 1 (mTORC1) growth pathway detects nutrients through a variety of sensors and regulators that converge on the Rag GTPases, which form heterodimers consisting of RagA or RagB tightly bound to RagC or RagD and control the subcellular localization of mTORC1. The Rag heterodimer uses a unique “locking” mechanism to stabilize its active (GTPRagA–RagCGDP) or inactive (GDPRagA–RagCGTP) nucleotide states. The Ragulator complex tethers the Rag heterodimer to the lysosomal surface, and the SLC38A9 transmembrane protein is a lysosomal arginine sensor that upon activation stimulates mTORC1 activity through the Rag GTPases. How Ragulator and SLC38A9 control the nucleotide loading state of the Rag GTPases remains incompletely understood. Here we find that Ragulator and SLC38A9 are each unique guanine exchange factors (GEFs) that collectively push the Rag GTPases toward the active state. Ragulator triggers GTP release from RagC, thus resolving the locked inactivated state of the Rag GTPases. Upon arginine binding, SLC38A9 converts RagA from the GDP- to the GTP-loaded state, and therefore activates the Rag GTPase heterodimer. Altogether, Ragulator and SLC38A9 act on the Rag GTPases to activate the mTORC1 pathway in response to nutrient sufficiency.
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Lee, Minji, Jong Hyun Kim, Ina Yoon, Chulho Lee, Mohammad Fallahi Sichani, Jong Soon Kang, Jeonghyun Kang, et al. "Coordination of the leucine-sensing Rag GTPase cycle by leucyl-tRNA synthetase in the mTORC1 signaling pathway." Proceedings of the National Academy of Sciences 115, no. 23 (May 21, 2018): E5279—E5288. http://dx.doi.org/10.1073/pnas.1801287115.

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A protein synthesis enzyme, leucyl-tRNA synthetase (LRS), serves as a leucine sensor for the mechanistic target of rapamycin complex 1 (mTORC1), which is a central effector for protein synthesis, metabolism, autophagy, and cell growth. However, its significance in mTORC1 signaling and cancer growth and its functional relationship with other suggested leucine signal mediators are not well-understood. Here we show the kinetics of the Rag GTPase cycle during leucine signaling and that LRS serves as an initiating “ON” switch via GTP hydrolysis of RagD that drives the entire Rag GTPase cycle, whereas Sestrin2 functions as an “OFF” switch by controlling GTP hydrolysis of RagB in the Rag GTPase–mTORC1 axis. The LRS–RagD axis showed a positive correlation with mTORC1 activity in cancer tissues and cells. The GTP–GDP cycle of the RagD–RagB pair, rather than the RagC–RagA pair, is critical for leucine-induced mTORC1 activation. The active RagD–RagB pair can overcome the absence of the RagC–RagA pair, but the opposite is not the case. This work suggests that the GTPase cycle of RagD–RagB coordinated by LRS and Sestrin2 is critical for controlling mTORC1 activation, and thus will extend the current understanding of the amino acid-sensing mechanism.
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Gollwitzer, Peter, Nina Grützmacher, Sabine Wilhelm, Daniel Kümmel, and Constantinos Demetriades. "A Rag GTPase dimer code defines the regulation of mTORC1 by amino acids." Nature Cell Biology 24, no. 9 (September 2022): 1394–406. http://dx.doi.org/10.1038/s41556-022-00976-y.

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AbstractAmino acid availability controls mTORC1 activity via a heterodimeric Rag GTPase complex that functions as a scaffold at the lysosomal surface, bringing together mTORC1 with its activators and effectors. Mammalian cells express four Rag proteins (RagA–D) that form dimers composed of RagA/B bound to RagC/D. Traditionally, the Rag paralogue pairs (RagA/B and RagC/D) are referred to as functionally redundant, with the four dimer combinations used interchangeably in most studies. Here, by using genetically modified cell lines that express single Rag heterodimers, we uncover a Rag dimer code that determines how amino acids regulate mTORC1. First, RagC/D differentially define the substrate specificity downstream of mTORC1, with RagD promoting phosphorylation of its lysosomal substrates TFEB/TFE3, while both Rags are involved in the phosphorylation of non-lysosomal substrates such as S6K. Mechanistically, RagD recruits mTORC1 more potently to lysosomes through increased affinity to the anchoring LAMTOR complex. Furthermore, RagA/B specify the signalling response to amino acid removal, with RagB-expressing cells maintaining lysosomal and active mTORC1 even upon starvation. Overall, our findings reveal key qualitative differences between Rag paralogues in the regulation of mTORC1, and underscore Rag gene duplication and diversification as a potentially impactful event in mammalian evolution.
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Rogala, Kacper B., Xin Gu, Jibril F. Kedir, Monther Abu-Remaileh, Laura F. Bianchi, Alexia M. S. Bottino, Rikke Dueholm, et al. "Structural basis for the docking of mTORC1 on the lysosomal surface." Science 366, no. 6464 (October 10, 2019): 468–75. http://dx.doi.org/10.1126/science.aay0166.

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The mTORC1 (mechanistic target of rapamycin complex 1) protein kinase regulates growth in response to nutrients and growth factors. Nutrients promote its translocation to the lysosomal surface, where its Raptor subunit interacts with the Rag guanosine triphosphatase (GTPase)–Ragulator complex. Nutrients switch the heterodimeric Rag GTPases among four different nucleotide-binding states, only one of which (RagA/B•GTP–RagC/D•GDP) permits mTORC1 association. We used cryo–electron microscopy to determine the structure of the supercomplex of Raptor with Rag-Ragulator at a resolution of 3.2 angstroms. Our findings indicate that the Raptor α-solenoid directly detects the nucleotide state of RagA while the Raptor “claw” threads between the GTPase domains to detect that of RagC. Mutations that disrupted Rag-Raptor binding inhibited mTORC1 lysosomal localization and signaling. By comparison with a structure of mTORC1 bound to its activator Rheb, we developed a model of active mTORC1 docked on the lysosome.
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Figlia, Gianluca, Sandra Müller, Anna M. Hagenston, Susanne Kleber, Mykola Roiuk, Jan-Philipp Quast, Nora ten Bosch, et al. "Brain-enriched RagB isoforms regulate the dynamics of mTORC1 activity through GATOR1 inhibition." Nature Cell Biology 24, no. 9 (September 2022): 1407–21. http://dx.doi.org/10.1038/s41556-022-00977-x.

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AbstractMechanistic target of rapamycin complex 1 (mTORC1) senses nutrient availability to appropriately regulate cellular anabolism and catabolism. During nutrient restriction, different organs in an animal do not respond equally, with vital organs being relatively spared. This raises the possibility that mTORC1 is differentially regulated in different cell types, yet little is known about this mechanistically. The Rag GTPases, RagA or RagB bound to RagC or RagD, tether mTORC1 in a nutrient-dependent manner to lysosomes where mTORC1 becomes activated. Although the RagA and B paralogues were assumed to be functionally equivalent, we find here that the RagB isoforms, which are highly expressed in neurons, impart mTORC1 with resistance to nutrient starvation by inhibiting the RagA/B GTPase-activating protein GATOR1. We further show that high expression of RagB isoforms is observed in some tumours, revealing an alternative strategy by which cancer cells can retain elevated mTORC1 upon low nutrient availability.
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Anandapadamanaban, Madhanagopal, Glenn R. Masson, Olga Perisic, Alex Berndt, Jonathan Kaufman, Chris M. Johnson, Balaji Santhanam, Kacper B. Rogala, David M. Sabatini, and Roger L. Williams. "Architecture of human Rag GTPase heterodimers and their complex with mTORC1." Science 366, no. 6462 (October 10, 2019): 203–10. http://dx.doi.org/10.1126/science.aax3939.

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The Rag guanosine triphosphatases (GTPases) recruit the master kinase mTORC1 to lysosomes to regulate cell growth and proliferation in response to amino acid availability. The nucleotide state of Rag heterodimers is critical for their association with mTORC1. Our cryo–electron microscopy structure of RagA/RagC in complex with mTORC1 shows the details of RagA/RagC binding to the RAPTOR subunit of mTORC1 and explains why only the RagAGTP/RagCGDP nucleotide state binds mTORC1. Previous kinetic studies suggested that GTP binding to one Rag locks the heterodimer to prevent GTP binding to the other. Our crystal structures and dynamics of RagA/RagC show the mechanism for this locking and explain how oncogenic hotspot mutations disrupt this process. In contrast to allosteric activation by RHEB, Rag heterodimer binding does not change mTORC1 conformation and activates mTORC1 by targeting it to lysosomes.
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Zhu, Min, and Xiu-qi Wang. "Regulation of mTORC1 by Small GTPases in Response to Nutrients." Journal of Nutrition 150, no. 5 (January 21, 2020): 1004–11. http://dx.doi.org/10.1093/jn/nxz301.

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ABSTRACT Mechanistic target of rapamycin complex 1 (mTORC1) is a highly evolutionarily conserved serine/threonine kinase that regulates cell growth and metabolism in response to multiple environmental cues, such as nutrients, hormones, energy, and stress. Deregulation of mTORC1 can lead to diseases such as diabetes, obesity, and cancer. A series of small GTPases, including Rag, Ras homolog enriched in brain (Rheb), adenosine diphosphate ribosylation factor 1 (Arf1), Ras-related protein Ral-A, Ras homolog (Rho), and Rab, are involved in regulating mTORC1 in response to nutrients, and mTORC1 is differentially regulated via these small GTPases according to specific conditions. Leucine and arginine sensing are considered to be well-confirmed amino acid–sensing signals, activating mTORC1 via a Rag GTPase–dependent mechanism as well as the Ragulator complex and vacuolar H+-adenosine triphosphatase (v-ATPase). Glutamine promotes mTORC1 activation via Arf1 independently of the Rag GTPase. In this review, we summarize current knowledge regarding the regulation of mTORC1 activity by small GTPases in response to nutrients, focusing on the function of small GTPases in mTORC1 activation and how small GTPases are regulated by nutrients.
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Meng, Delong, Qianmei Yang, Huanyu Wang, Chase H. Melick, Rishika Navlani, Anderson R. Frank, and Jenna L. Jewell. "Glutamine and asparagine activate mTORC1 independently of Rag GTPases." Journal of Biological Chemistry 295, no. 10 (February 4, 2020): 2890–99. http://dx.doi.org/10.1074/jbc.ac119.011578.

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Nutrient sensing by cells is crucial, and when this sensing mechanism is disturbed, human disease can occur. mTOR complex 1 (mTORC1) senses amino acids to control cell growth, metabolism, and autophagy. Leucine, arginine, and methionine signal to mTORC1 through the well-characterized Rag GTPase signaling pathway. In contrast, glutamine activates mTORC1 through a Rag GTPase–independent mechanism that requires ADP-ribosylation factor 1 (Arf1). Here, using several biochemical and genetic approaches, we show that eight amino acids filter through the Rag GTPase pathway. Like glutamine, asparagine signals to mTORC1 through Arf1 in the absence of the Rag GTPases. Both the Rag-dependent and Rag-independent pathways required the lysosome and lysosomal function for mTORC1 activation. Our results show that mTORC1 is differentially regulated by amino acids through two distinct pathways.
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Zhu, Xingxing, Xian Zhou, Chaofan Li, Yanfeng Li, Jie Sun, Ariel Raybuck, Mark Robin Boothby, and Hu Zeng. "Rag GTPase critically contributes to humoral immunity independent of canonical mTORC1 signaling." Journal of Immunology 208, no. 1_Supplement (May 1, 2022): 112.03. http://dx.doi.org/10.4049/jimmunol.208.supp.112.03.

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Abstract The humoral immune response requires that B cells undergo a rapid metabolic shift and high demand of nutrients, which are vital to sustain the formation of germinal center. Rag GTPase senses amino acid availability to activate mechanistic target of rapamycin complex 1(mTORC1) pathway and modulate the function of transcription factor EB (TFEB), a member of the microphthalmia (MiT/TFE) family of HLH-leucine zipper transcription factors. However, little is known about how Rag GTPase coordinates amino acid sensing, mTORC1 activation and TFEB activity in humoral immune response. Here, we show that B cell intrinsic Rag GTPase is critical to the development and activation of B cells. Disruption of Rag GTPase complex, but not mTORC1 complex, abrogates germinal center formation, antibody production as well as plasma cell generation upon respiratory influenza infection. Mechanistically, the Rag GTPase complex senses specific amino acids to suppress TFEB activity, independent of canonical mTORC1 activation. Collectively, our data support the idea that Rag GTPase critically contributes to humoral immunity partly through suppressing TFEB and it is largely not necessary for canonical mTORC1 signaling. Supported by Mayo Foundation for Medical Education and Research
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Petit, Constance S., Agnes Roczniak-Ferguson, and Shawn M. Ferguson. "Recruitment of folliculin to lysosomes supports the amino acid–dependent activation of Rag GTPases." Journal of Cell Biology 202, no. 7 (September 30, 2013): 1107–22. http://dx.doi.org/10.1083/jcb.201307084.

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Birt-Hogg-Dubé syndrome, a human disease characterized by fibrofolliculomas (hair follicle tumors) as well as a strong predisposition toward the development of pneumothorax, pulmonary cysts, and renal carcinoma, arises from loss-of-function mutations in the folliculin (FLCN) gene. In this study, we show that FLCN regulates lysosome function by promoting the mTORC1-dependent phosphorylation and cytoplasmic sequestration of transcription factor EB (TFEB). Our results indicate that FLCN is specifically required for the amino acid–stimulated recruitment of mTORC1 to lysosomes by Rag GTPases. We further demonstrated that FLCN itself was selectively recruited to the surface of lysosomes after amino acid depletion and directly bound to RagA via its GTPase domain. FLCN-interacting protein 1 (FNIP1) promotes both the lysosome recruitment and Rag interactions of FLCN. These new findings define the lysosome as a site of action for FLCN and indicate a critical role for FLCN in the amino acid–dependent activation of mTOR via its direct interaction with the RagA/B GTPases.
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Dissertations / Theses on the topic "Rag GTPase"

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ESPOSITO, ALESSANDRA. "DIVERSITY IN MTORC1 SUBSTRATE RECRUITMENT ENABLES SPECIFICITY OF METABOLIC RESPONSES TO NUTRITIONAL CUES." Doctoral thesis, Università degli Studi di Milano, 2020. http://hdl.handle.net/2434/793428.

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The mechanistic target of rapamycin kinase complex 1 (mTORC1) is a key signaling hub that acts as a central regulator of several cellular processes, including cell growth and metabolism. The activation of mTORC1 occurs at the lysosomal surface via a two-step mechanism that requires a) its amino acid-dependent recruitment to the lysosome via the Rag GTPases and b) its growth factor-dependent activation by Rheb. mTORC1 senses and integrates multiple upstream signals to phosphorylate a broad number of substrates and modulate the crucial balance between cell anabolism and catabolism. However, whether mTORC1 can differentially regulate specific proteins to selectively respond to such a variety of intracellular and environmental cues is poorly understood. Here we show that Transcription Factor EB (TFEB), a master modulator of lysosomal biogenesis and autophagy, is modulated by mTORC1 via a specific substrate recruitment mechanism that is mediated by Rag GTPases. Differently from the well-characterized mTORC1 substrates S6K and 4E-BP1, which are recruited by mTORC1 via binding to the regulatory subunit Raptor, TFEB interaction with mTORC1 relies on its physical association with active Rag C/D. Owing to this mechanism, TFEB phosphorylation is insensitive to growth factor-mediated activation of Rheb but highly sensitive to amino acid-mediated activation of Rag GTPases. Strikingly, substituting the region of TFEB responsible for its recruitment to mTORC1 with the one of S6K, inverted TFEB phosphorylation behaviour and made it similar to S6K/4E-BP1. Thus, our findings reveal that diversity in mTORC1 substrate recruitment mechanisms enables mTORC1 to induce selective responses to specific nutritional cues.
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Belbachir, Nadjet. "Mécanismes physiopathologies du syndrome de Brugada : caractérisation d'un nouveau gène morbide Rad GTPase." Thesis, Nantes, 2017. http://www.theses.fr/2017NANT1015/document.

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Le syndrome de Brugada est un trouble du rythme cardiaque héréditaire qui mène à l’apparition de fibrillations ventriculaires et à la mort subite cardiaque. Seulement 30% des cas atteints de ce syndrome sont liés à des mutations génétiques et ce à cause de la complexité du phénotype engendré. Le gène RRAD a été identifié dans une famille qui compte 5 membres atteints du syndrome de Brugada, tous porteurs du variant p.R211H. Ce gène code pour la protéine G monomérique Rad dont le rôle principal est de réguler le courant calcique de type L dans les cellules musculaires squelettiques et cardiaques. Cette étude associe trois modèles d’étude visant à discriminer l’implication de Rad dans le phénotype des patients atteints : Un modèle de surexpression pour étudier le rôle de Rad et l’impact de sa surexpression sur l’activité électrique et la structure des cardiomyocytes, des cardiomyocytes dérivés de cellules IPS reprogrammées des patients porteurs de la mutation pour en déterminer le phénotype cellulaire, et un modèle de souris knock in pour la mutation p.R211H généré dans le but d’intégrer le phénotype cellulaire à l’échelle de l’organe entier. Les résultats obtenus sur les trois modèles, montrent que Rad R211H provoque des troubles au niveau de l’activité électrique du coeur mais aussi au niveau de la structure des cellules différenciées et ces troubles se traduisent par des anomalies à l’ECG chez la souris. Cette étude est la première à démontrer l’implication de Rad GTPase dans le syndrome de Brugada et la seule à démontrer, à ce jour, des perturbations du cytosquelette dans cette pathologie qui est toujours considérée comme une pathologie exclusivement rythmique
Brugada syndrome (BrS) is a rare inherited cardiac disorder linked to high risk of ventricular arrhythmias and sudden death. In the present day, only 30% of BrS cases have known genetic causes. Most of these mutations have been identified in the SCN5A gene that encodes the cardiac voltage-gated sodium channel NaV1.5. We identified a rare variant in the RRAD gene encoding for the small G protein Rad GTPase, in a familial case of BrS. The aim of this work was to elucidate the mechanisms by which the RRAD p.R211H variant could lead to BrS. First, an overexpressing model was developed using neonatal mouse cardiomyocytes to define the involvement of Rad in the electrical function of cardiomyocytes. Then, cardiac cells were derived from human induced pluripotent stem cells reprogrammed from the carriers of the Rad mutation in order to investigate the phenotype induced at the cellular level. Furthermore, a knock in mouse has been generated to study the impact of this same mutation on the organ level. The three models summarized in a complementary way the phenotype caused by the Rad mutation on the electrical activity at the cellular and the organ levels. The mutation seem to trigger structural defects in the cardiomyocytes that can be involved in the electrical defects related to the disease. The present study is the first report of the potential link between Rad GTPase and BrS. The phenotype reported recapitulates the classical electrophysiological signature of the disease but also associates cytoskeleton disturbances
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Winge, Per. "The evolution of small GTP binding proteins in cellular organisms. Studies of RAS GTPases in arabidopsis thaliana and the Ral GTPase from Drosophila melanogaster." Doctoral thesis, Norwegian University of Science and Technology, Faculty of Natural Sciences and Technology, 2002. http://urn.kb.se/resolve?urn=urn:nbn:no:ntnu:diva-169.

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Small GTP binding proteins function as molecular switches which cycles between GTP-bound ON and GDP-bound OFF states, and regulate a wide variety of cellular processes as biological timers. The first characterized member of the small GTPase family, the mutated oncogene p21 src, later known as Harvey-Ras, was identified in the early 1980s (Shih, T. Y. et al. 1980). In the following years small Ras-lik GTPases were found in several organisms and it was soon discovered that they took part in processes, such as signal transduction, gene expression, cytoskeleton reorganisation, microtubule organisation, and vesicular and nuclear transport. The first Rho (Ras homology) gene was cloned in 1985 from the sea slug Aplysia (Madaule, P. et al. 1985) and because of their homology to Ras it was first suspected that they could act as oncogenes. Later studies have shown that even though they participate in processes such as cell migration and motility they are not mutated in cancers.

The first indications that Rho was a signaling protein regulating the actin cytoskeleton, came from experiments where activated forms of human RhoA was microinjected into 3T3 cells (Paterson, H. F. et al. 1990). Another Rho-like GTPase Rac1 (named after Ras-related C3 botulinum toxin substrate) was later shown to regulate actin cytoskeletal dynamics as well, suggesting that Rho-family members cooperate in controlling these processes (Ridley, A. J. et al. 1992). The Rac GTPase was also implicated in regulating the phagocytic NADPH oxidase, which produce superoxide for killing phagocytized microorganisms (Abo, A. et al. 1991). Thus, it soon became clear that Rac/Rho and the related GTPase Cdc42 (cell division cycle 42) had central functions in many important cellular processes.

There are at least three types of regulators for Rho-like proteins. The GDP/GTP exchange factors (GEFs) which stimulates conversion from the GDPbound form to the GTP-bound form. GDP dissociation inhibitors (GDIs) decrease the nucleotide dissociation from the GTPase and retrieve them from membranes to the cytosol. GTPase activating proteins (GAPs) stimulates the intrinsic GTPase activity and GTP hydrolysis. In addition there are probably regulators that dissociate GDI from the GTPase leaving it open for activation by the RhoGEFs.

Ras and Rho-family proteins participate in a coordinated regulation of cellular processes such as cell motility, cell growth and division. The Ral GTPase is closely related to Ras and recent studies have shown that this GTPase is involved in crosstalk between both Ras and Rho proteins (Feig, L. A. et al. 1996; Oshiro, T. et al. 2002). Ral proteins are not found in plants and they appear to be restricted to animalia and probably yeast. During a screen for small GTPases in Drosophila melanogaster I discovered in 1993 several new members of the Ras-family, such as Drosophila Ral (DRal), Ric1 and Rap2. The functions of Ral GTPases in Drosophila have until recently been poorly known, but in paper 2 we present some of the new findings.

Rho-like GTPases have been identified in several eukaryotic organisms such as, yeast (Bender, A. et al. 1989), Dictyostelium discoideum (Bush, J. et al. 1993), plants (Yang, Z. et al. 1993), Entamoeba histolytica (Lohia, A. et al. 1993) and Trypanosoma cruzi (Nepomuceno-Silva, J. L. et al. 2001). In our first publication, (Winge, P. et al. 1997), we describe the cloning of cDNAs from RAC-like GTPases in Arabidopsis thaliana and show mRNA expressions pattern for five of the genes. The five genes analyzed were expressed in most plant tissues with the exception of AtRAC2 (named Arac2 in the paper), which has an expression restricted to vascular tissues. We also discuss the evolution and development of RAC genes in plants. The third publication, (Winge, P. et al. 2000), describe the genetic structure and the genomic sequence of 11 RAC genes from Arabidopsis thaliana. As most genomic sequences of the AtRACs we analyzed came from the Landsberg erecta ecotype and the Arabidopsis thaliana genome was sequenced from the Columbia ecotype, it was possible to compare the sequences and identify new polymorphisms. The genomic location of the AtRAC genes plus the revelation of large genomic duplications provided additional information regarding the evolution of the gene family in plants. A summary and discussion of these new findings are presented together with a general study of small Ras-like GTPases and their evolution in cellular organisms. This study suggests that the small GTPases in eukaryots evolved from two bacterial ancestors, a Rab-like and a MglA/Arp-like (Arf-like) protein. The MglA proteins (after the mgl locus in Myxococcus xanthus) are required for gliding motility, which is a type of movement that take place without help of flagella.

The second publication describes experiments done with the Drosophila melanogaster DRal gene and its effects on cell shape and development. Ectopic expression of dominant negative forms of DRal reveals developmental defects in eye facets and hairs, while constitutive activated forms affects dorsal closure, leaving embryos with an open dorsal phenotype. Results presented in this publication suggest that DRal act through the Jun N-terminal kinase (JNK) pathway to regulate dorsal closure, but recent findings may point to additional explanations as well. The results also indicate a close association between processes regulated by Rac/Rho and Ral proteins in Drosophila.

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Ghiaur, Gabriel. "The role of Rho GTPases in hematopoietic stem cell biology RhoA GTPase regulates adult HSC engraftment and Rac1 GTPases is important for embryonic HSC /." Cincinnati, Ohio : University of Cincinnati, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1204374567.

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Maximano, Filipe Manuel Correia. "Armus : A novel link between Rac and Rab small GTPases." Thesis, Imperial College London, 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.526397.

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Yarwood, Sam. "Calcium signalling and the small GTPase Ras." Thesis, University of Bristol, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.492619.

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Calcium (Ca ²?) is a highly versatile signal that regulates a host of intracellular events across the biological spectrum. Carefully regulated changes in intracellular Ca²? concentration, over a broad temporal and spatial range, carry complex signals to a plethora of proteins who decode and transduce the information and regulate a wide variety of physiological processes.
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Kirsten, Marie Lis. "Biophysical studies of Rab GTPase membrane binding." Thesis, Imperial College London, 2011. http://hdl.handle.net/10044/1/6964.

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Rab proteins are the largest subfamily of the Ras superfamily of small GTPases, with more than 60 known members, that are involved in a multitude of different processes regulating membrane traffic. Rab proteins cycle between the cytosol and association with membranes, whereby each Rab exhibits a characteristic and specific subcellular localisation. It remains obscure how Rab proteins, in spite of high sequence and structure identity, distinguish between different membranes in the cell with such specificity. Membrane biophysical properties, such as stored curvature elastic stress and bending rigidity, are increasingly found to be determinants for protein recruitment and activity, and other Ras related proteins have recently been shown to exhibit sensitivity towards lipid species and elastic membrane properties. In this study Rab membrane binding is for the first time correlated to membrane bending rigidity, suggesting that biophysical properties of lipid membranes may play a role in the regulation of Rab targeting. Furthermore, all Rab proteins tested were observed to bind membranes in the absence of other protein factors, questioning the function of protein targeting factors for the Rab membrane recruitment process. Another aspect of Rab membrane interaction is Rab extraction from membranes by GDI. A large scale in vitro screening of 17 Rab proteins revealed a broad range of extractability from membranes with GDI. No correlation was found between extractability and the C-terminal prenylation motif, and no difference in extractability was observed in direct comparison of the extraction potential with GDIα and β. However, Rab proteins that exhibited low extractability from membranes are involved in secretory processes, suggesting a functional correlation to extractability. Furthermore, Rab40c as the first mammalian Rab protein to date was shown to be palmitoylated.
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Wakade, Rohan Sanjay. "Rôle de GTPase de type Rab, Ypt6, chez le pathogène fongique opportuniste de l’homme, Candida albicans." Thesis, Université Côte d'Azur (ComUE), 2017. http://www.theses.fr/2017AZUR4064.

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Candida albicans est un organisme commensal présent dans le microbiote, qui peut cependant provoquer des infections superficielles mais aussi systémiques, engageant alors le pronostic vital chez les patients immunodéprimés. La transition entre forme bourgeonnante et forme filamenteuse hyphale hautement polarisée, ce qui nécessite une réorganisation du cytosquelette et un trafic membranaire soutenu, est associée à la virulence. Chez les eucaryotes, les GTPases de la famille Rab (Ras related protein in the brain) et leurs régulateurs jouent un rôle central dans le trafic membranaire. L'objectif de ce travail est de comprendre le rôle de ces protéines, en particulier de Ypt6, l'homologue de Rab6 humain, dans la transition morphologique et la virulence de C. albicans. Dans ce but, j'ai construit des mutants « perte de fonction » et déterminé que YPT6 n'est pas essentiel à la viabilité, mais est critique pour l'intégrité de la paroi cellulaire et la croissance hyphale invasive ; les hyphes du mutant ypt6 sont plus courtes que celles de la souche sauvage. En outre, YPT6 est critique pour la virulence dans deux modèles murins de candidose. Lors de la croissance hyphale, Ypt6 est co-localisé avec Arl1, une GTPase de la famille Arf (ADP Ribosylation Factor), également nécessaire pour la croissance hyphale et la virulence de C. albicans. De plus, la surexpression de YPT6 compense spécifiquement le défaut de croissance hyphale du mutant de délétion arl1, mais pas l'inverse. La délétion de YPT6 résulte également en une augmentation du nombre de citernes Golgiennes, suggérant que l'intégrité du Golgi est altérée dans ce mutant. Utilisant de l'imagerie sur cellules vivantes, j'ai montré que la distribution d’Abp1 (Actin binding protein 1), qui est un rapporteur des sites d’endocytose, est aussi altérée dans le mutant ypt6, en ceci qu’elle n’est plus restreinte à l’apex de l’hyphe, comme observé dans les cellules sauvages. Ces données suggèrent que le défaut de maintien de la croissance hyphale du mutant ypt6 est au moins en partie associé à une altération de la distribution des sites d’endocytose. En résumé, j’ai identifié le rôle de Ypt6 dans la croissance hyphale invasive et la virulence du pathogène fongique opportuniste de l’homme C. albicans, et mis en évidence une interaction entre deux GTPases, Ypt6 et Arl1, lors du processus de croissance hyphale
Candida albicans is a harmless constituent of the human microbiota that causes superficial infections as well as life threatening infections in immune compromised individuals. The transition from a budding form to the highly polarized hyphal form is associated with virulence and requires cytoskeleton reorganization and sustained membrane trafficking. In a range of eukaryotes, Ras related protein in the brain (Rab) G proteins and their regulators have been shown to play a central role in membrane traffic. The objective of this work is to understand the role of Rab proteins, in particular Ypt6, the homolog of Human Rab6, in the morphological transition and virulence of C. albicans. To this aim, I generated loss of function mutants and found that YPT6 is not essential for viability, yet was critical for cell wall integrity and invasive hyphal growth, with ypt6 hyphal filaments shorter compared to that of the wild type (WT). Furthermore, YPT6 was important for virulence in two murine candidiasis models. I determined that Ypt6 was localized at the late Golgi compartment during hyphal growth, where it co-localized with Arl1, a small GTPase of the Arf (ADP Ribosylation Factor) family, also required for hyphal growth and virulence. Interestingly, overexpression of YPT6 specifically rescued the hyphal growth defect of the arl1 mutant, but not the converse. Further characterization of the ypt6 deletion mutant showed that the number of Golgi cisternae is increased in this mutant compared to that of WT strain, suggesting an alteration of Golgi integrity. In addition, using live cell imaging I showed that the distribution of Actin binding protein 1 (Abp1), which is a reporter for actin patches, was altered in the ypt6 mutant, in that it was no longer restricted to the tip of the filament, as is observed in WT cells. These data suggest that the defect in hyphal growth maintenance of the ypt6 deletion mutant is at least partly associated with an alteration of the distribution of endocytic sites. Thus, I identified a critical role of Ypt6 during invasive hyphal growth and virulence in the human fungal opportunistic pathogen C. albicans and revealed an interaction between Ypt6 and Arl1 in the hyphal growth process
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Fan, Wing-Tze. "Characterization of Ras-GRF2, a bifunctional guanine nucleotide exchange factor for the Ras and Rac GTPases." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2001. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/NQ63720.pdf.

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Jilkina, Olga. "The function of Ral GTPase in human platelets." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp02/NQ41614.pdf.

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Books on the topic "Rag GTPase"

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Li, Guangpu, and Nava Segev, eds. Rab GTPases. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1346-7.

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Li, Guangpu, ed. Rab GTPases. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2569-8.

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Rush, Mark, and Peter D’Eustachio, eds. The Small GTPase Ran. Boston, MA: Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-1501-2.

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Ed, Manser, and Leung Thomas, eds. GTPase protocols: The Ras superfamily. Totowa, N.J: Humana Press, 2002.

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Holmes, L. P. Gtpase protocols: The ras superfamily. [Place of publication not identified]: Humana, 2010.

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Der, Channing, ed. RAS Family GTPases. Dordrecht: Springer Netherlands, 2006. http://dx.doi.org/10.1007/1-4020-4708-8.

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Carlos, Lacal Juan, and McCormick Frank 1950-, eds. The Ras superfamily of GTPases. Boca Raton: CRC Press, 1993.

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1949-, Balch William Edward, Der Channing J. 1953-, and Hall A, eds. Small GTPases and their regulators. San Diego: Academic Press, 1995.

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1949-, Balch William Edward, Der Channing J, and Hall A, eds. Regulators and effectors of small GTPases. San Diego, CA: Academic Press, 2001.

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1949-, Balch William Edward, Der Channing J, and Hall A, eds. Regulators and effectors of small GTPases. San Diego: Academic Press, 2000.

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Book chapters on the topic "Rag GTPase"

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Jewell, Jenna L., and Kun-Liang Guan. "Rag GTPases." In Ras Superfamily Small G Proteins: Biology and Mechanisms 2, 277–92. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-07761-1_12.

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Konstantinidis, Diamantis G., and Theodosia A. Kalfa. "Rac GTPase." In Encyclopedia of Signaling Molecules, 4408–14. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_597.

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Konstantinidis, Diamantis G., and Theodosia A. Kalfa. "Rac GTPase." In Encyclopedia of Signaling Molecules, 1–7. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4614-6438-9_597-1.

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Knaus, Ulla G., Alison Bamberg, and Gary M. Bokoch. "Rac and Rap GTPase Activation Assays." In Neutrophil Methods and Protocols, 59–67. Totowa, NJ: Humana Press, 2007. http://dx.doi.org/10.1007/978-1-59745-467-4_5.

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Morrison, Deborah K., and Ira O. Daar. "RAS and the RAF/MEK/ERK Cascade." In RAS Family GTPases, 67–93. Dordrecht: Springer Netherlands, 2006. http://dx.doi.org/10.1007/1-4020-4708-8_4.

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Martemyanov, Kirill A., Pooja Parameswaran, Irene Aligianis, Mark Handley, Marga Gual-Soler, Tomohiko Taguchi, Jennifer L. Stow, et al. "Rac GTPases." In Encyclopedia of Signaling Molecules, 1557–62. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_597.

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Bischoff, F. Ralf, and Herwig Ponstingl. "Ran Regulation by Ran GEF and Ran GAP." In The Small GTPase Ran, 163–76. Boston, MA: Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-1501-2_9.

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Rojas, Jose M., and Eugenio Santos. "Ras-Gefs and Ras Gaps." In RAS Family GTPases, 15–43. Dordrecht: Springer Netherlands, 2006. http://dx.doi.org/10.1007/1-4020-4708-8_2.

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Moore, Mary Shannon. "The Role of Ran in Nuclear Import." In The Small GTPase Ran, 1–13. Boston, MA: Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-1501-2_1.

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Scheffzek, Klaus, and Alfred Wittinghofer. "Structural Views of the Ran GTPase Cycle." In The Small GTPase Ran, 177–201. Boston, MA: Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-1501-2_10.

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Conference papers on the topic "Rag GTPase"

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Ortega-Molina, Ana, Cristina Lebrero-Fernández, Nerea Deleyto-Seldas, Alba Sanz, and Alejo Efeyan. "Abstract IA13: Oncogenic Rag GTPase signaling links cellular nutrients with the FL microenvironment." In Abstracts: AACR Virtual Meeting: Advances in Malignant Lymphoma; August 17-19, 2020. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/2643-3249.lymphoma20-ia13.

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Padi, Sathish K. R., Neha Singh, Ghassan Mouneimne, Andrew S. Kraft, and Koichi Okumura. "Abstract PR01: Phosphorylation of DEPDC5 by the Pim-1 protein kinase, a cancer driver, stimulates mTORC1 activity by regulating the DEPDC5- Rag GTPase interaction." In Abstracts: AACR Special Conference on Targeting PI3K/mTOR Signaling; November 30-December 8, 2018; Boston, MA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1557-3125.pi3k-mtor18-pr01.

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Mondal, Subhanjan, and Said A. Goueli. "Abstract B44: GTPase/GAP/GEF-Glo™: A bioluminescent system to measure GTPase, GAP, and GEF activities." In Abstracts: AACR Special Conference on RAS Oncogenes: From Biology to Therapy; February 24-27, 2014; Lake Buena Vista, FL. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1557-3125.rasonc14-b44.

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Osanai, Kazuhiro, Makoto Kobayashi, Junko Higuchi, Min Zhou, Jyongsu Huang, and Hirohisa Toga. "Aberrant Lung Surfactant Homeostasis In RAB38 Small Gtpase-Mutated Rat Lungs." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a5164.

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Choi, Byeong Hyeok, Changyan Chen, Mark Philips, and Wei Dai. "Abstract 3544: Ras GTPases are modified by SUMOylation." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-3544.

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Sahasrabudhe, Deepak M., and Jeremy Bechelli. "Abstract 4122: Ras GTPase activating like protein (IQGAP1) in human acute myelogenous leukemia." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-4122.

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Dykstra, Kaitlyn M., Cheryl L. Allen, and Sarah A. Holstein. "Abstract 4768: Determination of Rab GTPase-mediated pathways critical for the antimyeloma activity of Rab GGTase inhibitors." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-4768.

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Lu, Qun, Christi Boykin, Huchen Zhou, Amy Friesland, and Yan-Hua Chen. "Abstract A35: Targeting Ras downstream to control motions: Rho GTPases." In Abstracts: AACR Special Conference on RAS Oncogenes: From Biology to Therapy; February 24-27, 2014; Lake Buena Vista, FL. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1557-3125.rasonc14-a35.

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Smith, Steven C., Alexander S. Baras, Hong Wang, Charles R. Owens, and Dan Theodorescu. "Abstract 5063: Signatures of Ral GTPase status define key clinicopathologic characteristics and outcomes in cancer." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-5063.

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Gentry, Leanna R., Timothy D. Martin, David J. Reiner, and Channing J. Der. "Abstract A08: Mechanistic dissection of Ral GTPase signaling in driving KRAS-dependent pancreatic cancer growth." In Abstracts: AACR Special Conference on RAS Oncogenes: From Biology to Therapy; February 24-27, 2014; Lake Buena Vista, FL. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1557-3125.rasonc14-a08.

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Reports on the topic "Rag GTPase"

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Symons, Marc H. Role of Rac GTPases in Chemokine-Stimulated Breast Carcinoma. Fort Belvoir, VA: Defense Technical Information Center, July 2006. http://dx.doi.org/10.21236/ada457469.

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Leng, Jie. Role of RAC GTPases in Tumor Mobility and Metastasis. Fort Belvoir, VA: Defense Technical Information Center, July 1997. http://dx.doi.org/10.21236/ada337864.

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Delmer, Deborah P., Douglas Johnson, and Alex Levine. The Role of Small Signal Transducing Gtpases in the Regulation of Cell Wall Deposition Patterns in Plants. United States Department of Agriculture, August 1995. http://dx.doi.org/10.32747/1995.7570571.bard.

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The combined research of the groups of Delmer, Levine and Johnson has led to a number of interesting findings with respect to the function of the small GTPase Rac in plants and also opened up new leads for future research. The results have shown: 1) The Rac13 protein undergoes geranylgeranlyation and is also translocated to the plasma membrane as found for Rac in mammals; 2) When cotton Rac13 is highly- expressed in yeast, it leads to an aberrant phenotype reminiscent of mutants impaired in actin function, supporting a role for Rac13 in cytoskeletal organization; 3) From our searches, there is no strong evidence that plants contain homologs of the related CDC42 genes found in yeast and mammals; 4) We have identified a rather unique Rac gene in Arabidopsis that has unusual extensions at both the N- and C-terminal portions of the protein; 5) New evidence was obtained that an oxidative burst characterized by substantial and sustained production of H202 occurs coincident with the onset of secondary wall synthesis in cotton fibers. Further work indicates that the H202 produced may be a signal for the onset of this phase of development and also strongly suggests that Rac plays an important role in signaling for event. Since the secondary walls of plants that contain high levels of lignin and cellulose are the major source of biomass on earth, understanding what signals control this process may well in the future have important implications for manipulating the timing and extent of secondary wall deposition. 6) When the cotton Rac13 promoter is fused to the reporter gene GUS, expression patterns in Arabidopsis indicate very strong and specific expression in developing trichomes and in developing xyelm. Since both of these cell types are engaged in secondary wall synthesis, this further supports a role for Rac in signaling for onset of this process. Since cotton fibers are anatomically defined as trichomes, these data may also be quite useful for future studies in which the trichomes of Arabidopsis may serve as a model for cotton fiber development; the Rac promoter can therefore be useful to drive expression of other genes proposed to affect fiber development and study the effects on the process; 7) The Rac promoter has also been shown to be the best so far tested for use in development of a system for transient transformation of developing cotton fibers, a technique that should have many applications in the field of cotton biotechnology; 8) One candidate protein that may interact with Rac13 to be characterized further in the future is a protein kinase that may be analogous to the PAK kinase that is known to interact with Rac in mammals.
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Symons, Marc. Role of Rac GTPases in Chemokine-Stimulated Breast Carcinoma Metastasis. Fort Belvoir, VA: Defense Technical Information Center, January 2009. http://dx.doi.org/10.21236/ada502287.

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Cancelas, Jose. Inhibition of Rac GTPases in the Therapy of Chronic Myelogenous Leukemia. Fort Belvoir, VA: Defense Technical Information Center, April 2009. http://dx.doi.org/10.21236/ada510761.

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Chien, Yuchen. Critical Contribution of Ral GTPases to Growth and Survival of Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, April 2005. http://dx.doi.org/10.21236/ada435549.

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Dharmawardhane, Suranganie. Estrogen and the Dietary Phytoestrogen Resveratrol as Regulators of the Rho GTPase Rac in Breast Cancer Metastasis. Fort Belvoir, VA: Defense Technical Information Center, September 2011. http://dx.doi.org/10.21236/ada554793.

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Dharmawardhane, Suranganie. Estrogen and the Dietary Phytoestrogen Resveratrol as Regulators of the Rho GTPase Rac in Breast Cancer Research. Fort Belvoir, VA: Defense Technical Information Center, June 2009. http://dx.doi.org/10.21236/ada625286.

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Dharmawardhane, Suranganie. Estrogen and the Dietary Phytoestrogen Tesveratrol as Regulators of the Rho GTPase Rac in Breast Cancer Research. Fort Belvoir, VA: Defense Technical Information Center, June 2010. http://dx.doi.org/10.21236/ada625290.

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Cheng, Tzuling. Critical Contribution of RAL GTPases to Growth and Survival of Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, April 2007. http://dx.doi.org/10.21236/ada477979.

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