Relevant bibliographies by topics / Ral GTP-Binding Proteins

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Academic literature on the topic 'Ral GTP-Binding Proteins'

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Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Ral GTP-Binding Proteins"

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Cantor, S. B., T. Urano, and L. A. Feig. "Identification and characterization of Ral-binding protein 1, a potential downstream target of Ral GTPases." Molecular and Cellular Biology 15, no. 8 (August 1995): 4578–84. http://dx.doi.org/10.1128/mcb.15.8.4578.

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Ral proteins constitute a distinct family of Ras-related GTPases. Although similar to Ras in amino acid sequence, Ral proteins are activated by a unique nucleotide exchange factor and inactivated by a distinct GTPase-activating protein. Unlike Ras, they fail to promote transformed foci when activated versions are expressed in cells. To identify downstream targets that might mediate a Ral-specific function, we used a Saccharomyces cerevisiae-based interaction assay to clone a novel cDNA that encodes a Ral-binding protein (RalBP1). RalBP1 binds specifically to the active GTP-bound form of RalA and not to a mutant Ral with a point mutation in its putative effector domain. In addition to a Ral-binding domain, RalBP1 also contains a Rho-GTPase-activating protein domain that interacts preferentially with Rho family member CDC42. Since CDC42 has been implicated in bud site selection in S. cerevisiae and filopodium formation in mammalian cells, Ral may function to modulate the actin cytoskeleton through its interactions with RalBP1.
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Gupta, A., B. Bastani, P. Chardin, and K. A. Hruska. "Localization of ral, a small Mr GTP-binding protein, to collecting duct cells in bovine and rat kidney." American Journal of Physiology-Renal Physiology 261, no. 6 (December 1, 1991): F1063—F1070. http://dx.doi.org/10.1152/ajprenal.1991.261.6.f1063.

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Plasma membranes from bovine kidney cortex were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and transferred to nitrocellulose membranes. Blotting with [alpha-32P]GTP and [35S]GTP gamma S demonstrated specific binding to three and six distinct protein bands, respectively, in the 20,000- to 29,000-Mr range. This indicated the presence of small Mr GTP binding proteins (smg) in bovine kidney cortex. Only one smg with 28,000 Mr was labeled with hydrolysis-resistant GTP photoaffinity probe p3-(4-azidoanilido)-p1-5GTP (AAGTP). The major smg in platelet membranes that binds GTP on nitrocellulose blots has been identified as ral-Mr 29,000. With the use of an antiserum against the ral A gene product, one of the smg with Mr of 29,000 present in bovine renal cortical plasma membranes was identified as ral. Ral was absent from glomerular homogenate, suggesting that it is localized to the tubular segments of the nephron. Ral was detected only in the particulate fraction and not the cytosol. Further subcellular localization of ral was investigated by immunohistochemical staining. Anti-ral antibody immunostained the apical and basolateral membranes of cells in the cortical and medullary collecting ducts in a speckled pattern in the bovine kidney. In the rat kidney, however, uniform linear staining of cortical and medullary collecting ducts predominantly localized to the apical membrane was observed. To date, no function has been assigned to ral. Localization of the ral gene product to the collecting duct suggests a specific functional role for this GTP-binding protein.
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Bhullar, Rajinder P., Richard R. Clough, Juddy Kanungo, Sherif M. Elsaraj, and Ognjen Grujic. "Ral-GTPase interacts with the β1 subunit of Na+/K+-ATPase and is activated upon inhibition of the Na+/K+ pumpThis paper is one of a selection of papers published in this Special Issue, entitled The Cellular and Molecular Basis of Cardiovascular Dysfunction, Dhalla 70th Birthday Tribute." Canadian Journal of Physiology and Pharmacology 85, no. 3-4 (March 2007): 444–54. http://dx.doi.org/10.1139/y07-027.

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Na+/K+-ATPase functions as both an ion pump and a signal transducer. Cardiac glycosides partially inhibit Na+/K+-ATPase, causing activation of multiple interrelated growth pathways via the Na+/K+-ATPase/c-Src/epidermal growth factor receptor complex. Such pathways include Ras/MEK/ERK and Ral/RalGDS cascades, which can lead to cardiac hypertrophy. In search of novel Ral-GTPase binding proteins, we used RalB as the bait to screen a human testes cDNA expression library using the yeast 2-hybrid system. The results demonstrated that 1 of the RalB interacting clones represented the C-terminal region of the β1 subunit of Na+/K+-ATPase. Further analysis using the yeast 2-hybrid system and full-length β1 subunit of Na+/K+-ATPase confirmed the interaction with RalA and RalB. In vitro binding and pull-down assays demonstrated that the β1 subunit of Na+/K+-ATPase interacts directly with RalA and RalB. Ral-GTP pull-down assays demonstrated that short-term ouabain treatment of A7r5 cells, a rat aorta smooth muscle cell line, caused activation of Ral GTPase. Maximal activation was observed 10 min after ouabain treatment. Ouabain-mediated Ral activation was inhibited upon the stimulation of Na+/K+-ATPase activity by Ang II. We propose that Ral GTPase is involved in the signal transducing function of Na+/K+-ATPase and provides a possible molecular mechanism connecting Ral to cardiac hypertrophy during diseased conditions.
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Bauer, Bettina, Gladys Mirey, Ingrid R. Vetter, Juan A. Garcı́a-Ranea, Alfonso Valencia, Alfred Wittinghofer, Jacques H. Camonis, and Robbert H. Cool. "Effector Recognition by the Small GTP-binding Proteins Ras and Ral." Journal of Biological Chemistry 274, no. 25 (June 18, 1999): 17763–70. http://dx.doi.org/10.1074/jbc.274.25.17763.

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Wildey, G. M., M. Viggeswarapu, S. Rim, and J. K. Denker. "Isolation of cDNA Clones and Tissue Expression of Rat Ral A and Ral B GTP-Binding Proteins." Biochemical and Biophysical Research Communications 194, no. 1 (July 1993): 552–59. http://dx.doi.org/10.1006/bbrc.1993.1855.

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Karunanithi, Sheelarani, Tingting Xiong, Maeran Uhm, Dara Leto, Jingxia Sun, Xiao-Wei Chen, and Alan R. Saltiel. "A Rab10:RalA G protein cascade regulates insulin-stimulated glucose uptake in adipocytes." Molecular Biology of the Cell 25, no. 19 (October 2014): 3059–69. http://dx.doi.org/10.1091/mbc.e14-06-1060.

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Insulin-stimulated glucose uptake in fat and muscle is mediated by the major facilitative glucose transporter Glut4. Insulin controls the trafficking of Glut4 to the plasma membrane via regulation of a series of small G proteins, including RalA and Rab10. We demonstrate here that Rab10 is a bona fide target of the GTPase-activating protein AS160, which is inhibited after phosphorylation by the protein kinase Akt. Once activated, Rab10 can increase the GTP binding of RalA by recruiting the Ral guanyl nucleotide exchange factor, Rlf/Rgl2. Rab10 and RalA reside in the same pool of Glut4-storage vesicles in untreated cells, and, together with Rlf, they ensure maximal glucose transport. Overexpression of membrane-tethered Rlf compensates for the loss of Rab10 in Glut4 translocation, suggesting that Rab10 recruits Rlf to membrane compartments for RalA activation and that RalA is downstream of Rab10. Together these studies identify a new G protein cascade in the regulation of insulin-stimulated Glut4 trafficking and glucose uptake.
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Kikuchi, A., S. D. Demo, Z. H. Ye, Y. W. Chen, and L. T. Williams. "ralGDS family members interact with the effector loop of ras p21." Molecular and Cellular Biology 14, no. 11 (November 1994): 7483–91. http://dx.doi.org/10.1128/mcb.14.11.7483.

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Using a yeast two-hybrid system, we identified a novel protein which interacts with ras p21. This protein shares 69% amino acid homology with ral guanine nucleotide dissociation stimulator (ralGDS), a GDP/GTP exchange protein for ral p24. We designated this protein RGL, for ralGDS-like. Using the yeast two-hybrid system, we found that an effector loop mutant of ras p21 was defective in interacting with the ras p21-interacting domain of RGL, suggesting that this domain binds to ras p21 through the effector loop of ras p21. Since ralGDS contained a region highly homologous with the ras p21-interacting domain of RGL, we examined whether ralGDS could interact with ras p21. In the yeast two-hybrid system, ralGDS failed to interact with an effector loop mutant of ras p21. In insect cells, ralGDS made a complex with v-ras p21 but not with a dominant negative mutant of ras p21. ralGDS interacted with the GTP-bound form of ras p21 but not with the GDP-bound form in vitro. ralGDS inhibited both the GTPase-activating activity of the neurofibromatosis gene product (NF1) for ras p21 and the interaction of Raf with ras p21 in vitro. These results demonstrate that ralGDS specifically interacts with the active form of ras p21 and that ralGDS can compete with NF1 and Raf for binding to the effector loop of ras p21. Therefore, ralGDS family members may be effector proteins of ras p21 or may inhibit interactions between ras p21 and its effectors.
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Kikuchi, A., S. D. Demo, Z. H. Ye, Y. W. Chen, and L. T. Williams. "ralGDS family members interact with the effector loop of ras p21." Molecular and Cellular Biology 14, no. 11 (November 1994): 7483–91. http://dx.doi.org/10.1128/mcb.14.11.7483-7491.1994.

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Using a yeast two-hybrid system, we identified a novel protein which interacts with ras p21. This protein shares 69% amino acid homology with ral guanine nucleotide dissociation stimulator (ralGDS), a GDP/GTP exchange protein for ral p24. We designated this protein RGL, for ralGDS-like. Using the yeast two-hybrid system, we found that an effector loop mutant of ras p21 was defective in interacting with the ras p21-interacting domain of RGL, suggesting that this domain binds to ras p21 through the effector loop of ras p21. Since ralGDS contained a region highly homologous with the ras p21-interacting domain of RGL, we examined whether ralGDS could interact with ras p21. In the yeast two-hybrid system, ralGDS failed to interact with an effector loop mutant of ras p21. In insect cells, ralGDS made a complex with v-ras p21 but not with a dominant negative mutant of ras p21. ralGDS interacted with the GTP-bound form of ras p21 but not with the GDP-bound form in vitro. ralGDS inhibited both the GTPase-activating activity of the neurofibromatosis gene product (NF1) for ras p21 and the interaction of Raf with ras p21 in vitro. These results demonstrate that ralGDS specifically interacts with the active form of ras p21 and that ralGDS can compete with NF1 and Raf for binding to the effector loop of ras p21. Therefore, ralGDS family members may be effector proteins of ras p21 or may inhibit interactions between ras p21 and its effectors.
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Polakis, P. G., R. F. Weber, B. Nevins, J. R. Didsbury, T. Evans, and R. Snyderman. "Identification of the ral and rac1 Gene Products, Low Molecular Mass GTP-binding Proteins from Human Platelets." Journal of Biological Chemistry 264, no. 28 (October 1989): 16383–89. http://dx.doi.org/10.1016/s0021-9258(19)84717-8.

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Rosário, Marta, Hugh F. Paterson, and Christopher J. Marshall. "Activation of the Ral and Phosphatidylinositol 3′ Kinase Signaling Pathways by the Ras-Related Protein TC21." Molecular and Cellular Biology 21, no. 11 (June 1, 2001): 3750–62. http://dx.doi.org/10.1128/mcb.21.11.3750-3762.2001.

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ABSTRACT TC21 is a member of the Ras superfamily of small GTP-binding proteins that, like Ras, has been implicated in the regulation of growth-stimulating pathways. We have previously identified the Raf/mitogen-activated protein kinase pathway as a direct TC21 effector pathway required for TC21-induced transformation (M. Rosário, H. F. Paterson, and C. J. Marshall, EMBO J. 18:1270–1279, 1999). In this study we have identified two further effector pathways for TC21, which contribute to TC21-stimulated transformation: the phosphatidylinositol 3′ kinase (PI-3K) and Ral signaling pathways. Expression of constitutively active TC21 leads to the activation of Ral A and the PI-3K-dependent activation of Akt/protein kinase B. Strong activation of the PI-3K/Akt pathway is seen even with very low levels of TC21 expression, suggesting that TC21 may be a key small GTPase-regulator of PI-3K. TC21-induced alterations in cellular morphology in NIH 3T3 and PC12 cells are also PI-3K dependent. On the other hand, activation of the Ral pathway by TC21 is required for TC21-stimulated DNA synthesis but not transformed morphology. We show that inhibition of Ral signaling blocks DNA synthesis in human tumor cell lines containing activating mutations in TC21, demonstrating for the first time that this pathway is required for the proliferation of human tumor cells. Finally, we provide mechanisms for the activation of these pathways, namely, the direct in vivo interaction of TC21 with guanine nucleotide exchange factors for Ral, resulting in their translocation to the plasma membrane, and the direct interaction of TC21 with PI-3K. In both cases, the effector domain region of TC21 is required since point mutations in this region can interfere with activation of downstream signaling.
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Dissertations / Theses on the topic "Ral GTP-Binding Proteins"

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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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Falsetti, Samuel C. "The Role of RalA and RalB in Cancer." [Tampa, Fla] : University of South Florida, 2008. http://purl.fcla.edu/usf/dc/et/SFE0002307.

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Bramble, Sharyl Elizabeth. "Guanine nucleotide binding properties and attempted immunopurification of ras protein from dictyostelium discoideum." Thesis, University of British Columbia, 1987. http://hdl.handle.net/2429/26172.

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One purpose of this study was to determine whether the ras protein from Dictyostelium discoideum (p23) binds guanine nucleotides like the ras proteins from mammals (p21) and yeast. The other purpose of this investigation was to purify or enrich for p23ras from D. discoideum by immunoaffinity chromatography. A number of different approaches were used to determine guanine nucleotide binding by p23RAS . A simple filter binding assay, binding to Western blots, and photoaffinity labeling all failed to demonstrate specific binding with lysates of D. discoideum cells. In contrast p21RAS from transformed NIH-3T3 cell lysate was successfully photoaffinity labeled in the presence of ³²P-α-guanosine 5¹-triphosphate (GTP) suggesting that the technique had been performed correctly. It was concluded that either p23RAS has a very low affinity for guanine nucleotides such that GTP binding was not detectable in these experiments or that the ras protein from D. discoideum simply does not bind guanine nucleotides. The purification of p23RAS from D. discoideum cells was attempted in order to provide a purified protein preparation for guanine nucleotide binding and for reconstitution studies. An anti-ras monoclonal antibody (Y13-259) was used as the ligand for the immunoaffinity chromatography. This approach was not successful in that the ras protein could not be enriched relative to other proteins because the immunoaffinity columns did not bind p23RAS.
Science, Faculty of
Microbiology and Immunology, Department of
Graduate
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4

Gibson, Janet Rae. "A study of RAS p21 and related GTP-binding proteins." Thesis, University of East Anglia, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.293243.

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Seibold, Marcel [Verfasser], Ralf C. [Gutachter] Bargou, and Thomas [Gutachter] Dandekar. "Funktionelle Charakterisierung des Ras family small GTP binding protein RAL im Multiplen Myelom / Marcel Seibold ; Gutachter: Ralf C. Bargou, Thomas Dandekar." Würzburg : Universität Würzburg, 2020. http://d-nb.info/1214181007/34.

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Seibold, Marcel Verfasser], Ralf C. [Gutachter] [Bargou, and Thomas [Gutachter] Dandekar. "Funktionelle Charakterisierung des Ras family small GTP binding protein RAL im Multiplen Myelom / Marcel Seibold ; Gutachter: Ralf C. Bargou, Thomas Dandekar." Würzburg : Universität Würzburg, 2020. http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-208003.

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Scapin, Sandra Mara Naressi. "Analises estruturais de GTPases da familia RAB e mecanismo de regulção de MAFB pela proteina TIPRL." [s.n.], 2007. http://repositorio.unicamp.br/jspui/handle/REPOSIP/317183.

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Orientadores: Nilson Ivo Tonin Zanchin, Beatriz Gomes Guimaraes
Tese (doutorado) - Universidade Estadual de Campinas, Instituto de Biologia
Made available in DSpace on 2018-08-09T09:39:45Z (GMT). No. of bitstreams: 1 Scapin_SandraMaraNaressi_D.pdf: 11335048 bytes, checksum: 153f9eea9142fb7f3cb17de59a608da6 (MD5) Previous issue date: 2007
Resumo: As GTPases da família Rab regulam o transporte intracelular de vesículas em eucariotos. Cada Rab atua em uma via de transporte específica e seu mecanismo de ação se dá através da realização de um ciclo de ligação e hidrólise de GTP. Neste trabalho, foi determinada a estrutura cristalográfica das formas inativa (ligada a GDP) e ativa (ligada a GppNHp) da GTPase Rab11b, um membro da subfamília Rab11 que está envolvida na reciclagem de proteínas dos endossomos para a membrana plasmática, no tráfego de vesículas da rede trans-Golgi para a membrana plasmática e na fagocitose. Os resultados foram confrontados com os dados estruturais da Rab11a descritos anteriormente. A Rab11b inativa cristalizou como um monômero, o que gera conflitos a respeito da formação de dímeros funcionais pela Rab11a. A Rab11b e a Rab11a ativas divergiram em relação à posição e à interação da serina 20, que é importante na hidrólise de GTP, mas apresentaram taxas hidrolíticas semelhantes in vitro. Visando uma investigação mais ampla da família Rab, a GTPase Rab21 também foi cristalizada, mas os cristais difrataram até 2.90 Å de resolução. Ensaios de desnaturação térmica revelaram que a Rab21 é estruturalmente mais instável do que a Rab11, talvez pela presença de cisteínas que estão susceptíveis à oxidação, contribuindo para a agregação e precipitação da proteína. A Rab11 é bastante estável, e possivelmente forma estruturas do tipo beta-amilóide em altas temperaturas. Este trabalho envolveu também o estudo funcional da interação entre a proteína TIP41 humana (TIPRL) e o fator de transcrição MafB. A TIPRL é uma proteína conservada que foi identificada como uma ativadora de MAP quinases enquanto sua homóloga em levedura foi caracterizada como um antagonista da via de sinalização da quinase TOR que regula o crescimento celular. A MafB está envolvida no controle transcricional em diversos processos de desenvolvimento, mas seus reguladores ainda não estão bem estabelecidos. A interação direta entre a TIPRL e a MafB inteira, ou seu domínio bZIP isolado, foi confirmada através de ensaios de ligação in vitro. As proteínas co-localizaram no núcleo de células HEK293 e nossos resultados preliminares mostram que a TIPRL inibe a atividade transcricional da MafB in vivo, embora apenas interfira na ligação in vitro do domínio bZIP da MafB ao seu DNA-alvo mediante a estabilização do complexo TIPRL-bZIP. A TIPRL pode, portanto, constituir um novo regulador da atividade de MafB
Abstract: GTPases of the Rab family are responsible for the intracellular transport of vesicles. Each family member acts on a specific transport pathway and their function is regulated by GTP binding and hydrolysis, cycling between inactive (GDP-bound) and active (GTP-bound) forms. In this work, we describe the crystal structure of inactive and active forms of the GTPase Rab11b, a member of the Rab11 subfamily which is involved in recycling of proteins from endosomes to the plasma membrane, in polarized transport in epithelial cells, in the transport of molecules of the trans-Golgi network to the plasma membrane and in phagocytosis. The Rab11b structure showed several differences from the Rab11a isoform previously described. Inactive Rab11b crystallized as a monomer, contradicting the hypothesis about functional dimers formed by Rab11a. Active Rab11b differ from Rab11a relative to the position of the serine 20 sidechain, which is involved in GTP hydrolysis, although both GTPases show similar GTP hydrolysis rates in vitro. In order to obtain structural information on Rab GTPases, Rab21 was also crystallized, but the crystals diffracted to a relatively low resolution (2.90 Å). Rab21 is a cysteine rich protein, showing a higher instability relative to Rab11b. Thermal unfolding followed by circular dicroism confirmed this hypothesis. Both Rab11b and Rab11a show a relatively high thermal stability and circular dicroism analysis indicate that they undergo conversion to structures rich in beta-strands upon thermal denaturation. This work includes also studies on the function of TIPRL in regard to its interaction with the transcription factor MafB. TIPRL is a conserved human protein identified as an activator of MAP kinases whereas its yeast counterpart Tip41 functions as an antagonist of the TOR kinase pathway. MafB is a large member of the Maf family of bZIP transcription factors controlling developmental processes in vertebrates. Regulation of MafB is critical, for example, during erythroid differentiation. A direct interaction between TIPRL and full length MafB and the bZIP domain of MafB was confirmed by in vitro interaction assays. TIPRL is localized throughout the whole cell and overlaps with MafB in the nucleus of HEK293 cells. Preliminary assays showed that TIPRL inhibits transcriptional activation mediated by MafB in HEK293 cells, although MafB shows a higher binding affinity to its target DNA relative to TIPRL in vitro. This evidence indicates that TIPRL may control MafB activity in vivo
Doutorado
Genetica Animal e Evolução
Doutor em Genetica e Biologia Molecular
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8

Tuxworth, Richard Ian. "The control of cell motility and differentiation by Ras pathways." Thesis, University College London (University of London), 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.314227.

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Self, Annette Jane. "Structural and functional analysis of Ras and Ruo-related small GTP-binding proteins." Thesis, Institute of Cancer Research (University Of London), 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.266353.

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Diekmann, Dagmar. "Structural and functional analysis of the small GTP-binding proteins rho and rac." Thesis, Institute of Cancer Research (University Of London), 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.283195.

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Books on the topic "Ral GTP-Binding Proteins"

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Marino, Zerial, and Huber Lukas A, eds. Guidebook to the small GTPases. Oxford: Oxford University Press, 1995.

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(Editor), W. E. Balch, Channing J. Der (Editor), and Alan Hall (Editor), eds. Regulators and Effectors of Small GTPases, Part G: Ras Family II (Methods in Enzymology, Vol 333) (Methods in Enzymology). Academic Press, 2001.

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(Editor), W. E. Balch, Channing J. Der (Editor), and Alan Hall (Editor), eds. Regulators and Effectors of Small GTPases, Part G: Ras Family II (Methods in Enzymology, Vol 333) (Methods in Enzymology). 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, 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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(Editor), John N. Abelson, Melvin I. Simon (Editor), W. E. Balch (Editor), Channing J. Der (Editor), and Alan Hall (Editor), eds. Methods in Enzymology, Volume 332: Regulators and Effectors of Small GTPases, Part F: Ras Family I (Methods in Enzymology). 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, 2001.

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(Editor), W. E. Balch, Channing J. Der (Editor), Alan Hall (Editor), John N. Abelson (Series Editor), and Melvin I. Simon (Series Editor), eds. Regulators and Effectors of Small GTPases, Part E: GTPases (Methods in Enzymology). Academic Press, 2001.

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Book chapters on the topic "Ral GTP-Binding Proteins"

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Pizon, V., P. Chardin, I. Lerosey, and A. Tavitian. "The rap Proteins : GTP Binding Proteins Related to p21 ras with a Possible Reversion Effect on ras Transformed Cells." In ras Oncogenes, 83–91. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4757-1235-3_13.

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Bucci, Cecilia, Rodolfo Frunzio, Lorenzo Chiariotti, Alexandra L. Brown, Matthew M. Rechler, and Carmelo B. Bruni. "Isolation and Partial Characterization of a New Gene (br1) Belonging to the Superfamily of the Small GTP-Binding Proteins." In ras Oncogenes, 287–96. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4757-1235-3_38.

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Lanoix, Joël, and Jacques Paiement. "Low Molecular Weight GTP-binding Proteins in Rough Endoplasmic Reticulum Membranes from Rat Liver and Rat Hepatocellular Carcinomas." In Molecular Mechanisms of Membrane Traffic, 405–7. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-662-02928-2_85.

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Gallwitz, D., J. Becker, M. Benli, L. Hengst, C. Mosrin-Huaman, M. Mundt, T. J. Tan, P. Vollmer, and H. Wichmann. "The YPT-Branch of the ras Superfamily of GTP-Binding Proteins in Yeast: Functional Importance of the Putative Effector Region." In The Superfamily of ras-Related Genes, 121–28. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4684-6018-6_14.

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Cevher-Keskin, Birsen. "Endomembrane Trafficking in Plants." In Electrodialysis. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.91642.

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The functional organization of eukaryotic cells requires the exchange of proteins, lipids, and polysaccharides between membrane compartments through transport intermediates. Small GTPases largely control membrane traffic, which is essential for the survival of all eukaryotes. Transport from one compartment of this pathway to another is mediated by vesicular carriers, which are formed by the controlled assembly of coat protein complexes (COPs) on donor organelles. The activation of small GTPases is essential for vesicle formation from a donor membrane. In eukaryotic cells, small GTP-binding proteins comprise the largest family of signaling proteins. The ADP-ribosylation factor 1 (ARF1) and secretion-associated RAS superfamily 1 (SAR1) GTP-binding proteins are involved in the formation and budding of vesicles throughout plant endomembrane systems. ARF1 has been shown to play a critical role in coat protein complex I (COPI)-mediated retrograde trafficking in eukaryotic systems, whereas SAR1 GTPases are involved in intracellular coat protein complex II (COPII)-mediated protein trafficking from the endoplasmic reticulum (ER) to the Golgi apparatus. The dysfunction of the endomembrane system can affect signal transduction, plant development, and defense. This chapter offers a summary of membrane trafficking system with an emphasis on the role of GTPases especially ARF1, SAR1, and RAB, their regulatory proteins, and interaction with endomembrane compartments. The vacuolar and endocytic trafficking are presented to enhance our understanding of plant development and immunity in plants.
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Simons, Peter, and Charlotte M. Vines. "Analysis of GTP-Binding Protein–Coupled Receptor Assemblies by Flow Cytometry." In Flow Cytometry for Biotechnology. Oxford University Press, 2005. http://dx.doi.org/10.1093/oso/9780195183146.003.0022.

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GTP-binding protein–coupled receptors (GPCRs) represent the largest family of integral membrane signal-transducing molecules in the human genome, with estimates of at least 600 members. As such, they represent the targets of approximately 30%–50% of the prescription drugs on the market. They are involved in virtually every physiological process in the human body, with ligands including light, odorants, amines, peptides, proteins, lipids, and nucleotides. Binding of these ligands on the extracellular surface of the receptor leads to conformational changes within the receptor, resulting in a multitude of cellular responses. GPCRs, as their name implies, function through the actions of heterotrimeric GTP-binding proteins (G proteins). These G proteins then couple to a diverse array of effector molecules at the cell surface and inside the cell. GPCRs contain a common structural motif, with seven transmembrane alpha helices. With the recent description of the three-dimensional crystal structure of rhodopsin in its inactive state, a greater, though still incomplete, understanding of the functions of this receptor family has been achieved. In addition to the activation of G proteins, GPCRs undergo extensive regulation mediated primarily by a variety of kinases, including second messenger kinases and the family of G protein–coupled receptor kinases (GRKs). Following receptor phosphorylation by GRKs, additional proteins named arrestins associate with GPCRs. The traditional role of these molecules has been to serve as desensitizing agents, preventing further association of the receptor with G proteins. However, recent studies have demonstrated that arrestins can serve as adapters in the process of receptor internalization as well as scaffolds in the activation of numerous kinase pathways. Interactions between GPCRs and cellular proteins such as adaptins, rab GTPases, phosphatases, and ion channels have also been described. Thus, it has become apparent that understanding the interactions between GPCRs and their associated proteins is critical for any detailed understanding of receptor function. An overview of the activation and regulation of GPCRs is shown in figure 17.1 to provide a context for the approaches to be described in the remainder of this chapter.
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Scheffler, Julie E., Susan E. Kiefer, Kathleen Prinzo, and Eva Bekesi. "Scintillation proximity assay to measure the binding of ras-GTP to the ras-binding domain of c-Raf-1." In Techniques in Protein Chemistry, 101–6. Elsevier, 1996. http://dx.doi.org/10.1016/s1080-8914(96)80014-7.

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Porfiri, Emilio, and John F. Hancock. "[10] Stimulation of nucleotide exchange on Ras- and Rho-related proteins by small GTP-binding protein GDP dissociation stimulator." In Small GTPases and Their Regulators Part B: Rho Family, 85–90. Elsevier, 1995. http://dx.doi.org/10.1016/0076-6879(95)56012-2.

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