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dc.contributor.authorCantor, Sharon B.
dc.contributor.authorUrano, Takeshi
dc.contributor.authorFeig, Larry A.
dc.date2022-08-11T08:08:02.000
dc.date.accessioned2022-08-23T15:40:02Z
dc.date.available2022-08-23T15:40:02Z
dc.date.issued1995-08-01
dc.date.submitted2008-12-10
dc.identifier.citation<p>Mol Cell Biol. 1995 Aug;15(8):4578-84.</p>
dc.identifier.issn0270-7306 (Print)
dc.identifier.doi10.1128/mcb.15.8.4578
dc.identifier.pmid7623849
dc.identifier.urihttp://hdl.handle.net/20.500.14038/26310
dc.description.abstractRal 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.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=7623849&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC230698
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectBase Sequence
dc.subjectBlotting, Northern
dc.subjectCarrier Proteins
dc.subjectCell Cycle Proteins
dc.subjectCells, Cultured
dc.subjectDNA, Complementary
dc.subjectFungal Proteins
dc.subjectGTP Phosphohydrolases
dc.subjectGTP-Binding Proteins
dc.subject*GTPase-Activating Proteins
dc.subjectGene Library
dc.subjectImmunoblotting
dc.subjectMolecular Sequence Data
dc.subjectProtein Binding
dc.subjectRats
dc.subjectRecombinant Proteins
dc.subjectSaccharomyces cerevisiae
dc.subjectSequence Analysis, DNA
dc.subjectSequence Homology, Amino Acid
dc.subject*Signal Transduction
dc.subjectcdc42 GTP-Binding Protein, Saccharomyces cerevisiae
dc.subjectral GTP-Binding Proteins
dc.subjectAmino Acids, Peptides, and Proteins
dc.subjectCancer Biology
dc.subjectNeoplasms
dc.titleIdentification and characterization of Ral-binding protein 1, a potential downstream target of Ral GTPases
dc.typeJournal Article
dc.source.journaltitleMolecular and cellular biology
dc.source.volume15
dc.source.issue8
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/cancerbiology_pp/9
dc.identifier.contextkey679287
html.description.abstract<p>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.</p>
dc.identifier.submissionpathcancerbiology_pp/9
dc.contributor.departmentDepartment of Cancer Biology
dc.source.pages4578-84


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