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Rim and Exocytosis: Rab3a-Binding and Secretion-Enhancing Domains Are Separate and Function Independently

dc.contributor.authorSun, Leien_US
dc.contributor.authorBittner, Mary A.en_US
dc.contributor.authorHolz, Ronald W.en_US
dc.date.accessioned2010-06-01T22:27:11Z
dc.date.available2010-06-01T22:27:11Z
dc.date.issued2002-10en_US
dc.identifier.citationSUN, LEI; BITTNER, MARY A.; HOLZ, RONALD W. (2002). "Rim and Exocytosis: Rab3a-Binding and Secretion-Enhancing Domains Are Separate and Function Independently." Annals of the New York Academy of Sciences 971(1 THE CHROMAFFIN CELL: TRANSMITTER BIOSYNTHESIS, STORAGE, RELEASE, ACTIONS, AND INFORMATICS: 11th INTERNATIONAL SYMPOSIUM ON CHROMAFFIN CELL BIOLOGY ): 244-247. <http://hdl.handle.net/2027.42/75443>en_US
dc.identifier.issn0077-8923en_US
dc.identifier.issn1749-6632en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/75443
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=12438124&dopt=citationen_US
dc.description.abstractRim1 has been identified in brain by its ability to bind Rab3a-GTP and has been postulated to be a Rab3a effector protein. Like Rabphilin3, another putative Rab3a effector protein, Rim1 modulates secretion and contains a zinc-finger and two C2 domains. We have investigated the structural basis for the ability of Rim1 to bind Rab3a-GTP and to stimulate exocytosis in chromaffin cells.en_US
dc.format.extent1083352 bytes
dc.format.extent3109 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.publisherBlackwell Publishing Ltden_US
dc.rights2002 New York Academy of Sciencesen_US
dc.subject.otherRim1en_US
dc.subject.otherRab3aen_US
dc.subject.otherRabphilin3en_US
dc.subject.otherSecretionen_US
dc.subject.otherExocytosisen_US
dc.titleRim and Exocytosis: Rab3a-Binding and Secretion-Enhancing Domains Are Separate and Function Independentlyen_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelScience (General)en_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Pharmacology, University of Michigan Medical School, Ann Arbor, Michigan, USAen_US
dc.identifier.pmid12438124en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/75443/1/j.1749-6632.2002.tb04468.x.pdf
dc.identifier.doi10.1111/j.1749-6632.2002.tb04468.xen_US
dc.identifier.sourceAnnals of the New York Academy of Sciencesen_US
dc.identifier.citedreferenceNovick, P. & P. Brennwald. 1993. Friends and family: the role of the Rab GTPases in vesicular traffic. Cell 75: 597 – 601.en_US
dc.identifier.citedreferenceBajjalieh, S.M. & R.H. Scheller. 1995. The biochemistry of neurotransmitter secretion. J. Biol. Chem. 270: 1971 – 1974.en_US
dc.identifier.citedreferenceNovick, P. & M. Zerial. 1997. The diversity of Rab proteins in vesicle transport. Curr. Opin. Cell Biol. 9: 496 – 504.en_US
dc.identifier.citedreferenceWang, Y., M. Okamoto, F. Schmitz, et al. 1997. Rim is a putative rab3 effector in regulating synaptic-vesicle fusion. Nature 388: 593 – 598.en_US
dc.identifier.citedreferenceWang, Y., S. Sugita & T.C. Sudhof. 2000. The RIM/NIM family of neuronal C2 domain proteins: interactions with Rab3 and a new class of Src homology 3 domain proteins. J. Biol. Chem. 275: 20033 – 20044.en_US
dc.identifier.citedreferenceShirataki, H., K. Kaibuchi, T. Sakoda, et al. 1993. Rabphilin-3A, a putative target protein for smg p25A/rab3A p25 small GTP-binding protein related to synaptotagmin. Mol. Cell. Biol. 13: 2061 – 2068.en_US
dc.identifier.citedreferenceChung, S-H., Y.T. Akai & R.W. Holz. 1995. Evidence that the rab3a-binding protein, rabphilin3a, enhances regulated secretion: studies in adrenal chromaffin cells. J. Biol. Chem. 270: 16714 – 16718.en_US
dc.identifier.citedreferenceChung, S-H., P. Stabila, I.G. Macara & R.W. Holz. 1997. Importance of the Rab3a-GTP binding domain for the intracellular stability and function of Rabphilin3a in secretion. J. Neurochem. 69: 164 – 173.en_US
dc.identifier.citedreferenceSun, L., M.A. Bittner & R.W. Holz. 2001. Rab3a binding and secretion-enhancing domains in Rim1 are separate and unique. J. Biol. Chem. 276: 12911 – 12917.en_US
dc.identifier.citedreferenceOstermeier, C. & A.T. Brunger. 1999. Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3a complexed with the effector domain of Rabphilin-3a. Cell 96: 363 – 374.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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