Importance of the Rab3a-GTP Binding Domain for the Intracellular Stability and Function of Rabphilin3a in Secretion
dc.contributor.author | Chung, Sul-Hee | en_US |
dc.contributor.author | Stabila, Paul | en_US |
dc.contributor.author | Macara, Ian G. | en_US |
dc.date.accessioned | 2010-04-01T15:51:38Z | |
dc.date.available | 2010-04-01T15:51:38Z | |
dc.date.issued | 1997-07 | en_US |
dc.identifier.citation | Chung, Sul-Hee; Stabila, Paul; Macara, Ian G. (1997). "Importance of the Rab3a-GTP Binding Domain for the Intracellular Stability and Function of Rabphilin3a in Secretion." Journal of Neurochemistry 69(1): 164-173. <http://hdl.handle.net/2027.42/66356> | en_US |
dc.identifier.issn | 0022-3042 | en_US |
dc.identifier.issn | 1471-4159 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/66356 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=9202307&dopt=citation | en_US |
dc.description.abstract | We had previously demonstrated that Rab3a-GTP inhibits and the Rab3a-binding protein Rabphilin3a enhances secretion in bovine chromaffin cells. In this study, we investigated the role of Rab3a-GTP binding in the intracellular expression and the function of Rabphilin3a in regulated exocytosis in bovine chromaffin cells. Using transient transfections, we found that a minimal domain, Rp(51 190), that inhibits secretion coincides with a minimal domain that effectively binds Rab3a-GTP and allows intracellular stability of the construct. This domain includes a cysteine-rich, Zn 2+ -binding domain whose integrity is also required for Rab3a-GTP binding and the ability to inhibit secretion. A Rabphilin3a mutant, containing both C2 domains but defective in Rab3a-GTP, and wild-type Rabphilin3a both localized to chromaffin granules and stimulated secretion similarly despite lessened intracellular expression of the mutant protein. The data are consistent with a sequence of events in which a Rab3a-GTP Rabphilin3a complex forms on the secretory granule as a precursor in a pathway that enhances secretion. The complex dissociates (perhaps because of GTP hydrolysis) to permit the enhancement of secretion by Rabphilin3a. | en_US |
dc.format.extent | 1277803 bytes | |
dc.format.extent | 3110 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | Blackwell Science Ltd | en_US |
dc.rights | Blackwell Science Inc | en_US |
dc.subject.other | Exocytosis | en_US |
dc.subject.other | Rabphilin3a | en_US |
dc.subject.other | Rab3a | en_US |
dc.subject.other | Adrenal Chromaffin Cells | en_US |
dc.title | Importance of the Rab3a-GTP Binding Domain for the Intracellular Stability and Function of Rabphilin3a in Secretion | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Neurosciences | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationother | Department of Pathology, University of Vermont College of Medicine, Burlington, Vermont, U.S.A. | en_US |
dc.identifier.pmid | 9202307 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/66356/1/j.1471-4159.1997.69010164.x.pdf | |
dc.identifier.doi | 10.1046/j.1471-4159.1997.69010164.x | en_US |
dc.identifier.source | Journal of Neurochemistry | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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