| pubmed-article:9034329 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9034329 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:9034329 | lifeskim:mentions | umls-concept:C0752065 | lld:lifeskim |
| pubmed-article:9034329 | lifeskim:mentions | umls-concept:C0752093 | lld:lifeskim |
| pubmed-article:9034329 | lifeskim:mentions | umls-concept:C0012727 | lld:lifeskim |
| pubmed-article:9034329 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:9034329 | lifeskim:mentions | umls-concept:C0030685 | lld:lifeskim |
| pubmed-article:9034329 | lifeskim:mentions | umls-concept:C1152881 | lld:lifeskim |
| pubmed-article:9034329 | lifeskim:mentions | umls-concept:C0680255 | lld:lifeskim |
| pubmed-article:9034329 | lifeskim:mentions | umls-concept:C0391871 | lld:lifeskim |
| pubmed-article:9034329 | lifeskim:mentions | umls-concept:C1283071 | lld:lifeskim |
| pubmed-article:9034329 | lifeskim:mentions | umls-concept:C1963578 | lld:lifeskim |
| pubmed-article:9034329 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:9034329 | pubmed:dateCreated | 1997-3-13 | lld:pubmed |
| pubmed-article:9034329 | pubmed:abstractText | Prenylated Rab GTPases occur in the cytosol in their GDP-bound conformations bound to a cytosolic protein termed GDP-dissociation inhibitor (GDI). Rab-GDI complexes represent a pool of active, recycling Rab proteins that can deliver Rabs to specific and distinct membrane-bound compartments. Rab delivery to cellular membranes involves release of GDI, and the membrane-associated Rab protein then exchanges its bound GDP for GTP. We report here the identification of a novel, membrane-associated protein factor that can release prenylated Rab proteins from GDI. This GDI-displacement factor (GDF) is not a guanine nucleotide exchange factor because it did not influence the intrinsic rates of nucleotide exchange by Rabs 5, 7 or 9. Rather, GDF caused the release of each of these endosomal Rabs from GDI, permitting them to exchange nucleotide at their intrinsic rates. GDF displayed the greatest catalytic rate enhancement on Rab9-GDI complexes. However, catalytic rate enhancement paralleled the potency of GDI in blocking nucleotide exchange: GDI was shown to be most potent in blocking nucleotide exchange by Rab9. The failure of GDF to act on Rab1-GDI complexes suggests that it may be specific for endosomal Rab proteins. This novel, membrane-associated activity may be part of the machinery used to localize Rabs to their correct intracellular compartments. | lld:pubmed |
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| pubmed-article:9034329 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9034329 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9034329 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9034329 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:9034329 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:9034329 | pubmed:author | pubmed-author:PfefferS RSR | lld:pubmed |
| pubmed-article:9034329 | pubmed:author | pubmed-author:SumizawaTT | lld:pubmed |
| pubmed-article:9034329 | pubmed:author | pubmed-author:Dirac-Svejstr... | lld:pubmed |
| pubmed-article:9034329 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9034329 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:9034329 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:9034329 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9034329 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9034329 | pubmed:pagination | 465-72 | lld:pubmed |
| pubmed-article:9034329 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:9034329 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9034329 | pubmed:articleTitle | Identification of a GDI displacement factor that releases endosomal Rab GTPases from Rab-GDI. | lld:pubmed |
| pubmed-article:9034329 | pubmed:affiliation | Department of Biochemistry, Stanford University School of Medicine, CA 94305-5307, USA. | lld:pubmed |
| pubmed-article:9034329 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9034329 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9034329 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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