| pubmed-article:10859313 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10859313 | lifeskim:mentions | umls-concept:C0205474 | lld:lifeskim |
| pubmed-article:10859313 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:10859313 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:10859313 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:10859313 | lifeskim:mentions | umls-concept:C2348205 | lld:lifeskim |
| pubmed-article:10859313 | pubmed:issue | 41 | lld:pubmed |
| pubmed-article:10859313 | pubmed:dateCreated | 2000-11-13 | lld:pubmed |
| pubmed-article:10859313 | pubmed:abstractText | Small G proteins of the Rab family are regulators of intracellular vesicle traffic. Their intrinsic rate of GTP hydrolysis is very low but is enhanced by specific GTPase-activating proteins (GAPs) that switch G proteins to their inactive form. We have characterized the activity of recombinant Rab3-GAP on Rab3A in solution. The K(m) and K(d) values (75 microm) indicate a low affinity of Rab3-GAP for its substrate. The affinity is higher for the transition state analog Rab3A:GDP:AlF(x) (15 microm). The k(cat) (1 s(-)(1)) is within the range of values reported for other GAPs. A mutation in the switch I region of Rab3A disrupted the interaction with Rab3-GAP. Furthermore, Rabphilin, a putative target of Rab3, inhibited the activity of Rab3-GAP on Rab3. Therefore, the Rab3-GAP-binding site involves the switch I region of Rab3 and overlaps with the Rabphilin-binding domain. Substitution of a single arginine residue (Arg-728) of Rab3-GAP disrupted its catalytic activity but not its interaction with Rab3A. We propose that Rab3-GAP, like Ras- and Rho-GAPs, stabilizes the transition state of Rab3 and provides a critical arginine residue to accelerate the GTPase reaction. | lld:pubmed |
| pubmed-article:10859313 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10859313 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10859313 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10859313 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10859313 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10859313 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10859313 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:10859313 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10859313 | pubmed:author | pubmed-author:HenryJ PJP | lld:pubmed |
| pubmed-article:10859313 | pubmed:author | pubmed-author:DarchenFF | lld:pubmed |
| pubmed-article:10859313 | pubmed:author | pubmed-author:ClabecqAA | lld:pubmed |
| pubmed-article:10859313 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10859313 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:10859313 | pubmed:volume | 275 | lld:pubmed |
| pubmed-article:10859313 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10859313 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10859313 | pubmed:pagination | 31786-91 | lld:pubmed |
| pubmed-article:10859313 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:10859313 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10859313 | pubmed:articleTitle | Biochemical characterization of Rab3-GTPase-activating protein reveals a mechanism similar to that of Ras-GAP. | lld:pubmed |
| pubmed-article:10859313 | pubmed:affiliation | CNRS UPR 1929, Institut de Biologie Physico-Chimique, 13 rue P. et M. Curie, 75005 Paris, France. | lld:pubmed |
| pubmed-article:10859313 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10859313 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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