Source:http://linkedlifedata.com/resource/pubmed/id/16473600
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2006-2-13
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pubmed:abstractText |
Guanine nucleotide dissociation inhibitor (GDI) is a central regulator of Rab GTPase family members. GDI recycles Rab proteins from the membrane and sequesters the inactive GDP-bound form of Rab in the cytosol for use in multiple rounds of transport. The balance between the membrane-bound form of Rab and the cytosolic reserve pool of the Rab-GDI complex is critical for vesicular trafficking between membrane compartments. Recycling of Rab GTPases is likely to require a membrane-bound complex of GDI, Hsp90, and Rab given that alphaGDI-dependent recycling of Rab3A at the synapse and neurotransmitter transmitter release is inhibited by Hsp90-specific inhibitors. Here we describe methods required for establishing the dependence of Rab recycling pathways on Hsp90 in vitro.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Dissociation...,
http://linkedlifedata.com/resource/pubmed/chemical/HSP90 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/rab3 GTP-Binding Proteins
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pubmed:status |
MEDLINE
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pubmed:issn |
0076-6879
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
403
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
339-47
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16473600-Animals,
pubmed-meshheading:16473600-Cells, Cultured,
pubmed-meshheading:16473600-Guanine Nucleotide Dissociation Inhibitors,
pubmed-meshheading:16473600-HSP90 Heat-Shock Proteins,
pubmed-meshheading:16473600-Rats,
pubmed-meshheading:16473600-Recombinant Proteins,
pubmed-meshheading:16473600-Synaptosomes,
pubmed-meshheading:16473600-rab3 GTP-Binding Proteins
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pubmed:year |
2005
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pubmed:articleTitle |
Use of Hsp90 inhibitors to disrupt GDI-dependent Rab recycling.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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