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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1994-8-18
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pubmed:abstractText |
An in vitro assay that measures endosome fusion was used to characterize the role of guanosine triphosphate (GTP)-binding proteins in endocytosis. Guanosine 5',3-(thio)triphosphate (GTP gamma S), a nonhydrolyzable analog of GTP, stimulates the binding of cytosolic factors to the endosomal membrane (priming). GTP gamma S also enhances vesicle aggregation, resulting in the formation of an intermediate that is resistant to dilution. In this report we demonstrate that priming precedes the appearance of a dilution-resistant intermediate. Thus, GTP-binding proteins are involved in multiple sequential events preceding endosome fusion. Both heterotrimeric G proteins (G proteins) and ADP-ribosylation factors (ARFs) are GTP-binding proteins that regulate undefined steps involved in endocytosis. The addition of G beta gamma subunits of G proteins to the in vitro fusion assay resulted in inhibition of priming. In contrast, addition of ARF to the assay enhanced priming. Thus, heterotrimeric G proteins and ARF may regulate endocytosis by mediating the binding of cytosolic factor(s) required for fusion to the endosomal membrane. Taken together, the results show that multiple GTP-binding proteins regulate a series of distinct biochemical events required for endosome fusion.
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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/ADP-Ribosylation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine 5'-O-(3-Thiotriphosphate),
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0003-9861
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
312
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
474-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8037460-ADP-Ribosylation Factors,
pubmed-meshheading:8037460-Animals,
pubmed-meshheading:8037460-Biological Transport,
pubmed-meshheading:8037460-Cell Line,
pubmed-meshheading:8037460-Endocytosis,
pubmed-meshheading:8037460-GTP-Binding Proteins,
pubmed-meshheading:8037460-Guanosine 5'-O-(3-Thiotriphosphate),
pubmed-meshheading:8037460-Intracellular Membranes,
pubmed-meshheading:8037460-Membrane Fusion,
pubmed-meshheading:8037460-Mice,
pubmed-meshheading:8037460-Peptide Fragments
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pubmed:year |
1994
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pubmed:articleTitle |
Heterotrimeric GTP-binding proteins (G proteins) and ADP-ribosylation factor (ARF) regulate priming of endosomal membranes for fusion.
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pubmed:affiliation |
Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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