Source:http://linkedlifedata.com/resource/pubmed/id/14731509
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
2004-1-20
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pubmed:abstractText |
Small GTP-binding proteins of the Ras superfamily play diverse roles in intracellular trafficking. In order to perform these functions, the proteins must associate with specific donor vesicles and be recycled after fusion of these vesicles with their acceptor membrane target. Recent results have identified a number of lipid modifications of these proteins, occurring at the N- or C-termini, that contribute to their membrane binding. Recycling appears, in some cases, to be mediated by soluble proteins that bind the lipid-modified tails, removing them from the membrane and allowing their reutilization via the cytosol.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:status |
PubMed-not-MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0962-8924
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
318-23
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pubmed:year |
1992
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pubmed:articleTitle |
The role of lipid anchors for small G proteins in membrane trafficking.
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pubmed:affiliation |
Laboratory of Eukaryotic Molecular Genetics, National Institute for Medical Research, Mill Hill, London, UK.
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pubmed:publicationType |
Journal Article
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