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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
29
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pubmed:dateCreated |
2001-7-17
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pubmed:abstractText |
FYVE domains are small zinc-finger-like domains found in many proteins that are involved in regulating membrane traffic and have been shown to bind specifically to phosphatidylinositol 3-phosphate (PtdIns-3-P). FYVE domains are thought to recruit PtdIns-3-P effectors to endosomal locations in vivo, where these effectors participate in controlling endosomal maturation and vacuolar protein sorting. We have compared the characteristics of PtdIns-3-P binding by the FYVE domain from Hrs-1 (the hepatocyte growth factor-regulated tyrosine kinase substrate) with those of specific phosphoinositide binding by Pleckstrin homology (PH) domains. Like certain PH domains (such as that from phospholipase C-delta(1)), the Hrs-1 FYVE domain specifically recognizes a single phosphoinositide. However, while phosphoinositide binding by highly specific PH domains is driven almost exclusively by interactions with the lipid headgroup, this is not true for the Hrs-1 FYVE domain. The phospholipase C-delta(1) PH domain shows a 10-fold preference for binding isolated headgroup over its preferred lipid (phosphatidylinositol 4,5-bisphosphate) in a membrane, while the Hrs-1 FYVE domain greatly prefers (more than 50-fold) intact lipid in a bilayer over the isolated headgroup (inositol 1,3-bisphosphate). By contrast with reports for certain PH domains, we find that this preference for membrane binding over interaction with soluble lipid headgroups does not require FYVE domain oligomerization.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cation Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/FGD1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Liposomes,
http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharide Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RSC1A1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Symporters,
http://linkedlifedata.com/resource/pubmed/chemical/phosphatidylinositol 3-phosphate,
http://linkedlifedata.com/resource/pubmed/chemical/platelet protein P47
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0006-2960
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
40
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8581-7
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pubmed:dateRevised |
2009-7-17
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pubmed:meshHeading |
pubmed-meshheading:11456498-Binding, Competitive,
pubmed-meshheading:11456498-Blood Proteins,
pubmed-meshheading:11456498-Carrier Proteins,
pubmed-meshheading:11456498-Cation Transport Proteins,
pubmed-meshheading:11456498-Glutathione Transferase,
pubmed-meshheading:11456498-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:11456498-HeLa Cells,
pubmed-meshheading:11456498-Humans,
pubmed-meshheading:11456498-Liposomes,
pubmed-meshheading:11456498-Monosaccharide Transport Proteins,
pubmed-meshheading:11456498-Phosphatidylinositol Phosphates,
pubmed-meshheading:11456498-Phospholipids,
pubmed-meshheading:11456498-Phosphoproteins,
pubmed-meshheading:11456498-Protein Binding,
pubmed-meshheading:11456498-Protein Structure, Tertiary,
pubmed-meshheading:11456498-Proteins,
pubmed-meshheading:11456498-Recombinant Fusion Proteins,
pubmed-meshheading:11456498-Symporters,
pubmed-meshheading:11456498-Zinc Fingers
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pubmed:year |
2001
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pubmed:articleTitle |
High-affinity binding of a FYVE domain to phosphatidylinositol 3-phosphate requires intact phospholipid but not FYVE domain oligomerization.
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pubmed:affiliation |
Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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