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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2002-3-25
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pubmed:abstractText |
The FYVE zinc finger domain is conserved from yeast (five proteins) to man (27 proteins). It functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is found mainly on endosomes. Here we review recent work that sheds light on the targeting of FYVE finger proteins to PI3P-containing membranes, and how these proteins serve to regulate multiple cellular functions.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
513
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
77-84
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:11911884-Amino Acid Sequence,
pubmed-meshheading:11911884-Animals,
pubmed-meshheading:11911884-Binding Sites,
pubmed-meshheading:11911884-Humans,
pubmed-meshheading:11911884-Models, Molecular,
pubmed-meshheading:11911884-Molecular Sequence Data,
pubmed-meshheading:11911884-Nematoda,
pubmed-meshheading:11911884-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:11911884-Phosphatidylinositol Phosphates,
pubmed-meshheading:11911884-Protein Conformation,
pubmed-meshheading:11911884-Protein Kinases,
pubmed-meshheading:11911884-Protein Structure, Secondary,
pubmed-meshheading:11911884-Saccharomyces cerevisiae,
pubmed-meshheading:11911884-Sequence Alignment,
pubmed-meshheading:11911884-Sequence Homology, Amino Acid
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pubmed:year |
2002
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pubmed:articleTitle |
The phosphatidylinositol 3-phosphate-binding FYVE finger.
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pubmed:affiliation |
Department of Biochemistry, The Norwegian Radium Hospital, Oslo, Norway. h.a.stenmark@farmasi.uio.no
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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