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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
2004-10-22
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pubmed:abstractText |
Sorting nexins (SNXs) are phox homology (PX) domain-containing proteins thought to regulate endosomal sorting of internalized receptors. The prototypical SNX is sorting nexin-1 (SNX1), a protein that through its PX domain binds phosphatidylinositol 3-monophosphate [PtdIns(3)P] and phosphatidylinositol 3,5-bisphosphate [PtdIns(3,5)P(2)]. SNX1 is associated with early endosomes, from where it has been proposed to regulate the degradation of internalized epidermal growth factor (EGF) receptors through modulating endosomal-to-lysosomal sorting.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0960-9822
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
14
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1791-800
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pubmed:dateRevised |
2009-10-1
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pubmed:meshHeading |
pubmed-meshheading:15498486-Biological Transport,
pubmed-meshheading:15498486-Carrier Proteins,
pubmed-meshheading:15498486-Endosomes,
pubmed-meshheading:15498486-Fluorescent Antibody Technique,
pubmed-meshheading:15498486-HeLa Cells,
pubmed-meshheading:15498486-Humans,
pubmed-meshheading:15498486-Intracellular Membranes,
pubmed-meshheading:15498486-Microscopy, Electron,
pubmed-meshheading:15498486-Phosphatidylinositols,
pubmed-meshheading:15498486-Protein Structure, Tertiary,
pubmed-meshheading:15498486-RNA, Small Interfering,
pubmed-meshheading:15498486-RNA Interference,
pubmed-meshheading:15498486-Receptor, IGF Type 2,
pubmed-meshheading:15498486-Transfection,
pubmed-meshheading:15498486-Vesicular Transport Proteins,
pubmed-meshheading:15498486-trans-Golgi Network
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pubmed:year |
2004
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pubmed:articleTitle |
Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high- curvature membranes and 3-phosphoinositides.
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pubmed:affiliation |
Henry Wellcome Integrated Signalling Laboratories, Department of Biochemistry, School of Medical Sciences, University of Bristol, Bristol BS8 1TD, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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