rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2002-6-25
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pubmed:abstractText |
Dynamic regulation of the cell surface expression of adhesion molecules is an important mechanism for controlling neuronal growth cone motility and guidance. Clathrin-mediated vesicular internalization of L1 via the tyrosine-based endocytosis motif YRSL regulates adhesion and signaling by this Ig superfamily molecule. Here, we present evidence that tyrosine-1176 (Y1176) of the YRSL motif is phosphorylated in vivo. The nonreceptor tyrosine kinase (p60src) is implicated in L1-mediated neurite outgrowth, and we find that p60src phosphorylates Y1176 in vitro. Phosphorylation of Y1176 prevents L1 binding to AP-2, an adaptor required for clathrin-mediated internalization of L1. mAb 74-5H7 recognizes the sequence immediately NH2-terminal to the tyrosine-based motif and binds L1 only when Y1176 is dephosphorylated. 74-5H7 identifies a subset of L1 present at points of cell-cell contact and in vesicle-like structures that colocalize with an endocytosis marker. L1-L1 binding or L1 cross-linking induces a rapid increase in 74-5H7 immunoreactivity. Our data suggest a model in which homophilic binding or L1 cross-linking triggers transient dephosphorylation of the YRSL motif that makes L1 available for endocytosis. Thus, the regulation of L1 endocytosis through dephosphorylation of Y1176 is a critical regulatory point of L1-mediated adhesion and signaling.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12082080-10608864,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12082080-10804209,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12082080-10934325,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12082080-1585177,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12082080-9712716
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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/Adaptor Proteins, Vesicular...,
http://linkedlifedata.com/resource/pubmed/chemical/Biological Markers,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Leukocyte L1 Antigen Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neural Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9525
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
157
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1223-32
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pubmed:dateRevised |
2011-4-1
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pubmed:meshHeading |
pubmed-meshheading:12082080-Animals,
pubmed-meshheading:12082080-Brain,
pubmed-meshheading:12082080-Tyrosine,
pubmed-meshheading:12082080-Neurons,
pubmed-meshheading:12082080-Phosphorylation,
pubmed-meshheading:12082080-Ganglia, Spinal,
pubmed-meshheading:12082080-Chick Embryo,
pubmed-meshheading:12082080-Membrane Proteins,
pubmed-meshheading:12082080-Tumor Cells, Cultured,
pubmed-meshheading:12082080-Cells, Cultured,
pubmed-meshheading:12082080-Cell Communication,
pubmed-meshheading:12082080-Biological Markers
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