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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2002-3-18
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pubmed:abstractText |
Intercellular adhesion molecule 3 (ICAM-3) is a leukocyte-specific receptor involved in primary immune responses. We have investigated the interaction between ICAM-3 and ezrin/radixin/moesin (ERM) proteins and its role in LFA-1-induced cell-cell interactions and membrane positioning of ICAM-3 in polarized migrating lymphocytes. Protein-protein binding assays demonstrated a phosphatidylinositol 4,5-bisphosphate-induced association between ICAM-3 and the amino-terminal domain of ERM proteins. This interaction was not essential for the binding of ICAM-3 to LFA-1. Dynamic fluorescence videomicroscopy studies of cells demonstrated that moesin and ICAM-3 coordinately redistribute on the plasma membrane during lymphocyte migration. Furthermore, overexpression of the amino-terminal domain of moesin, which lacks the consensus moesin actin-binding site, caused the subcellular mislocalization of ICAM-3. A CD4 chimerical protein containing the cytoplasmic tail of ICAM-3 was targeted to the trailing edge. Point mutation of Ser(487), Ser(489), and Ser(496) to alanine in the juxtamembrane region of ICAM-3 significantly impaired both ERM binding and polarization of ICAM-3. ERM-directed polarization of ICAM-3 was also impaired by phosphorylation-like mutation of Ser(487) and Ser(489), but not of Ser(496). Our results underscore the key role of specific serine residues within the cytoplasmic region of ICAM-3 for its ERM-directed positioning at the trailing edge of motile lymphocytes.
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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/Alanine,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD4,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation,
http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ICAM3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/ezrin,
http://linkedlifedata.com/resource/pubmed/chemical/moesin,
http://linkedlifedata.com/resource/pubmed/chemical/radixin
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10400-9
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pubmed:dateRevised |
2008-6-13
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pubmed:meshHeading |
pubmed-meshheading:11784723-Alanine,
pubmed-meshheading:11784723-Amino Acid Motifs,
pubmed-meshheading:11784723-Amino Acid Sequence,
pubmed-meshheading:11784723-Animals,
pubmed-meshheading:11784723-Antigens, CD,
pubmed-meshheading:11784723-Antigens, CD4,
pubmed-meshheading:11784723-Antigens, Differentiation,
pubmed-meshheading:11784723-Blood Proteins,
pubmed-meshheading:11784723-Blotting, Western,
pubmed-meshheading:11784723-Cell Adhesion Molecules,
pubmed-meshheading:11784723-Cell Communication,
pubmed-meshheading:11784723-Cell Line,
pubmed-meshheading:11784723-Cell Membrane,
pubmed-meshheading:11784723-Cell Movement,
pubmed-meshheading:11784723-Cytoplasm,
pubmed-meshheading:11784723-Cytoskeletal Proteins,
pubmed-meshheading:11784723-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:11784723-Glutathione Transferase,
pubmed-meshheading:11784723-Green Fluorescent Proteins,
pubmed-meshheading:11784723-Humans,
pubmed-meshheading:11784723-K562 Cells,
pubmed-meshheading:11784723-Luminescent Proteins,
pubmed-meshheading:11784723-Lymphocytes,
pubmed-meshheading:11784723-Membrane Proteins,
pubmed-meshheading:11784723-Mice,
pubmed-meshheading:11784723-Microfilament Proteins,
pubmed-meshheading:11784723-Microscopy, Fluorescence,
pubmed-meshheading:11784723-Microscopy, Video,
pubmed-meshheading:11784723-Molecular Sequence Data,
pubmed-meshheading:11784723-Phosphoproteins,
pubmed-meshheading:11784723-Phosphorylation,
pubmed-meshheading:11784723-Plasmids,
pubmed-meshheading:11784723-Precipitin Tests,
pubmed-meshheading:11784723-Protein Binding,
pubmed-meshheading:11784723-Protein Biosynthesis,
pubmed-meshheading:11784723-Protein Structure, Tertiary,
pubmed-meshheading:11784723-Recombinant Fusion Proteins,
pubmed-meshheading:11784723-Sequence Homology, Amino Acid,
pubmed-meshheading:11784723-Serine,
pubmed-meshheading:11784723-Transfection
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pubmed:year |
2002
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pubmed:articleTitle |
A novel serine-rich motif in the intercellular adhesion molecule 3 is critical for its ezrin/radixin/moesin-directed subcellular targeting.
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pubmed:affiliation |
Servicio de Inmunologia, Hospital de la Princesa, Universidad Autónoma de Madrid, Madrid 28006, Spain.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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