| pubmed-article:9281591 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9281591 | lifeskim:mentions | umls-concept:C0521449 | lld:lifeskim |
| pubmed-article:9281591 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:9281591 | lifeskim:mentions | umls-concept:C0081938 | lld:lifeskim |
| pubmed-article:9281591 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:9281591 | lifeskim:mentions | umls-concept:C1519249 | lld:lifeskim |
| pubmed-article:9281591 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:9281591 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:9281591 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:9281591 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:9281591 | pubmed:dateCreated | 1997-10-9 | lld:pubmed |
| pubmed-article:9281591 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9281591 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9281591 | pubmed:abstractText | The cytoplasmic domains of integrins are essential for cell adhesion. We report identification of a novel protein, ICAP-1 (integrin cytoplasmic domain- associated protein-1), which binds to the 1 integrin cytoplasmic domain. The interaction between ICAP-1 and beta1 integrins is highly specific, as demonstrated by the lack of interaction between ICAP-1 and the cytoplasmic domains of other beta integrins, and requires a conserved and functionally important NPXY sequence motif found in the COOH-terminal region of the beta1 integrin cytoplasmic domain. Mutational studies reveal that Asn and Tyr of the NPXY motif and a Val residue located NH2-terminal to this motif are critical for the ICAP-1 binding. Two isoforms of ICAP-1, a 200-amino acid protein (ICAP-1alpha) and a shorter 150-amino acid protein (ICAP-1beta), derived from alternatively spliced mRNA, are expressed in most cells. ICAP-1alpha is a phosphoprotein and the extent of its phosphorylation is regulated by the cell-matrix interaction. First, an enhancement of ICAP-1alpha phosphorylation is observed when cells were plated on fibronectin-coated but not on nonspecific poly-L-lysine-coated surface. Second, the expression of a constitutively activated RhoA protein that disrupts the cell-matrix interaction results in dephosphorylation of ICAP-1alpha. The regulation of ICAP-1alpha phosphorylation by the cell-matrix interaction suggests an important role of ICAP-1 during integrin-dependent cell adhesion. | lld:pubmed |
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| pubmed-article:9281591 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9281591 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9281591 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9281591 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9281591 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9281591 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:9281591 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:9281591 | pubmed:author | pubmed-author:LiuJJ | lld:pubmed |
| pubmed-article:9281591 | pubmed:author | pubmed-author:SmithHH | lld:pubmed |
| pubmed-article:9281591 | pubmed:author | pubmed-author:WongCC | lld:pubmed |
| pubmed-article:9281591 | pubmed:author | pubmed-author:ChangD DDD | lld:pubmed |
| pubmed-article:9281591 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9281591 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:9281591 | pubmed:volume | 138 | lld:pubmed |
| pubmed-article:9281591 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9281591 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9281591 | pubmed:pagination | 1149-57 | lld:pubmed |
| pubmed-article:9281591 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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