| pubmed-article:7636193 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7636193 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
| pubmed-article:7636193 | lifeskim:mentions | umls-concept:C0023516 | lld:lifeskim |
| pubmed-article:7636193 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:7636193 | lifeskim:mentions | umls-concept:C0010853 | lld:lifeskim |
| pubmed-article:7636193 | lifeskim:mentions | umls-concept:C0014239 | lld:lifeskim |
| pubmed-article:7636193 | lifeskim:mentions | umls-concept:C0376525 | lld:lifeskim |
| pubmed-article:7636193 | lifeskim:mentions | umls-concept:C1511625 | lld:lifeskim |
| pubmed-article:7636193 | lifeskim:mentions | umls-concept:C0333117 | lld:lifeskim |
| pubmed-article:7636193 | lifeskim:mentions | umls-concept:C0292863 | lld:lifeskim |
| pubmed-article:7636193 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:7636193 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:7636193 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:7636193 | pubmed:dateCreated | 1995-9-12 | lld:pubmed |
| pubmed-article:7636193 | pubmed:abstractText | Selected functions of integrins, including regulated cytoskeletal association and transmembrane signaling, depend on a poorly defined bidirectional communication between the extracellular and cytoplasmic domains of the alpha and beta subunits. To investigate this problem in the leukocyte integrin alpha L beta 2 (LFA-1), we generated a series of cytoplasmic truncation or internal substitution mutants of the alpha L and beta 2 cytoplasmic domains, and assessed their biochemical and functional properties upon ectopic expression in constitutively adherent cells. Expression of the alpha L beta 2 heterodimer in stably adherent cells is sufficient to promote its constitutive cytoskeletal association. Structural determinants for such association are located in selected regions of the beta 2 cytoplasmic domain, which display functional interdependence. In addition, a conserved region (Arg733-Lys742) in the beta 2 cytoplasmic domain seems to be critical not only for its cytoskeletal association, but also for endoplasmic reticulum retention, assembly, and transport to the plasma membrane of the mature alpha L beta 2 heterodimer. Analysis of deletion mutants of the alpha L subunit demonstrates a role of the conserved, membrane-proximal GFFKR motif in conferring stability to the alpha beta complex, possibly because of its direct involvement in heterodimer formation. We propose that a previously uncharacterized association of defined subregions of the cytoplasmic domains of integrin alpha and beta subunits affects the dimerization and regulated function of the adhesion receptor. | lld:pubmed |
| pubmed-article:7636193 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7636193 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7636193 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7636193 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:7636193 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7636193 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7636193 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7636193 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7636193 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:7636193 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:7636193 | pubmed:author | pubmed-author:BossiGG | lld:pubmed |
| pubmed-article:7636193 | pubmed:author | pubmed-author:BendelJ PJP | lld:pubmed |
| pubmed-article:7636193 | pubmed:author | pubmed-author:PardyBB | lld:pubmed |
| pubmed-article:7636193 | pubmed:author | pubmed-author:InverardiLL | lld:pubmed |
| pubmed-article:7636193 | pubmed:author | pubmed-author:RovidaEE | lld:pubmed |
| pubmed-article:7636193 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7636193 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:7636193 | pubmed:volume | 155 | lld:pubmed |
| pubmed-article:7636193 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7636193 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7636193 | pubmed:pagination | 1252-63 | lld:pubmed |
| pubmed-article:7636193 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:7636193 | pubmed:meshHeading | pubmed-meshheading:7636193-... | lld:pubmed |
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| pubmed-article:7636193 | pubmed:meshHeading | pubmed-meshheading:7636193-... | lld:pubmed |
| pubmed-article:7636193 | pubmed:meshHeading | pubmed-meshheading:7636193-... | lld:pubmed |
| pubmed-article:7636193 | pubmed:meshHeading | pubmed-meshheading:7636193-... | lld:pubmed |
| pubmed-article:7636193 | pubmed:meshHeading | pubmed-meshheading:7636193-... | lld:pubmed |
| pubmed-article:7636193 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7636193 | pubmed:articleTitle | Conserved regions in the cytoplasmic domains of the leukocyte integrin alpha L beta 2 are involved in endoplasmic reticulum retention, dimerization, and cytoskeletal association. | lld:pubmed |
| pubmed-article:7636193 | pubmed:affiliation | Scientific Institute San Raffaele-DIBIT, University of Milano School of Medicine, Italy. | lld:pubmed |
| pubmed-article:7636193 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7636193 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7636193 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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