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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1995-9-12
|
| 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.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
AIM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0022-1767
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
1
|
| pubmed:volume |
155
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1252-63
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading |
pubmed-meshheading:7636193-Allosteric Regulation,
pubmed-meshheading:7636193-Amino Acid Sequence,
pubmed-meshheading:7636193-Animals,
pubmed-meshheading:7636193-Cell Compartmentation,
pubmed-meshheading:7636193-Cell Line, Transformed,
pubmed-meshheading:7636193-Cercopithecus aethiops,
pubmed-meshheading:7636193-Cytoskeleton,
pubmed-meshheading:7636193-Endoplasmic Reticulum,
pubmed-meshheading:7636193-Lymphocyte Function-Associated Antigen-1,
pubmed-meshheading:7636193-Molecular Sequence Data,
pubmed-meshheading:7636193-Protein Conformation,
pubmed-meshheading:7636193-Protein Multimerization,
pubmed-meshheading:7636193-Protein Structure, Tertiary,
pubmed-meshheading:7636193-Recombinant Fusion Proteins,
pubmed-meshheading:7636193-Sequence Deletion,
pubmed-meshheading:7636193-T-Lymphocytes,
pubmed-meshheading:7636193-Tetradecanoylphorbol Acetate,
pubmed-meshheading:7636193-Transfection
|
| pubmed:year |
1995
|
| 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.
|
| pubmed:affiliation |
Scientific Institute San Raffaele-DIBIT, University of Milano School of Medicine, Italy.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|