| pubmed-article:7532472 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7532472 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
| pubmed-article:7532472 | lifeskim:mentions | umls-concept:C0087111 | lld:lifeskim |
| pubmed-article:7532472 | lifeskim:mentions | umls-concept:C0021701 | lld:lifeskim |
| pubmed-article:7532472 | lifeskim:mentions | umls-concept:C1511625 | lld:lifeskim |
| pubmed-article:7532472 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:7532472 | lifeskim:mentions | umls-concept:C1512032 | lld:lifeskim |
| pubmed-article:7532472 | lifeskim:mentions | umls-concept:C0066772 | lld:lifeskim |
| pubmed-article:7532472 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:7532472 | pubmed:dateCreated | 1995-3-24 | lld:pubmed |
| pubmed-article:7532472 | pubmed:abstractText | Integrin receptors localize to focal contact sites and interact with the cytoskeleton via the beta 1 cytoplasmic domain. To study the role of this domain in adhesion, we have expressed in NIH 3T3 cells a cDNA consisting of the interleukin 2 receptor alpha subunit extracellular and transmembrane domains, connected to the integrin beta 1 cytoplasmic domain (IL2R-beta 1). Since the extracellular domain of the chimeric protein has no role in adhesion, this protein could uncouple adhesion from intracellular events. As expected, in a cell line expressing IL2R-beta 1, this chimera was directed to focal contact sites. Unexpectedly, the cells exhibited normal adhesion to fibronectin (FN). However, when a rapid reorganization of the cytoskeleton was induced using lysophosphatidic acid (LPA), IL2R-beta 1 cells detached from FN in contrast to wild-type cells. The detachment in response to LPA could be prevented with cytochalasin D, an inhibitor of actin polymerization. These results imply that a beta 1 cytoplasmic domain, which is uncoupled from adhesion, can compete with the cytoplasmic domain of native integrin beta 1 for cytoskeletal proteins. As a consequence, the IL2R-beta 1 protein acts as a dominant negative effector of adhesion by disrupting the integrin-cytoskeleton connection. | lld:pubmed |
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| pubmed-article:7532472 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7532472 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7532472 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7532472 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:7532472 | pubmed:issn | 1059-1524 | lld:pubmed |
| pubmed-article:7532472 | pubmed:author | pubmed-author:SmilenovLL | lld:pubmed |
| pubmed-article:7532472 | pubmed:author | pubmed-author:MarcantonioE... | lld:pubmed |
| pubmed-article:7532472 | pubmed:author | pubmed-author:BriesewitzRR | lld:pubmed |
| pubmed-article:7532472 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7532472 | pubmed:volume | 5 | lld:pubmed |
| pubmed-article:7532472 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7532472 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7532472 | pubmed:pagination | 1215-23 | lld:pubmed |
| pubmed-article:7532472 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7532472 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7532472 | pubmed:articleTitle | Integrin beta 1 cytoplasmic domain dominant negative effects revealed by lysophosphatidic acid treatment. | lld:pubmed |
| pubmed-article:7532472 | pubmed:affiliation | Department of Pathology, College of Physicians and Surgeons, Columbia University, New York, New York 10032. | lld:pubmed |
| pubmed-article:7532472 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7532472 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:7532472 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7532472 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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