| pubmed-article:18195072 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18195072 | lifeskim:mentions | umls-concept:C0039194 | lld:lifeskim |
| pubmed-article:18195072 | lifeskim:mentions | umls-concept:C0021701 | lld:lifeskim |
| pubmed-article:18195072 | lifeskim:mentions | umls-concept:C0027100 | lld:lifeskim |
| pubmed-article:18195072 | lifeskim:mentions | umls-concept:C0079717 | lld:lifeskim |
| pubmed-article:18195072 | lifeskim:mentions | umls-concept:C0600210 | lld:lifeskim |
| pubmed-article:18195072 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
| pubmed-article:18195072 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:18195072 | pubmed:dateCreated | 2008-1-22 | lld:pubmed |
| pubmed-article:18195072 | pubmed:abstractText | Precise spatial and temporal regulation of cell adhesion and de-adhesion is critical for dynamic lymphocyte migration. Although a great deal of information has been learned about integrin lymphocyte function-associated antigen (LFA)-1 adhesion, the mechanism that regulates efficient LFA-1 de-adhesion from intercellular adhesion molecule (ICAM)-1 during T lymphocyte migration is unknown. Here, we show that nonmuscle myosin heavy chain IIA (MyH9) is recruited to LFA-1 at the uropod of migrating T lymphocytes, and inhibition of the association of MyH9 with LFA-1 results in extreme uropod elongation, defective tail detachment, and decreased lymphocyte migration on ICAM-1, without affecting LFA-1 activation by chemokine CXCL-12. This defect was reversed by a small molecule antagonist that inhibits both LFA-1 affinity and avidity regulation, but not by an antagonist that inhibits only affinity regulation. Total internal reflection fluorescence microscopy of the contact zone between migrating T lymphocytes and ICAM-1 substrate revealed that inactive LFA-1 is selectively localized to the posterior of polarized T lymphocytes, whereas active LFA-1 is localized to their anterior. Thus, during T lymphocyte migration, uropodal adhesion depends on LFA-1 avidity, where MyH9 serves as a key mechanical link between LFA-1 and the cytoskeleton that is critical for LFA-1 de-adhesion. | lld:pubmed |
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| pubmed-article:18195072 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18195072 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18195072 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18195072 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18195072 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18195072 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:18195072 | pubmed:issn | 1540-9538 | lld:pubmed |
| pubmed-article:18195072 | pubmed:author | pubmed-author:SpringerTimot... | lld:pubmed |
| pubmed-article:18195072 | pubmed:author | pubmed-author:ShimaokaMotom... | lld:pubmed |
| pubmed-article:18195072 | pubmed:author | pubmed-author:ChinY... | lld:pubmed |
| pubmed-article:18195072 | pubmed:author | pubmed-author:TangJay XJX | lld:pubmed |
| pubmed-article:18195072 | pubmed:author | pubmed-author:KingMichael... | lld:pubmed |
| pubmed-article:18195072 | pubmed:author | pubmed-author:ReichnerJonat... | lld:pubmed |
| pubmed-article:18195072 | pubmed:author | pubmed-author:KimMinsooM | lld:pubmed |
| pubmed-article:18195072 | pubmed:author | pubmed-author:MorinNicole... | lld:pubmed |
| pubmed-article:18195072 | pubmed:author | pubmed-author:OakesPatrick... | lld:pubmed |
| pubmed-article:18195072 | pubmed:author | pubmed-author:LeeDooyoungD | lld:pubmed |
| pubmed-article:18195072 | pubmed:author | pubmed-author:HyunYoung-Min... | lld:pubmed |
| pubmed-article:18195072 | pubmed:author | pubmed-author:ChinEugene... | lld:pubmed |
| pubmed-article:18195072 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18195072 | pubmed:day | 21 | lld:pubmed |
