Abstract：
:The dynamics of cell adhesion sites control cell morphology and motility. Adhesion-site turnover is thought to depend on the local availability of the acidic phospholipid phosphatidylinositol-4,5-bisphosphate (PIP(2)). PIP(2) can bind to many cell adhesion proteins such as vinculin and talin, but the consequences of this interaction are poorly understood. To study the significance of phospholipid binding to vinculin for adhesion-site turnover and cell motility, we constructed a mutant, vinculin-LD, deficient in acidic phospholipid binding yet with functional actin-binding sites. When expressed in cells, vinculin-LD was readily recruited to adhesion sites, as judged by fluorescence recovery after photobleaching (FRAP) analysis, but cell spreading and migration were strongly impaired, and PIP(2)-dependent disassembly of adhesions was suppressed. Thus, PIP(2) binding is not essential for vinculin activation and recruitment, as previously suggested. Instead, we propose that PIP(2) levels can regulate the uncoupling of adhesion sites from the actin cytoskeleton, with vinculin functioning as a sensor.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Chandrasekar I,Stradal TE,Holt MR,Entschladen F,Jockusch BM,Ziegler WHdoi
10.1242/jcs.01734keywords:
subject
Has Abstractpub_date
2005-04-01 00:00:00pages
1461-72issue
Pt 7eissn
0021-9533issn
1477-9137pii
jcs.01734journal_volume
118pub_type
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