Characterization of PINCH-2, a new focal adhesion protein that regulates the PINCH-1-ILK interaction, cell spreading, and migration - PubMed (original) (raw)
. 2002 Oct 11;277(41):38328-38.
doi: 10.1074/jbc.M205576200. Epub 2002 Aug 6.
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- PMID: 12167643
- DOI: 10.1074/jbc.M205576200
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Characterization of PINCH-2, a new focal adhesion protein that regulates the PINCH-1-ILK interaction, cell spreading, and migration
Yongjun Zhang et al. J Biol Chem. 2002.
Free article
Abstract
Integrin-linked kinase (ILK) is a multidomain protein that plays important roles at cell-extracellular matrix (ECM) adhesion sites. We describe here a new LIM-domain containing protein (termed as PINCH-2) that forms a complex with ILK. PINCH-2 is co-expressed with PINCH-1 (previously known as PINCH), another member of the PINCH protein family, in a variety of human cells. Immunofluorescent staining of cells with PINCH-2-specific antibodies show that PINCH-2 localizes to both cell-ECM contact sites and the nucleus. Deletion of the first LIM (LIM1) domain of PINCH-2 abolished the ability of PINCH-2 to form a complex with ILK. The ILK-binding defective LIM1-deletion mutant, unlike the wild type PINCH-2 or the ILK-binding competent LIM5-deletion mutant, was incapable of localizing to cell-ECM contact sites, suggesting that ILK binding is required for this process. Importantly, the PINCH-2-ILK and PINCH-1-ILK interactions are mutually exclusive. Overexpression of PINCH-2 significantly inhibited the PINCH-1-ILK interaction and reduced cell spreading and migration. These results identify a novel nuclear and focal adhesion protein that associates with ILK and reveals an important role of PINCH-2 in the regulation of the PINCH-1-ILK interaction, cell shape change, and migration.
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