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J. Biol. Chem., Vol. 277, Issue 41, 38328-38338, October 11, 2002
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From the Department of Pathology, University of Pittsburgh,
Pittsburgh, Pennsylvania 15261
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.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF484961.
Characterization of PINCH-2, a New Focal Adhesion Protein That
Regulates the PINCH-1-ILK Interaction, Cell Spreading, and
Migration*
,,
*
This work was supported by National Institutes
of Health Grants GM65188 and DK54639 (to C. W.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Both authors contributed equally to this work.
§
To whom correspondence should be addressed: 707B Scaife Hall, Dept.
of Pathology, University of Pittsburgh, 3550 Terrace St., Pittsburgh,
PA 15261. Tel.: 412-648-2350; Fax: 509-561-4062; E-mail: carywu@pitt.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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