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Vol. 12, Issue 8, 2290-2307, August 2001
i-Milivojevi
,*
ko
Ili
*Metabolic Research Unit and Departments of §Medicine
and Hypertrophic terminally differentiated cardiac myocytes show
increased sarcomeric organization and altered gene expression. Previously, we established a role for the nonreceptor tyrosine kinase
Src in signaling cardiac myocyte hypertrophy. Here we report evidence
that p130Cas (Cas) and focal adhesion kinase (FAK) regulate this
process. In neonatal cardiac myocytes, tyrosine phosphorylation of Cas
and FAK increased upon endothelin (ET) stimulation. FAK, Cas, and
paxillin were localized in sarcomeric Z-lines, suggesting that the
Z-line is an important signaling locus in these cells. Cas, alone or in
cooperation with Src, modulated basal and ET-stimulated atrial
natriuretic peptide (ANP) gene promoter activity, a marker of cardiac
hypertrophy. Expression of the C-terminal focal adhesion-targeting domain of FAK interfered with localization of endogenous FAK to Z-lines. Expression of the Cas-binding proline-rich region 1 of FAK
hindered association of Cas with FAK and impaired the structural stability of sarcomeres. Collectively, these results suggest that interaction of Cas with FAK, together with their localization to
Z-lines, is critical to assembly of sarcomeric units in cardiac myocytes in culture. Moreover, expression of the focal
adhesion-targeting and/or the Cas-binding proline-rich regions of FAK
inhibited ANP promoter activity and suppressed ET-induced ANP and brain
natriuretic peptide gene expression. In summary, assembly of signaling
complexes that include the focal adhesion proteins Cas, FAK, and
paxillin at Z-lines in the cardiac myocyte may regulate, either
directly or indirectly, both cytoskeletal organization and gene
expression associated with cardiac myocyte hypertrophy.
Stomatology, University of California San Francisco,
San Francisco, California 94143-0540
Corresponding author. E-mail address:
branka{at}itsa.ucsf.edu.
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