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Papers In Press, published online ahead of print August 19, 2002
Center For Cell Biology & Cancer Reseach, Albany Medical College (Mail Code 165), Albany, New York 12208-3479
Corresponding Author: ZhengM{at}mail.amc.edu
Transforming growth factor-beta1 (TGF-beta1) is a multipotential cytokine which regulates remodeling tissue extracellular matrix during the early tumorigenesis and wound healing. Human enhancer of filamentation-1 (HEF1), a multifunctional docking protein, is involved in integrin-based signaling which affects cell motility, growth and apoptosis. Our studies reveal that TGF-beta1 is a potent inducer of HEF1 gene transcription in human dermal fibroblasts. TGF-beta1 promoted HEF1 expression in a dose-dependent manner and resulted in a sixteen-fold increase in HEF1 protein level. TGF-beta1 had no effect on the stability of either HEF1 protein or mRNA. The TGF-beta1-induced HEF1 expression was independent of cell adhesion and resistant to cytoskeleton disruption. TGF-beta1 increased levels of both p105 and p115 HEF1 in adherent fibroblasts. Digestion with specific phosphatases indicated that the p115HEF1 resulted from serine/threonine phosphorylation of p105HEF1. The appearance of the p115HEF1 as well as tyrosine phosphorylation of p105HEF1 required cell adhesion and/or an organized cytoskeleton. An in-vitro kinase assay indicated that p105HEF1 was a substrate for Src. PP1, a specific Src kinase inhibitor, was able to block adhesion-dependent tyrosine phosphorylation of p105HEF1. These findings suggest that TGF-beta1 regulates HEF1 gene expression and that HEF1 phosphorylation is dependent on cell adhesion and Src kinase activity.
J. Biol. Chem, 10.1074/jbc.M202263200
Submitted on March 7, 2002
Revised on August 14, 2002
Accepted on August 19, 2002
Regulation of HEF1 expression and phosphorylation by TGF-beta1 and cell adhesion
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