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Papers In Press, published online ahead of print January 25, 2002
Department of Dermatology, Osaka University, Suita, Osaka 565-0871
Corresponding Author: itami{at}derma.med.osaka-u.ac.jp
We previously reported that Stat3 plays a crucial role in transducing a signal for migration of keratinocytes (EMBO J. 18: 4659-4668, 1999). To clarify the role of Stat3 in signaling the migration, we studied the intracellular signaling pathway through an integrin receptor in Stat3-deficient keratinocytes. Stat3-deficient keratinocytes demonstrated increased adhesiveness and fast spreading on a collagen matrix. Staining with anti-phosphotyrosine antibody revealed that Stat3-deficient keratinocytes had an increased number of tyrosyl-hyperphosphorylated focal adhesions. Analyses with immunoprecipitation revealed that p130Cas was constitutively hyperphosphorylated on tyrosine residues, while other focal adhesion molecules such as FAK and paxillin were not. Transfection of Stat3-deficient keratinocytes with an adenoviral vector encoding wild-type Stat3 gene reversed not only impaired migration, but also the increased tyrosine phosphorylation of p130Cas. These results strongly suggest that Stat3 in keratinocytes plays a critical role in turnover of tyrosine phosphorylation of p130Cas, modulating cell adhesiveness to the substratum leading to growth factor-dependent cell migration.
J. Biol. Chem, 10.1074/jbc.M110795200
Submitted on November 9, 2001
Revised on January 10, 2002
Accepted on January 25, 2002
Stat3 deficiency in keratinocytes leads to compromised cell migration through hyperphosphorylation of p130Cas
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