Title : Unphosphorylated and tyrosine-phosphorylated forms of a focal adhesion protein, paxillin, are substrates for calpain II in vitro: implications for the possible involvement of calpain II in mitosis-specific degradation of paxillin.

Pub. Date : 1994 Dec 12

PMID : 7988702






4 Functional Relationships(s)
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Protein Name
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1 Unphosphorylated and tyrosine-phosphorylated forms of a focal adhesion protein, paxillin, are substrates for calpain II in vitro: implications for the possible involvement of calpain II in mitosis-specific degradation of paxillin. Tyrosine paxillin Homo sapiens
2 Unphosphorylated and tyrosine-phosphorylated forms of a focal adhesion protein, paxillin, are substrates for calpain II in vitro: implications for the possible involvement of calpain II in mitosis-specific degradation of paxillin. Tyrosine paxillin Homo sapiens
3 Paxillin is tyrosine-phosphorylated during interphase of the cell cycle by protein tyrosine kinases (PTK) such as c-Src and Csk, and becomes dephosphorylated during mitosis. Tyrosine paxillin Homo sapiens
4 Our data, however, indicate that tyrosine phosphorylation of paxillin does not affect the rate of paxillin degradation by calpain in vitro. Tyrosine paxillin Homo sapiens