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Pervanadate‐triggered MAP kinase activation and cell proliferation are not sensitive to PD 98059
Author(s) -
Krady Marie-Marthe,
Malviya Anant N.,
Dupont Jean-Luc
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00989-2
Subject(s) - protein tyrosine phosphatase , microbiology and biotechnology , cell growth , mitogen activated protein kinase , ask1 , protein kinase a , mitogen activated protein kinase kinase , kinase , phosphatase , chemistry , tyrosine kinase , signal transduction , phosphorylation , biology , biochemistry
A tight and stable complex with corresponding protein kinases and phosphatases establishes coupling between activators and inactivators. One such example is emerging from the studies of the Ras‐dependent MAP kinase cascade signaling pathway. Pervanadate, a potent inhibitor of protein tyrosine phosphatase, stimulates MAP kinase and elicits cell proliferation in cultured mouse fibroblasts which is insensitive to PD 98059, the major inhibitor of upstream MEK, whereas serum‐ or TPA‐ triggered proliferation is sensitive to PD 98059. It is suggested that imbalanced coordination between protein kinase and protein phosphatase determines the cellular responses such as cell proliferation. The PD 98059‐insensitive cell proliferation upon protein tyrosine phosphatase inhibition is attributed to a MEK bypass pathway.