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Activation of the MAP kinase homologue RK requires the phosphorylation of Thr‐180 and Tyr‐182 and both residues are phosphorylated in chemically stressed KB cells
Author(s) -
Yair N. Doza,
Ana Cuenda,
Gareth M. Thomas,
Philip Cohen,
Àngel R. Nebreda
Publication year - 1995
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 - 10.1016/0014-5793(95)00346-b
Subject(s) - phosphorylation , kinase , enzyme , chemistry , microbiology and biotechnology , map kinase kinase kinase , mitogen activated protein kinase , protein kinase a , mapk14 , biochemistry , biology
A MAP kinase homologue, termed the reactivating kinase (RK), lies in a signalling pathway which mediates cellular responses to stress. Here we demonstrate that the stress‐induced activation of the RK in human KB cells is accompanied by the phosphorylation of Thr‐180 and Tyr‐182, and that the phosphorylation of both residues is required for the activation of this enzyme.