Open AccessEpidermal growth factor (EGF) receptor T669 peptide kinase from 3T3-L1 cells is an EGF-stimulated "MAP" kinase.
Author(s) -
Kunio Takishima,
Irene Griswold-Prenner,
Thomas S. Ingebritsen,
Marsha Rich Rosner
Publication year - 1991
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.88.6.2520
Subject(s) - epidermal growth factor , mapk14 , map kinase kinase kinase , map2k7 , mitogen activated protein kinase kinase , biology , mapk7 , cyclin dependent kinase 2 , microbiology and biotechnology , tropomyosin receptor kinase c , kinase , biochemistry , chemistry , receptor , protein kinase a , platelet derived growth factor receptor , growth factor
The epidermal growth factor (EGF) receptor is both an activator and a target of growth factor-stimulated kinases involved in cellular signaling. Threonine-669 (T669) of the EGF receptor is phosphorylated in response to a wide variety of growth-modulating agents. MAP kinase is similarly phosphorylated as well as stimulated by growth activators, including EGF. To determine whether a MAP-type kinase is responsible for T669 kinase activity in EGF-stimulated 3T3-L1 cells, we partially purified and characterized the T669 peptide kinase. The results indicate that a MAP kinase phosphorylates the T669 peptide and raise the possibility that this enzyme may participate in a feedback loop, being activated by the EGF receptor and in turn phosphorylating the receptor.