Evidence that extracellular signal-regulated kinases are the insulin-activated Raf-1 kinase kinases.
作者： R M Lee , M H Cobb , P J Blackshear
DOI: 10.1016/S0021-9258(18)48399-8
关键词: Cyclin-dependent kinase 9 、 Biology 、 Cyclin-dependent kinase 2 、 Kinase activity 、 MAP kinase kinase kinase 、 ASK1 、 MAPK14 、 Biochemistry 、 MAP2K7 、 Mitogen-activated protein kinase kinase
摘要: The Raf-1 proto-oncogene protein kinase can be phosphorylated and activated after stimulation of cells with insulin a variety other growth factors mitogens. We recently presented evidence that certain one or more activities (Lee, R.M., Rapp, U. R., Blackshear, P.J. (1991) J. Biol. Chem. 266, 10351-10357). In the present study, four peaks activity were identified anion-exchange chromatography cell lysates, two these by insulin. Further chromatographic characterization insulin-activated indicated they contained three apparently distinct activities. Two comigrated immunoreactive extracellular signal-regulated kinases (ERK) 1 2 (mitogen-activated kinase) through different separations. Both ERK1 ERK2 reasonably high affinity (Km for = 90 nM; Km 120 nM), produced similar, complex phosphopeptide maps; both also myelin basic protein. third but did not comigrate exactly either ERK2. conclude possibly are members ERK family.
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