Raf-1 forms a stable complex with Mek1 and activates Mek1 by serine phosphorylation.
- 1 December 1993
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 90 (23) , 10947-10951
- https://doi.org/10.1073/pnas.90.23.10947
Abstract
Recombinant Mek1 and Raf-1 proteins produced in Sf9 cells undergo a tight association both in vivo and in vitro, which apparently does not depend on additional factors or the kinase activity of Mek1 or Raf-1. The complex can be disrupted by two polyclonal antibodies raised against Raf-1 peptides. Coinfection with Raf-1 activates Mek1 > 150-fold, and coinfection with Raf-1 and Mek1 activates Erk1 approximately 90-fold. The activation of Mek1 by Raf-1 involves only serine phosphorylation, which is directly proportional to the extent of Mek1 activation. Phosphopeptide maps suggest a single Raf-1 phosphorylation site on mek1.Keywords
This publication has 26 references indexed in Scilit:
- The MAP kinase cascade is essential for diverse signal transduction pathwaysTrends in Biochemical Sciences, 1993
- A protein kinase similar to MAP kinase activator acts downstream of the raf kinase in DrosophilaCell, 1993
- Activation of the MAP kinase pathway by the protein kinase rafCell, 1992
- MAP Kinases: Charting the Regulatory PathwaysScience, 1992
- Activation of Mitogen-Activated Protein Kinase Kinase by v-Raf in NIH 3T3 Cells and in VitroScience, 1992
- Ordered phosphorylation of p42mapk by MAP kinase kinaseFEBS Letters, 1992
- MAP kinase by any other name smells just as sweetCell, 1992
- Dissection of the protein kinase cascade by which nerve growth factor activates MAP kinasesNature, 1991
- Molecular cloning of a GTPase activating protein specific for the Krev-1 protein p21rap1Cell, 1991
- A novel genetic system to detect protein–protein interactionsNature, 1989