Second nature: Biological functions of the Raf‐1 “kinase”
Open Access
- 23 March 2005
- journal article
- review article
- Published by Wiley in FEBS Letters
- Vol. 579 (15) , 3271-3277
- https://doi.org/10.1016/j.febslet.2005.03.024
Abstract
More than 20 years ago, Raf was discovered as a cellular oncogene transduced by transforming retroviruses. Since then, the three Raf isoforms have been intensively studied, mainly as the kinases linking Ras to the MEK/ERK signaling module. As this pathway is activated in human cancer, the Raf kinases are considered promising therapeutic targets, and we have learned a lot about their regulation, targets, and functions. Do they still hold surprises? Recent gene targeting studies indicate that they do. This review focuses on the regulation and biology of the best‐studied Raf isoform, Raf‐1, in the context of its kinase‐independent functions.Keywords
This publication has 66 references indexed in Scilit:
- The RAF proteins take centre stageNature Reviews Molecular Cell Biology, 2004
- Binding activity of H-Ras is necessary for in vivo inhibition of ASK1 activityCell Research, 2004
- An old kinase on a new path: Raf and apoptosisCell Death & Differentiation, 2002
- ERK signalling and oncogene transformation are not impaired in cells lacking A-RafOncogene, 2002
- Raf-1-associated Protein Phosphatase 2A as a Positive Regulator of Kinase ActivationJournal of Biological Chemistry, 2000
- Post-natal lethality and neurological and gastrointestinal defects in mice with targeted disruption of the A-Raf protein kinase geneCurrent Biology, 1996
- Biochemical Analysis of MEK Activation in NIH3T3 FibroblastsPublished by Elsevier ,1995
- Complexes of Ras⋅GTP with Raf-1 and Mitogen-Activated Protein Kinase KinaseScience, 1993
- Activation of the MAP kinase pathway by the protein kinase rafCell, 1992
- ERKs: A family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGFCell, 1991