Raf Kinase | Tocris Bioscience

Raf kinases, a family of three serine/threonine kinases, are part of the Ras-MAPK signaling cascade and phosphorylate MEK. Upon growth factor stimulation, Raf-1 (c-Raf) is activated by GTP-bound Ras and recruited to the cell membrane. This activation process is tightly regulated.

Raf kinases, a family of three serine/threonine kinases, are part of the Ras-MAPK signaling cascade and phosphorylate MEK. Upon growth factor stimulation, Raf-1 (or c-Raf) is activated by GTP-bound Ras and recruited to the cell membrane. This activation process is tightly regulated by a number of factors including phosphatases (e.g. PP1, PP2A, PP5), kinases (e.g. Src, ERK, Akt, PKC) and proteins that bind directly to Raf-1 (e.g. RKIP, 14-3-3 , KSR, Hsp90).

Raf-1 is also thought to be able to dimerize with wild type B-Raf in a Ras-dependent process. B-Raf is commonly mutated and thereby activated in many human cancers, the most frequent mutation being the V600E mutation of the kinase domain. Whilst wild type B-Raf and Raf-1 are strongly activated by growth factor signals via Ras and Src, a-Raf is only modestly activated and has low basal activity. All three isoforms of Raf are considered to be oncogenic.

External sources of pharmacological information for Raf Kinases : BJP Guide

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