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Kinase suppressor of Ras (KSR) is involved in the regulation of the Ras activated MAPK pathway. KSR contains some kinase activity, phosphorylating Raf-1 at Thr269 in response to Ras stimulation. One study found this was necessary for the optimal activation of Raf-1 in response to EGF. Further studies popularly supported the idea that KSR acts as a scaffolding protein for the Ras stimulated MAPK pathway by supporting the formation of a large complex. Within human embryonic kidney cells KSR forms part of a multimolecular complex consisting of MEK1, MEK2, HSP90, HSP70, HSP68, p50CDC37, and 14-3-3, along with other currently unidentified proteins. The binding of protein 14-3-3 to KSR is associated with KSR phosphorylation sites Ser297 and Ser392. These sites are phosphorylated when KSR is inactive. Three other important sites on KSR are Thr260, Thr274, and Ser443, which appear to be phosphorylated by active MAPKs. Inactive ERK MAPKs may also transiently associate with the complex. These kinases will be phosphorylated by the MEK part of the KSR signaling complex.
Gene Name: | kinase suppressor of ras 1 |
Family/Subfamily: | Protein Kinase , Raf |
Synonyms: | KSR1, B-KSR1, KSR, RSU2, Kinase suppressor of ras, Kinase suppressor of ras 1 |
Target Sequences: | U43586 AAC50354.1 Q8IVT5 |
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