Kinase suppressor of Ras (KSR) is a conserved component of the Ras pathway that interacts directly with MEK and MAPK. It has been shown that KSR1 translocates from the cytoplasm to the cell surface in response to growth factor treatment and that this process is regulated by MARK3 (1). MARK3 phosphorylates serine 309 and serine 404 on KSR1. While, PPP2CA dephosphorlyates serine 404 on KSR1. MARK3 seems to be a positive regulator of the beta-catenin pathway and an inhibitor of the JNK pathway. These findings show that MARK3, a regulator of polarity, is also a modulator of Wnt-beta-catenin signalling, indicating a link between two important developmental pathways (2).
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