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. Author manuscript; available in PMC: 2010 Jun 29.

Published in final edited form as: J Muscle Res Cell Motil. 2009 Apr 21;30(1-2):67–72. doi: 10.1007/s10974-009-9176-y

In vitro kinase assays were performed with c-Raf-1 using MEK as substrate (Panel A), Pak and/or c-Raf-1 in the absence (−) or presence (+) of 10 μM GW5074 (Panel B), with WT-cTnT or cTnT-T206E as substrate (Panel C) or PKCδ with WT-cTnT or cTnT-T206E as substrate (Panel D). Of note, the data in individual panels in this figure are from a single experiment, and permit a side-by-side comparison of c-Raf-1 activity towards MEK (which contains at least two Raf-1 phosphorylation sites) and TnT (which is phosphorylated by Raf-1 specifically at Thr²⁰⁶). Results were replicated in three separate experiments.

In vitro kinase assays were performed with c-Raf-1 using MEK as substrate (Panel A), Pak and/or c-Raf-1 in the absence (−) or presence (+) of 10 μM GW5074 (Panel B), with WT-cTnT or cTnT-T206E as substrate (Panel C) or PKCδ with WT-cTnT or cTnT-T206E as substrate (Panel D). Of note, the data in individual panels in this figure are from a single experiment, and permit a side-by-side comparison of c-Raf-1 activity towards MEK (which contains at least two Raf-1 phosphorylation sites) and TnT (which is phosphorylated by Raf-1 specifically at Thr²⁰⁶). Results were replicated in three separate experiments.