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. 2011 Dec 19;6(12):e29304. doi: 10.1371/journal.pone.0029304

Figure 2. MARK2 phosphorylates KSR1 at Ser392 in vitro and in vivo.

Figure 2

A. KSR1-FLAG, C-TAK1-HA, and MARK2-HA were individually transfected into 293T cells. Thirty-six hours later cells were lysed and HA- or FLAG-immunoprecipitations were performed. KSR1-FLAG immunoprecipitates were phosphatase treated, then incubated with MARK2-HA or C-TAK1-HA immunoprecipitates in the presence of ATP. Western blots were performed and immunoblotted with an anti-pS392 KSR1 specific antibody, anti-KSR1 antibody, or anti-HA antibody. B. Quantification of pS392 KSR1/total KSR1 from panel A, normalized to phosphatase treated WT KSR1 control. Results are the mean +/- S.D. of three independent experiments. C. KSR1-FLAG, C-TAK1-HA, MARK2-HA and their respective empty vectors were transfected in combination in 293T cells. Thirty-six hours after transfection cells were lysed. Proteins were detected on a western blot using antibodies to pS392KSR1, KSR1, or epitope tag of MARK2 and C-TAK1. *p<0.05 compared to ppase treated control.