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. Author manuscript; available in PMC: 2017 Mar 29.
Published in final edited form as: Biochemistry. 2016 Mar 16;55(12):1909–1917. doi: 10.1021/acs.biochem.6b00096

Figure 2.

Figure 2

Phosphorylated T188 (pT188) is present in bacterial preparations of ERK2. (A) Summary of MS analysis of fractions from a MonoQ purification of ERK2. (B) Selected fractions were immunoblotted with antibodies that recognize ERK2 regardless of its phosphorylation state, activated ERK2 (ppERK2), and pT188 selectively15. MAP kinase phosphatase 3 (MKP3) is able to dephosphorylate pY185 and pT183 but not pT188. (C) Immunoblot of MonoQ fractions of purified wild type ERK2 and a preparation of a kinase-dead ERK2 (K52R) with a pT188-selective antibody. (D) MEK1R4F recognizes and phosphorylates eluted fractions containing pT188, increasing ERK2 kinase activity toward MBP. (E) Model of the triply phosphorylated ERK2 activation loop.