MEK inhibition and phosphorylation of serine 4 on B23 are two coincident events in mitosis.
Previous studies have shown that activation of the Raf/ MEK/ ERK pathway is necessary for G2/M transition. However, as for the activation state of MEK in mitosis the conclusion is not consistent. Here we show that MEK is inhibited in mitosis. In addition, we identify a multifunctional protein named B23 that strongly cross-reacts with a phospho- MEK antibody in mitotic cells. Sequence homology between the N-terminus surrounding Ser 4 of B23 and the Raf phosphorylation site on MEK suggests a mechanism for cross-reaction of the antibody. Thus, mutation of Ser 4 to alanine abolishes cross-reactivity between B23 and the phospho- MEK antibody. Our findings may explain the discrepancy of results obtained with the use of phospho- MEK antibody regarding the activation state of MEK in mitosis.[1]References
- MEK inhibition and phosphorylation of serine 4 on B23 are two coincident events in mitosis. Hayne, C., Xiang, X., Luo, Z. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
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