Identification of in vivo phosphorylation sites of MLK3 by mass spectrometry and phosphopeptide mapping.

@article{Vacratsis2002IdentificationOI,
  title={Identification of in vivo phosphorylation sites of MLK3 by mass spectrometry and phosphopeptide mapping.},
  author={Panayiotis O Vacratsis and Brett S Phinney and Douglas A. Gage and Kathleen A Gallo},
  journal={Biochemistry},
  year={2002},
  volume={41 17},
  pages={5613-24}
}
MLK3 is a serine/threonine protein kinase that functions as an upstream activator of the JNK pathway. Previous work has suggested that MLK3 is a multiphosphorylated protein. In this study, mass spectrometry coupled with comparative phosphopeptide mapping was used to directly characterize MLK3 in vivo phosphorylation sites. Various types of mass spectrometry were used to analyze MLK3 tryptic peptides separated by C18 reverse-phase HPLC, leading to the identification of Ser(524), Ser(654), Ser… CONTINUE READING

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