Identification of Phosphorylation Sites in the C-Terminal Region of Charged Multivesicular Body Protein 1A (CHMP1A)

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  • MAEMOTO Yuki
    Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University
  • SHIBATA Hideki
    Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University
  • MAKI Masatoshi
    Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University

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Human charged multivesicular body protein 1A (CHMP1A) displayed two bands on SDS–PAGE and differences in efficiency of complex formation with IST1. By site-directed mutagenesis and phosphate-affinity PAGE, we identified Ser179 and Ser182 located in the C-terminal region as major phosphorylation sites that cause a mobility shift, but interaction with IST1 was not affected by Ser-to-Ala mutations.

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