title: Identification of phosphorylation sites in the C-terminal region of charged multivesicular body protein 1A (CHMP1A).
abstract: 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 Ser(179) and Ser(182) 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.
authors.affiliation: Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Japan.
authors.forename: Yuki
authors.initials: Y
authors.lastname: Maemoto
authors.forename: Hideki
authors.initials: H
authors.lastname: Shibata
authors.forename: Masatoshi
authors.initials: M
authors.lastname: Maki
mesh_terms: D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D056827:Endosomal Sorting Complexes Required for Transport / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D046912:Multiprotein Complexes / Q000737:chemistry; D016297:Mutagenesis, Site-Directed; D015513:Oncogene Proteins / Q000737:chemistry* / Q000378:metabolism; D010766:Phosphorylation; D012694:Serine / Q000737:chemistry*; D013329:Structure-Activity Relationship; D033921:Vesicular Transport Proteins
chemical_list: C443709:CHMP1A protein, human; D056827:Endosomal Sorting Complexes Required for Transport; C533705:IST1 protein, human; D046912:Multiprotein Complexes; D015513:Oncogene Proteins; D033921:Vesicular Transport Proteins; D012694:Serine