Identification of phosphorylation sites in the C-terminal region of charged multivesicular body protein 1A (CHMP1A)

Yuki Maemoto; Hideki Shibata; Masatoshi Maki

doi:10.1271/bbb.130065

Identification of phosphorylation sites in the C-terminal region of charged multivesicular body protein 1A (CHMP1A)

Biosci Biotechnol Biochem. 2013;77(6):1317-9. doi: 10.1271/bbb.130065. Epub 2013 Jun 7.

Authors

Yuki Maemoto¹, Hideki Shibata, Masatoshi Maki

Affiliation

¹ Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Japan.

PMID: 23748770
DOI: 10.1271/bbb.130065

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Electrophoresis, Polyacrylamide Gel
Endosomal Sorting Complexes Required for Transport / chemistry*
Endosomal Sorting Complexes Required for Transport / metabolism
Humans
Multiprotein Complexes / chemistry
Mutagenesis, Site-Directed
Oncogene Proteins / chemistry*
Oncogene Proteins / metabolism
Phosphorylation
Serine / chemistry*
Structure-Activity Relationship
Vesicular Transport Proteins

Substances

CHMP1A protein, human
Endosomal Sorting Complexes Required for Transport
IST1 protein, human
Multiprotein Complexes
Oncogene Proteins
Vesicular Transport Proteins
Serine