TRIM50 protein regulates vesicular trafficking for acid secretion in gastric parietal cells

Miyuki Nishi, Fumiyo Aoyama, Fumihiko Kisa, Hua Zhu, Mingzhai Sun, Peihui Lin, Hiroya Ohta, Bo Van, Shinichiro Yamamoto, Sho Kakizawa, Hideki Sakai, Jianjie Ma, Akira Sawaguchi*, Hiroshi Takeshima

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

Of the TRIM/RBCC family proteins taking part in a variety of cellular processes, TRIM50 is a stomach-specific member with no defined biological function. Our biochemical data demonstrated that TRIM50 is specifically expressed in gastric parietal cells and is predominantly localized in the tubulovesicular and canalicular membranes. In cultured cells ectopically expressing GFP-TRIM50, confocal microscopic imaging revealed dynamic movement of TRIM50-associated vesicles in a phosphoinositide 3-kinase-dependent manner. A protein overlay assay detected preferential binding of the PRY-SPRY domain from the TRIM50 C-terminal region to phosphatidylinositol species, suggesting that TRIM50 is involved in vesicular dynamics by sensing the phosphorylated state of phosphoinositol lipids. Trim50 knockout mice retained normal histology in the gastric mucosa but exhibited impaired secretion of gastric acid. In response to histamine, Trim50 knock-out parietal cells generated deranged canaliculi, swollen microvilli lacking actin filaments, and excess multilamellar membrane complexes. Therefore, TRIM50 seems to play an essential role in tubulovesicular dynamics, promoting the formation of sophisticated canaliculi and microvilli during acid secretion in parietal cells.

Original languageEnglish
Pages (from-to)33523-33532
Number of pages10
JournalJournal of Biological Chemistry
Volume287
Issue number40
DOIs
StatePublished - 2012/09/28

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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