Acyl-CoA binding domain containing 3 (ACBD3) recruits the protein phosphatase PPM1L to ER-Golgi membrane contact sites

Yasuharu Shinoda, Kohsuke Fujita, Satoko Saito, Hiroyuki Matsui, Yusuke Kanto, Yuko Nagaura, Kohji Fukunaga, Shinri Tamura, Takayasu Kobayashi

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

The metal-dependent protein phosphatase family (PPM) governs a number of signaling pathways. PPM1L, originally identified as a negative regulator of stress-activated protein kinase signaling, was recently shown to be involved in the regulation of ceramide trafficking at ER-Golgi membrane contact sites. Here, we identified acyl-CoA binding domain containing 3 (ACBD3) as an interacting partner of PPM1L. We showed that this association, which recruits PPM1L to ER-Golgi membrane contact sites, is mediated by a GOLD (Golgi dynamics) domain in ACBD3. These results suggested that ACBD3 plays a pivotal role in ceramide transport regulation at the ER-Golgi interface. Structured summary of protein interactions: ACBD3 and PPM1L colocalize by fluorescence microscopy (View interaction) FYCO1 physically interacts with PPM1L by pull down (View interaction) SEC14L2 physically interacts with PPM1L by pull down (View interaction) ACBD3 physically interacts with PPM1L by pull down (View interaction) SEC14L1 physically interacts with PPM1L by pull down (View interaction) PPM1L physically interacts with ACBD3 by two hybrid (View interaction).

Original languageEnglish
Pages (from-to)3024-3029
Number of pages6
JournalFEBS Letters
Volume586
Issue number19
DOIs
Publication statusPublished - 2012 Sep 21

Keywords

  • ACBD3
  • CERT
  • GOLD domain
  • PPM1L

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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