Intracellular phospholipase A(iPLA) is a novel factor involved in coat protein complex I-and Rab6-independent retrograde transport between the endoplasmic reticulum and the golgi complex

Rei K. Morikawa, Junken Aoki, Fumi Kano, Masayuki Murata, Akitsugu Yamamoto, Masafumi Tsujimoto, Hiroyuki Arai

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38 Citations (Scopus)

Abstract

The mammalian intracellular phospholipase A1 (iPLA1) family consists of three members, iPLA1α/PA-PLA1, iPLA1β/p125, and iPLA1γ/KIAA0725p. Although iPLA1β has been implicated in organization of the ER-Golgi compartments, little is known about the physiological role of its closest paralog, iPLA1γ. Here we show that iPLA1γ mediates a specific retrograde membrane transport pathway between the endoplasmic reticulum (ER) and the Golgi complex. iPLA1γ appeared to be localized to the cytosol, the cis-Golgi, and the ER-Golgi intermediate compartment (ERGIC). Time-lapse microscopy revealed that a population of GFP-iPLA1γ was associated with transport carriers moving out from the Golgi complex. Knockdown of iPLA1γ expression by RNAi did not affect the anterograde transport of VSVGts045 but dramatically delayed two types of Golgi-to-ER retrograde membrane transport; that is, transfer of the Golgi membrane into the ER in the presence of brefeldin A and delivery of cholera toxin B subunit from the Golgi complex to the ER. Notably, knockdown of iPLA1γ did not impair COPI- and Rab6-dependent retrograde transports represented by ERGIC-53 recycling and ER delivery of Shiga toxin, respectively. Thus, iPLA1γ is a novel membrane transport factor that contributes to a specific Golgi-to-ER retrograde pathway distinct from presently characterized COPI- and Rab6-dependent pathways.

Original languageEnglish
Pages (from-to)26620-26630
Number of pages11
JournalJournal of Biological Chemistry
Volume284
Issue number39
DOIs
Publication statusPublished - 2009 Sep 25

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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