Affordable Access

deepdyve-link
Publisher Website

PARL partitions the lipid transfer protein STARD7 between the cytosol and mitochondria

Authors
  • Saita, Shotaro1, 2
  • Tatsuta, Takashi1
  • Lampe, Philipp A1
  • König, Tim1, 3
  • Ohba, Yohsuke1
  • Langer, Thomas1, 1, 4
  • 1 University of Cologne, Germany , (Germany)
  • 2 Osaka University, Japan , (Japan)
  • 3 McGill University, Canada , (Canada)
  • 4 Max‐Planck‐Institute for Biology of Ageing, Germany , (Germany)
Type
Published Article
Journal
The EMBO Journal
Publisher
EMBO
Publication Date
Jan 04, 2018
Volume
37
Issue
4
Identifiers
DOI: 10.15252/embj.201797909
PMID: 29301859
PMCID: PMC5813258
Source
PubMed Central
Keywords
License
Unknown
External links

Abstract

Intramembrane‐cleaving peptidases of the rhomboid family regulate diverse cellular processes that are critical for development and cell survival. The function of the rhomboid protease PARL in the mitochondrial inner membrane has been linked to mitophagy and apoptosis, but other regulatory functions are likely to exist. Here, we identify the START domain‐containing protein STARD 7 as an intramitochondrial lipid transfer protein for phosphatidylcholine. We demonstrate that PARL ‐mediated cleavage during mitochondrial import partitions STARD 7 to the cytosol and the mitochondrial intermembrane space. Negatively charged amino acids in STARD 7 serve as a sorting signal allowing mitochondrial release of mature STARD 7 upon cleavage by PARL . On the other hand, membrane insertion of STARD 7 mediated by the TIM 23 complex promotes mitochondrial localization of mature STARD 7. Mitochondrial STARD 7 is necessary and sufficient for the accumulation of phosphatidylcholine in the inner membrane and for the maintenance of respiration and cristae morphogenesis. Thus, PARL preserves mitochondrial membrane homeostasis via STARD 7 processing and is emerging as a critical regulator of protein localization between mitochondria and the cytosol.

Report this publication

Statistics

Seen <100 times