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

Saita, S., Tatsuta, T., Lampe, P. A., Konig, T., Ohba, Y., & Langer, T. (2018). PARL partitions the lipid transfer protein STARD7 between the cytosol and mitochondria. EMBO J. doi:10.15252/embj.201797909.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0004-7224-3 Version Permalink: http://hdl.handle.net/21.11116/0000-0004-739F-8
Genre: Journal Article

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 Creators:
Saita, S.1, Author
Tatsuta, T.1, Author
Lampe, P. A.1, Author
Konig, T.1, Author
Ohba, Y.1, Author
Langer, T.1, Author
Affiliations:
1Max Planck Institute for Biology of Ageing, Max Planck Society, Joseph-Stelzmann-Str. 9b, D-50931 Cologne, DE, ou_1942284              

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Free keywords: Parl Stard7 lipid transfer protein mitochondria rhomboid
 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 STARD7 as an intramitochondrial lipid transfer protein for phosphatidylcholine. We demonstrate that PARL-mediated cleavage during mitochondrial import partitions STARD7 to the cytosol and the mitochondrial intermembrane space. Negatively charged amino acids in STARD7 serve as a sorting signal allowing mitochondrial release of mature STARD7 upon cleavage by PARL On the other hand, membrane insertion of STARD7 mediated by the TIM23 complex promotes mitochondrial localization of mature STARD7. Mitochondrial STARD7 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 STARD7 processing and is emerging as a critical regulator of protein localization between mitochondria and the cytosol.

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 Dates: 2018-01-042018-01-06
 Publication Status: Published in print
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 Identifiers: Other: 29301859
DOI: 10.15252/embj.201797909
ISSN: 1460-2075 (Electronic)0261-4189 (Linking)
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Title: EMBO J
Source Genre: Journal
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