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Early fate decision for mitochondrially encoded proteins by a molecular triage
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2023 (English)In: Molecular Cell, ISSN 1097-2765, E-ISSN 1097-4164, Vol. 83, no 19, p. 3470-3484Article in journal (Refereed) Published
Abstract [en]

Folding of newly synthesized proteins poses challenges for a functional proteome. Dedicated protein quality control (PQC) systems either promote the folding of nascent polypeptides at ribosomes or, if this fails, ensure their degradation. Although well studied for cytosolic protein biogenesis, it is not understood how these processes work for mitochondrially encoded proteins, key subunits of the oxidative phosphorylation (OXPHOS) system. Here, we identify dedicated hubs in proximity to mitoribosomal tunnel exits coordinating mitochondrial protein biogenesis and quality control. Conserved prohibitin (PHB)/m-AAA protease supercomplexes and the availability of assembly chaperones determine the fate of newly synthesized proteins by molecular triaging. The localization of these competing activities in the vicinity of the mitoribosomal tunnel exit allows for a prompt decision on whether newly synthesized proteins are fed into OXPHOS assembly or are degraded.

Place, publisher, year, edition, pages
Cell Press, 2023. Vol. 83, no 19, p. 3470-3484
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-214999DOI: 10.1016/j.molcel.2023.09.001OAI: oai:DiVA.org:umu-214999DiVA, id: diva2:1802771
Available from: 2023-10-05 Created: 2023-10-05 Last updated: 2023-10-16Bibliographically approved

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Kohler, AndreasKohler, Verena

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Kohler, AndreasKohler, VerenaOtt, Martin
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CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf