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Early fate decision for mitochondrially encoded proteins by a molecular triage

Kohler, Andreas, Dr. rer. nat. 1988- (author)
Stockholms universitet,Institutionen för biokemi och biofysik,Institutionen för molekylär biovetenskap, Wenner-Grens institut,University of Graz, Austria
Carlström, Andreas (author)
Stockholms universitet,Institutionen för biokemi och biofysik
Nolte, H. (author)
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Kohler, Verena, 1992- (author)
Stockholms universitet,Institutionen för molekylär biovetenskap, Wenner-Grens institut,University of Graz, Austria
Jung, Sung-Jun, 1987 (author)
Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi,Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Sridhara, Sagar, 1989 (author)
Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi,Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Tatsuta, T. (author)
Berndtsson, Jens, 1989- (author)
Stockholms universitet,Institutionen för biokemi och biofysik
Langer, T. (author)
Ott, Martin, 1974 (author)
Stockholms universitet,Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi,Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology,Institutionen för biokemi och biofysik,University of Gothenburg, Sweden
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 (creator_code:org_t)
Cell Press, 2023
2023
English.
In: Molecular Cell. - : Cell Press. - 1097-2765 .- 1097-4164. ; 83:19
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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.

Subject headings

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
NATURVETENSKAP  -- Biologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences (hsv//eng)

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