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Cotranslational sorting and processing of newly synthesized proteins in eukaryotes

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2024

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Trends in Biochemical Sciences. Elsevier. 2024, 49(2), pp. 105-118. ISSN 0968-0004. eISSN 1362-4326. Available under: doi: 10.1016/j.tibs.2023.10.003

Zusammenfassung

Ribosomes interact with a variety of different protein biogenesis factors that guide newly synthesized proteins to their native 3D shapes and cellular localization. Depending on the type of translated substrate, a distinct set of cotranslational factors must interact with the ribosome in a timely and coordinated manner to ensure proper protein biogenesis. While cytonuclear proteins require cotranslational maturation and folding factors, secretory proteins must be maintained in an unfolded state and processed cotranslationally by transport and membrane translocation factors. Here we explore the specific cotranslational processing steps for cytonuclear, secretory, and membrane proteins in eukaryotes and then discuss how the nascent polypeptide-associated complex (NAC) cotranslationally sorts these proteins into the correct protein biogenesis pathway.

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570 Biowissenschaften, Biologie

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ISO 690GAMERDINGER, Martin, Elke DEUERLING, 2024. Cotranslational sorting and processing of newly synthesized proteins in eukaryotes. In: Trends in Biochemical Sciences. Elsevier. 2024, 49(2), pp. 105-118. ISSN 0968-0004. eISSN 1362-4326. Available under: doi: 10.1016/j.tibs.2023.10.003
BibTex
@article{Gamerdinger2024Cotra-69566,
  year={2024},
  doi={10.1016/j.tibs.2023.10.003},
  title={Cotranslational sorting and processing of newly synthesized proteins in eukaryotes},
  number={2},
  volume={49},
  issn={0968-0004},
  journal={Trends in Biochemical Sciences},
  pages={105--118},
  author={Gamerdinger, Martin and Deuerling, Elke}
}
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