Ling, Qihua, Broad, William, Trösch, Raphael, Töpel, Mats, Demiral Sert, Tijen, Lymperopoulos, Panagiotis, Baldwin, Amy ORCID: https://orcid.org/0000-0002-2162-3771 and Jarvis, R. Paul 2019. Ubiquitin-dependent chloroplast-associated protein degradation in plants. Science 363 (6429) , eaav4467. 10.1126/science.aav4467 |
Abstract
Protein degradation is vital for cellular functions, and it operates selectively with distinct mechanisms in different organelles. Some organellar proteins are targeted by the ubiquitin-proteasome system (UPS)—a major proteolytic network in the eukaryotic cytosol. In such cases, the organelle membrane presents a substantial barrier to protein degradation. Working in the model plant Arabidopsis, Ling et al. identified mechanisms underlying the UPS-mediated degradation of proteins in the outer membrane of chloroplasts (the organelles responsible for photosynthesis). They identified an Omp85-type β-barrel outer membrane channel and a cytosolic AAA+ chaperone that fulfill conductance and motor functions in the retrotranslocation of target proteins from chloroplasts. This process thus enabled outer membrane protein processing by the cytosolic proteasome. Such chloroplast-associated protein degradation was initiated by ubiquitination of the targets by the chloroplast-localized E3 ubiquitin ligase SP1.
Item Type: | Article |
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Date Type: | Publication |
Status: | Published |
Schools: | Biosciences |
Publisher: | American Association for the Advancement of Science |
ISSN: | 0036-8075 |
Date of Acceptance: | 15 January 2019 |
Last Modified: | 25 Oct 2022 13:25 |
URI: | https://orca.cardiff.ac.uk/id/eprint/119780 |
Citation Data
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