期刊
EMBO JOURNAL
卷 42, 期 14, 页码 -出版社
WILEY
DOI: 10.15252/embj.2022112534
关键词
autophagy; chloroplast; NBR1; protein import; stress response
This study reveals that the translocon at the outer envelope membrane of chloroplasts (TOC) can undergo K63-linked polyubiquitination and regulation by selective autophagy, potentially enhancing stress tolerance in plants. The selective autophagy adaptor NBR1 is found to target TOC components and mediate their relocation into vacuoles for autophagic degradation. This selective autophagy controls TOC protein levels, chloroplast protein import, and affects photosynthetic activity, UV-B irradiation, and heat stress tolerance in Arabidopsis plants.
Chloroplasts are plant organelles responsible for photosynthesis and environmental sensing. Most chloroplast proteins are imported from the cytosol through the translocon at the outer envelope membrane of chloroplasts (TOC). Previous work has shown that TOC components are regulated by the ubiquitin-proteasome system (UPS) to control the chloroplast proteome, which is crucial for the organelle's function and plant development. Here, we demonstrate that the TOC apparatus is also subject to K63-linked polyubiquitination and regulation by selective autophagy, potentially promoting plant stress tolerance. We identify NBR1 as a selective autophagy adaptor targeting TOC components, and mediating their relocation into vacuoles for autophagic degradation. Such selective autophagy is shown to control TOC protein levels and chloroplast protein import and to influence photosynthetic activity as well as tolerance to UV-B irradiation and heat stress in Arabidopsis plants. These findings uncover the vital role of selective autophagy in the proteolytic regulation of specific chloroplast proteins, and how dynamic control of chloroplast protein import is critically important for plants to cope with challenging environments.
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