Protein degrons and degradation: Exploring substrate recognition and pathway selection in plants
The Plant Cell, vol. 36, pp. 3074–3098
Abstract
Proteome composition is dynamic and influenced by many internal and external cues, including developmental signals, light availability, or environmental stresses. Protein degradation, in synergy with protein biosynthesis, allows cells to respond to various stimuli and adapt by reshaping the proteome. Protein degradation mediates the final and irreversible disassembly of proteins, which is important for protein quality control and to eliminate misfolded or damaged proteins, as well as entire organelles. Consequently, it contributes to cell resilience by buffering against protein or organellar damage caused by stresses. Moreover, protein degradation plays important roles in cell signaling, as well as transcriptional and translational events. The intricate task of recognizing specific proteins for degradation is achieved by specialized systems that are tailored to the substrate's physicochemical properties and subcellular localization. These systems recognize diverse substrate cues collectively referred to as "degrons," which can assume a range of configurations. They are molecular surfaces recognized by E3 ligases of the ubiquitin-proteasome system but can also be considered as general features recognized by other degradation systems, including autophagy or even organellar proteases. Here we provide an overview of the newest developments in the field, delving into the intricate processes of protein recognition and elucidating the pathways through which they are recruited for degradation.
Authors 8
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Affiliation as printed
Department of Biology, University of Konstanz , 78457 Konstanz , Germany
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Affiliation as printed
Department of Biology, Hong Kong Baptist University , Kowloon Tong , Hong Kong
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Consejo Superior de Investigaciones Científicas · Centro Nacional de Biotecnología
Affiliation as printed
Department of Plant Molecular Genetics, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (CNB-CSIC) , 28049 Madrid , Spain
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Affiliation as printed
Department of Biology, Aachen RWTH University, Institute of Molecular Plant Physiology , 52074 Aachen , Germany
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Affiliation as printed
Institute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh , Edinburgh EH9 3BF , UK
University of Edinburgh, Institute of Molecular Plant Sciences, School of Biological Sciences, Edinburgh, United Kingdom
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Affiliation as printed
Institute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh , Edinburgh EH9 3BF , UK
University of Edinburgh, Institute of Molecular Plant Sciences, School of Biological Sciences, Edinburgh, United Kingdom
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Chinese University of Hong Kong
Affiliation as printed
School of Life Sciences, Centre for Cell and Developmental Biology and State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong , Shatin, New Territories, Hong Kong , China
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Affiliation as printed
Department of Biology, Aachen RWTH University, Institute of Molecular Plant Physiology , 52074 Aachen , Germany
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