Protein degrons and degradation: Exploring substrate recognition and pathway selection in plants
- 3 May 2024
- journal article
- review article
- Published by Oxford University Press (OUP) in The Plant Cell
- Vol. 36 (9) , 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.Keywords
Funding Information
- Deutsche Forschungsgemeinschaft
- Heisenberg program
- Research Grant (441867841)
- RWTH Aachen University (2019-T1/BIO-13731)
- Spanish Agencia Estatal de Investigación (PID2020-118607RB-I00)
- European Research Council (101001137)
- Biotechnology and Biological Sciences Research Council (BB/S016767/1)
- National Natural Science Foundation of China (32222087)
- Research Grants Council of Hong Kong (N_CUHK405/20, 24108820, 14106622, 14110923)
This publication has 302 references indexed in Scilit:
- N‐degron specificity of chloroplast ClpS1 in plantsFEBS Letters, 2019
- Membrane Protein Quantity Control at the Endoplasmic ReticulumThe Journal of Membrane Biology, 2016
- Organization, function and substrates of the essential Clp protease system in plastidsBiochimica et Biophysica Acta (BBA) - Bioenergetics, 2015
- ERAD and ERAD tuning: disposal of cargo and of ERAD regulators from the mammalian ERCurrent Opinion in Cell Biology, 2011
- Quality and quantity control at the endoplasmic reticulumCurrent Opinion in Cell Biology, 2010
- Proteasome-Mediated Turnover of the Transcription Coactivator NPR1 Plays Dual Roles in Regulating Plant ImmunityCell, 2009
- Quantitative Proteomics Reveals the Function of Unconventional Ubiquitin Chains in Proteasomal DegradationCell, 2009
- Ubiquitin Chains Are Remodeled at the Proteasome by Opposing Ubiquitin Ligase and Deubiquitinating ActivitiesCell, 2006
- Sequence analysis of Arabidopsis thaliana E/ANTH-domain-containing proteins: membrane tethers of the clathrin-dependent vesicle budding machineryProtoplasma, 2005
- Plant Mitochondria Contain at Least Two i-AAA-like ComplexesPlant Molecular Biology, 2005