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Updated: Jul 2, 2025

Assaying Proteasomal Degradation in a Cell-free System in Plants
Published on: March 26, 2014
Insights into a functional model of key deubiquitinases UBP12/13 in plants
Shiqi Zhang1, Ningning Hu1, Feifei Yu1
1College of Grassland Science and Technology, China Agricultural University, Beijing, 100083, China.
Abstract:
Understanding the complexities of protein ubiquitination is crucial, as it plays a multifaceted role in controlling protein stability, activity, subcellular localization, and interaction, which are central to diverse biological processes. Deubiquitinases (DUBs) serve to reverse ubiquitination, but research progress in plant DUBs is noticeably limited. Among existing studies, UBIQUITIN-SPECIFIC PROTEASE 12 (UBP12) and UBP13 have garnered attention for their extensive role in diverse biological processes in plants. This review systematically summarizes the recent advancements in UBP12/13 studies, emphasizing their function, and their substrate specificity, their relationship with E3 ubiquitin ligases, and the similarities and differences with their mammalian orthologue, USP7. By unraveling the molecular mechanisms of UBP12/13, this review offers in-depth insights into the ubiquitin-proteasome system (UPS) in plants and aims to catalyze further explorations and comprehensive understanding in this field.
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