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Updated: Feb 25, 2026

Assaying Proteasomal Degradation in a Cell-free System in Plants
Published on: March 26, 2014
ESCRT-dependent degradation of ubiquitylated plasma membrane proteins in plants
Erika Isono1, Kamila Kalinowska2
1Department of Plant Sciences, School of Life Sciences Weihenstephan, Technical University of Munich, Emil-Ramann-Str. 8, 85456 Freising, Germany; Department of Biology, University of Konstanz, Universtitätsstrasse 10, 78464 Konstanz, Germany.
Abstract:
To control the abundance of plasma membrane receptors and transporters is crucial for proper perception and response to extracellular signals from surrounding cells and the environment. Posttranslational modification of plasma membrane proteins, especially ubiquitin conjugation or ubiquitylation, is key for the determination of stability for many transmembrane proteins localized on the cell surface. The targeted degradation is ensured by a complex network of proteins among which the endosomal sorting complex required for transport (ESCRT) plays a central role. This review focuses on progresses made in recent years on the understanding of the function of the ESCRT machinery in the degradation of ubiquitylated plasma membrane proteins in plants.
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