Plant E3 ligases: flexible enzymes in a sessile world

Liyuan Chen; Hanjo Hellmann

doi:10.1093/mp/sst005

Back

Plant E3 ligases: flexible enzymes in a sessile world

Journal article

Open access

Peer reviewed

Plant E3 ligases: flexible enzymes in a sessile world

Liyuan Chen and Hanjo Hellmann

Molecular plant, Vol.6(5), pp.1388-1404

09/2013

DOI: https://doi.org/10.1093/mp/sst005

Handle:

https://hdl.handle.net/2376/113352

PMID: 23307436

Files and links (1)

url

https://doi.org/10.1093/mp/sst005View

Published (Version of record) Open

Abstract

Ubiquitin-Protein Ligases - classification

Models, Biological

Ubiquitin-Protein Ligases - metabolism

Plants - enzymology

E3 ligases comprise a highly diverse and important group of enzymes that act within the 26S ubiquitin proteasome pathway. They facilitate the transfer of ubiquitin moieties to substrate proteins which may be marked for degradation by this step. As such, they serve as central regulators in many cellular and physiological processes in plants. The review provides an update on the multitude of different E3 ligases currently known in plants, and illustrates the central role in plant biology of specific examples.

Metrics

9 Record Views

See more details

Details

Title: Plant E3 ligases: flexible enzymes in a sessile world
Creators: Liyuan Chen - Plant Stress Physiology, School of Biological Sciences, Abelson 435, PO Box 644236, Washington State University, Pullman, WA 99164-4236, USA
Hanjo Hellmann
Publication Details: Molecular plant, Vol.6(5), pp.1388-1404
Academic Unit: Biological Sciences, School of
Publisher: England
Identifiers: 99900547534301842
Language: English
Resource Type: Journal article