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Mol. Cells 2011; 31(3): 201-208

Published online March 31, 2011

https://doi.org/10.1007/s10059-011-0031-9

© The Korean Society for Molecular and Cellular Biology

Regulation of Abiotic Stress Signal Transduction by E3 Ubiquitin Ligases in Arabidopsis

Jae-Hoon Lee1, and Woo Taek Kim*

Department of Biology, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Korea, 1Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520-8104, USA

Correspondence to : *Correspondence: wtkim@yonsei.ac.kr

Received: December 1, 2010; Revised: December 23, 2010; Accepted: December 24, 2010

Abstract

Ubiquitination is a unique protein degradation system utilized by eukaryotes to efficiently degrade detrimental cellular proteins and control the entire pool of regulatory components. In plants, adaptation in response to various abiotic stresses can be achieved through ubiquitination and the resulting degradation of components specific to these stress signalings. Arabidopsis has more than 1,400 E3 enzymes, indicating E3 ligase acts as a main determi-nant of substrate specificity. However, as only a minority of E3 ligases related to abiotic stress signaling have been studied in Arabidopsis, the further elucidation of the biological roles and related substrates of newly identified E3 ligases is essential in order to clarify the functional relationship between abiotic stress and E3 ligases. Here, we review the current knowledge and future prospects of the regulatory mechanism and role of several E3 ligases involved in abiotic stress signal transduction in Arabidopsis. As another potential approach to understand how ubiquitination is involved in such signaling, we also briefly introduce factors that regulate the activity of cullin in multi-subunit E3 ligase complexes.

Keywords 26S proteasome, abiotic stress signal transduction, Arabidopsis, E3 ubiquitin ligase, ubiquitination

Article

Minireview

Mol. Cells 2011; 31(3): 201-208

Published online March 31, 2011 https://doi.org/10.1007/s10059-011-0031-9

Copyright © The Korean Society for Molecular and Cellular Biology.

Regulation of Abiotic Stress Signal Transduction by E3 Ubiquitin Ligases in Arabidopsis

Jae-Hoon Lee1, and Woo Taek Kim*

Department of Biology, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Korea, 1Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520-8104, USA

Correspondence to:*Correspondence: wtkim@yonsei.ac.kr

Received: December 1, 2010; Revised: December 23, 2010; Accepted: December 24, 2010

Abstract

Ubiquitination is a unique protein degradation system utilized by eukaryotes to efficiently degrade detrimental cellular proteins and control the entire pool of regulatory components. In plants, adaptation in response to various abiotic stresses can be achieved through ubiquitination and the resulting degradation of components specific to these stress signalings. Arabidopsis has more than 1,400 E3 enzymes, indicating E3 ligase acts as a main determi-nant of substrate specificity. However, as only a minority of E3 ligases related to abiotic stress signaling have been studied in Arabidopsis, the further elucidation of the biological roles and related substrates of newly identified E3 ligases is essential in order to clarify the functional relationship between abiotic stress and E3 ligases. Here, we review the current knowledge and future prospects of the regulatory mechanism and role of several E3 ligases involved in abiotic stress signal transduction in Arabidopsis. As another potential approach to understand how ubiquitination is involved in such signaling, we also briefly introduce factors that regulate the activity of cullin in multi-subunit E3 ligase complexes.

Keywords: 26S proteasome, abiotic stress signal transduction, Arabidopsis, E3 ubiquitin ligase, ubiquitination

Mol. Cells
Jul 31, 2022 Vol.45 No.7, pp. 435~512
COVER PICTURE
Mesenchymal stem cells (MSCs) are multipotent stem cells capable of differentiating into mesodermal lineages like adipogenic, osteogenic, and chondrogenic. Alcian blue-positive extracellular matrix secreted by chondrocytes in the lacuna confirmed the chondrogenic differentiation of MSCs (Bashyal et al., pp. 479-494).

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