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 determinant 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 multisubunit E3 ligase complexes.
| Original language | English |
|---|---|
| Pages (from-to) | 201-208 |
| Number of pages | 8 |
| Journal | Molecules and cells |
| Volume | 31 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 2011 Mar 1 |
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All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology
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Regulation of abiotic stress signal transduction by E3 ubiquitin ligases in arabidopsis. / Lee, Jae Hoon; Kim, Woo Taek.
In: Molecules and cells, Vol. 31, No. 3, 01.03.2011, p. 201-208.Research output: Contribution to journal › Review article
TY - JOUR
T1 - Regulation of abiotic stress signal transduction by E3 ubiquitin ligases in arabidopsis
AU - Lee, Jae Hoon
AU - Kim, Woo Taek
PY - 2011/3/1
Y1 - 2011/3/1
N2 - 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 determinant 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 multisubunit E3 ligase complexes.
AB - 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 determinant 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 multisubunit E3 ligase complexes.
UR - http://www.scopus.com/inward/record.url?scp=79959952615&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=79959952615&partnerID=8YFLogxK
U2 - 10.1007/s10059-011-0031-9
DO - 10.1007/s10059-011-0031-9
M3 - Review article
C2 - 21347703
AN - SCOPUS:79959952615
VL - 31
SP - 201
EP - 208
JO - Molecules and Cells
JF - Molecules and Cells
SN - 1016-8478
IS - 3
ER -