CUL3 E3 ligases in plant development and environmental response

被引:61
作者
Ban, Zhaonan [1 ]
Estelle, Mark [1 ]
机构
[1] Univ Calif San Diego, Sect Cell & Dev Biol, La Jolla, CA 92093 USA
基金
美国国家卫生研究院;
关键词
UBIQUITIN LIGASES; BTB PROTEIN; SIGNAL TRANSDUCER; ORDER OLIGOMERIZATION; MEDIATED DEGRADATION; PHOTOTROPIC RESPONSE; TRANSCRIPTION FACTOR; SUBSTRATE ADAPTERS; STRUCTURAL BASIS; GENE-EXPRESSION;
D O I
10.1038/s41477-020-00833-6
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Thirty years of research have revealed the fundamental role of the ubiquitin-proteasome system in diverse aspects of cellular regulation in eukaryotes. The ubiquitin-protein ligases or E3s are central to the ubiquitin-proteasome system since they determine the specificity of ubiquitylation. The cullin-RING ligases (CRLs) constitute one large class of E3s that can be subdivided based on the cullin isoform and the substrate adapter. SCF complexes, composed of CUL1 and the SKP1/F-box protein substrate adapter, are perhaps the best characterized in plants. More recently, accumulating evidence has demonstrated the essential roles of CRL3 E3s, consisting of a CUL3 protein and a BTB/POZ substrate adaptor. In this Review, we describe the variety of CRL3s functioning in plants and the wide range of processes that they regulate. Furthermore, we illustrate how different classes of E3s may cooperate to regulate specific pathways or processes. Cullin3-RING ligases (CRL3s) are a subclass of the vast family of ubiquitin E3 ligases. This Review comprehensively explores the role of CLR3 proteins in various biological processes, in light of exciting recent discoveries.
引用
收藏
页码:6 / 16
页数:11
相关论文
共 122 条
[11]   Identification of Arabidopsis MYB56 as a Novel Substrate for CRL3BPM E3 Ligases [J].
Chen, Liyuan ;
Bernhardt, Anne ;
Lee, JooHyun ;
Hellmann, Hanjo .
MOLECULAR PLANT, 2015, 8 (02) :242-250
[12]   Plant E3 Ligases: Flexible Enzymes in a Sessile World [J].
Chen, Liyuan ;
Hellmann, Hanjo .
MOLECULAR PLANT, 2013, 6 (05) :1388-1404
[13]   Arabidopsis BPM Proteins Function as Substrate Adaptors to a CULLIN3-Based E3 Ligase to Affect Fatty Acid Metabolism in Plants [J].
Chen, Liyuan ;
Lee, Joo Hyun ;
Weber, Henriette ;
Tohge, Takayuki ;
Witt, Sandra ;
Roje, Sanja ;
Fernie, Alisdair R. ;
Hellmann, Hanjo .
PLANT CELL, 2013, 25 (06) :2253-2264
[14]   NPY1 a BTB-NPH3-like protein, plays a critical role in auxin-regulated organogenesis in Arabidopsis [J].
Cheng, Youfa ;
Qin, Genji ;
Dai, Xinhua ;
Zhao, Yunde .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2007, 104 (47) :18825-18829
[15]   The Light-Response BTB1 and BTB2 Proteins Assemble Nuclear Ubiquitin Ligases That Modify Phytochrome B and D Signaling in Arabidopsis [J].
Christians, Matthew J. ;
Gingerich, Derek J. ;
Hua, Zhihua ;
Lauer, Timothy D. ;
Vierstra, Richard D. .
PLANT PHYSIOLOGY, 2012, 160 (01) :118-134
[16]   The BTB ubiquitin ligases ETO1, EOL1 and EOL2 act collectively to regulate ethylene biosynthesis in Arabidopsis by controlling type-2 ACC synthase levels [J].
Christians, Matthew J. ;
Gingerich, Derek J. ;
Hansen, Maureen ;
Binder, Brad M. ;
Kieber, Joseph J. ;
Vierstra, Richard D. .
PLANT JOURNAL, 2009, 57 (02) :332-345
[17]   TPR proteins: the versatile helix [J].
D'Andrea, LD ;
Regan, L .
TRENDS IN BIOCHEMICAL SCIENCES, 2003, 28 (12) :655-662
[18]   Molecular and functional characterization of Arabidopsis Cullin 3A [J].
Dieterle, M ;
Thomann, A ;
Renou, JP ;
Parmentier, Y ;
Cognat, V ;
Lemonnier, G ;
Müller, R ;
Shen, WH ;
Kretsch, T ;
Genschik, P .
PLANT JOURNAL, 2005, 41 (03) :386-399
[19]   Light-Dependent Degradation of PIF3 by SCFEBF1/2 Promotes a Photomorphogenic Response in Arabidopsis [J].
Dong, Jie ;
Ni, Weimin ;
Yu, Renbo ;
Deng, Xing Wang ;
Chen, Haodong ;
Wei, Ning .
CURRENT BIOLOGY, 2017, 27 (16) :2420-+
[20]   Ca2+/calmodulin regulates salicylic-acid-mediated plant immunity [J].
Du, Liqun ;
Ali, Gul S. ;
Simons, Kayla A. ;
Hou, Jingguo ;
Yang, Tianbao ;
Reddy, A. S. N. ;
Poovaiah, B. W. .
NATURE, 2009, 457 (7233) :1154-U116