Ubiquitin, hormones and biotic stress in plants

被引:407
作者
Dreher, Kate [1 ]
Callis, Judy [1 ]
机构
[1] Univ Calif Davis, Sect Mol & Cellular Biol, Plant Biol Grad Grp Program, Davis, CA 95616 USA
关键词
ubiquitin; E3; ligase; RING; U-Box; SCF; CRL; ubiquitylation; regulated proteolysis; plant defence; hormonal signalling; biotic stress; pathogen response;
D O I
10.1093/aob/mcl255
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Background The covalent attachment of ubiquitin to a substrate protein changes its fate. Notably, proteins typically tagged with a lysine48-linked polyubiquitin chain become substrates for degradation by the 26S proteasome. In recent years many experiments have been performed to characterize the proteins involved in the ubiquitylation process and to identify their substrates, in order to understand better the mechanisms that link specific protein degradation events to regulation of plant growth and development. Scope This review focuses on the role that ubiquitin plays in hormone synthesis, hormonal signalling cascades and plant defence mechanisms. Several examples are given of how targeted degradation of proteins affects downstream transcriptional regulation of hormone-responsive genes in the auxin, gibberellin, abscisic acid, ethylene and jasmonate signalling pathways. Additional experiments suggest that ubiquitin-mediated proteolysis may also act upstream of the hormonal signalling cascades by regulating hormone biosynthesis, transport and perception. Moreover, several experiments demonstrate that hormonal cross-talk can occur at the level of proteolysis. The more recently established role of the ubiquitin/proteasome system (UPS) in defence against biotic threats is also reviewed. Conclusions The UPS has been implicated in the regulation of almost every developmental process in plants, from embryogenesis to floral organ production probably through its central role in many hormone pathways. More recent evidence provides molecular mechanisms for hormonal cross-talk and links the UPS system to biotic defence responses.
引用
收藏
页码:787 / 822
页数:36
相关论文
共 351 条
[1]   Intracellular trafficking and proteolysis of the Arabidopsis auxin-efflux facilitator PIN2 are involved in root gravitropism [J].
Abas, L ;
Benjamins, R ;
Malenica, N ;
Paciorek, T ;
Wirniewska, J ;
Moulinier-Anzola, JC ;
Sieberer, T ;
Friml, J ;
Luschnig, C .
NATURE CELL BIOLOGY, 2006, 8 (03) :249-256
[2]   Type III effector AvrPtoB requires intrinsic E3 ubiquitin ligase activity to suppress plant cell death and immunity [J].
Abramovitch, RB ;
Janjusevic, R ;
Stebbins, CE ;
Martin, GB .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (08) :2851-2856
[3]   Integration of plant responses to environmentally activated phytohormonal signals [J].
Achard, P ;
Cheng, H ;
De Grauwe, L ;
Decat, J ;
Schoutteten, H ;
Moritz, T ;
Van Der Straeten, D ;
Peng, JR ;
Harberd, NP .
SCIENCE, 2006, 311 (5757) :91-94
[4]   Ethylene regulates Arabidopsis development via the modulation of DELLA protein growth repressor function [J].
Achard, P ;
Vriezen, WH ;
Van Der Straeten, D ;
Harberd, NP .
PLANT CELL, 2003, 15 (12) :2816-2825
[5]   The ethylene signaling pathway [J].
Alonso, JM ;
Stepanova, AN .
SCIENCE, 2004, 306 (5701) :1513-1515
[6]   The HVE/CAND1 gene is required for the early patterning of leaf venation in Arabidopsis [J].
Alonso-Peral, Maria Magdalena ;
Candela, Hector ;
del Pozo, Juan Carlos ;
Martinez-Laborda, Antonio ;
Ponce, Maria Rosa ;
Micol, Jose Luis .
DEVELOPMENT, 2006, 133 (19) :3755-3766
[7]   Gibberellins signal nuclear import of PHOR1, a photoperiod-responsive protein with homology to Drosophila armadillo [J].
Amador, V ;
Monte, E ;
García-Martínez, JL ;
Prat, S .
CELL, 2001, 106 (03) :343-354
[8]   Structure and biochemical function of a prototypical Arabidopsis U-box domain [J].
Andersen, P ;
Kragelund, BM ;
Olsen, AN ;
Larsen, FH ;
Chua, NH ;
Poulsen, FM ;
Skriver, K .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (38) :40053-40061
[9]   Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery [J].
Angers, Stephane ;
Li, Ti ;
Yi, Xianhua ;
MacCoss, Michael J. ;
Moon, Randall T. ;
Zheng, Ning .
NATURE, 2006, 443 (7111) :590-593
[10]   Fold prediction and evolutionary analysis of the POZ domain: Structural and evolutionary relationship with the potassium channel tetramerization domain [J].
Aravind, L ;
Koonin, EV .
JOURNAL OF MOLECULAR BIOLOGY, 1999, 285 (04) :1353-1361