Ubiquitin-Mediated Control of Plant Hormone Signaling
Ubiquitin-Mediated Control of Plant Hormone Signaling
复制标题
DOI:
10.1104/pp.112.200527
复制
发表时间:
2012-09-01
期刊:
影响因子:
7.4
通讯作者:
Estelle, Mark
中科院分区:
文献类型:
--
作者:
Kelley, Dior R.;Estelle, Mark
The ubiquitin-proteasome system (UPS) plays a role in nearly every aspect of plant biology. The wealth of emerging data demonstrates that regulated protein degradation rivals the well-studied area of transcriptional regulation for importance in cellular regulation. In this Update, we will highlight current research findings that illustrate the contributions of the UPS to phytohormone signaling. We will also consider outstanding questions and discuss possible experimental approaches that will increase our understanding of regulated protein degradation. UPS activity involves a three-step enzymatic cascade between E1, E2, and E3 enzymes that results in the covalent transfer of ubiquitin to target proteins. This process can result in different outcomes, including (1) proteolytic degradation by the 26S proteasome or reversible, nonproteolytic regulatory events. Current plant genome annotations indicate that most species can produce over 1,000 different UPS components; E3 ligase family proteins are the most abundant (Du et al., 2009; Vierstra, 2009). Thus, the potential scope of the UPS is extensive. E3 ligases provide specificity by directly controlling the transfer of ubiquitin to the target substrate and have been classified into four groups based on their complex composition and modes of action: HECT, RING, U-box, and cullin-RING ligases (CRLs; Vierstra, 2009). CRLs are multisubunit ligases that can be further subdivided into four groups based on a variable target recognition module:(1) F-box proteins in the case of S-phase kinase-associated protein1-cullin1-F-box (SCF) ligases;(2) bric-a-brac-tramtrak-broad complex (BTB) proteins that define the BTB group of E3s;(3) the DNA damage-binding (DDB) class that utilizes WD40 domain-containing DWD proteins; and (4) the anaphase-promoting complex category that contains several interchangeable recognition proteins (Vierstra, 2009). Altogether, these enzymatic modules are incredibly diverse, and many of their targets are currently unknown.