Plant CULLIN‐based E3s: Phytohormones come first

Thomann, Alexis; Dieterle, Monika; Genschik, Pascal

doi:10.1016/j.febslet.2005.02.068

Cited by 44 publications

(33 citation statements)

References 66 publications

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“…It has been reported that signal transduction pathways for many plant hormones, including auxin, gibberellin, ethylene, jasmonic acid, and ABA, use ubiquitin-mediated selective protein degradation for their downstream effects (Smalle and Vierstra, 2004). Although there have been several reports about roles of E3 ligases including CRLs in plant hormonal responses, the connection between CRLs and ABA responses is elusive (Thomann et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

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DWA1 and DWA2, Two Arabidopsis DWD Protein Components of CUL4-Based E3 Ligases, Act Together as Negative Regulators in ABA Signal Transduction

et al. 2010

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To elucidate potential roles of CUL4-DDB1-DWD (for Cullin 4-Damaged DNA Binding1-DDB1 binding WD40) E3 ligases in abscisic acid (ABA) signaling, we examined ABA sensitivities of T-DNA mutants of a number of Arabidopsis thaliana DWD genes, which encode substrate receptors for CUL4 E3 ligases. Mutants in two DWD genes, DWA1 and DWA2 (DWD hypersensitive to ABA1 and 2), had ABA-hypersensitive phenotypes. Both proteins interacted with DDB1 in yeast two-hybrid assays and associated with DDB1 and CUL4 in vivo, implying they could form CUL4-based complexes. Several ABAresponsive genes were hyperinduced in both mutants, and the ABA-responsive transcription factors ABA INSENSITIVE 5 (ABI5) and MYC2 accumulated to high levels in the mutants after ABA treatment. Moreover, ABI5 interacted with DWA1 and DWA2 in vivo. Cell-free degradation assays showed ABI5 was degraded more slowly in dwa1 and dwa2 than in wild-type cell extracts. Therefore, DWA1 and/or DWA2 may be the substrate receptors for a CUL4 E3 ligase that targets ABI5 for degradation. Our data indicate that DWA1 and DWA2 can directly interact with each other, and their double mutants exhibited enhanced ABA and NaCl hypersensitivities, implying they can act together. This report thus describes a previously unknown heterodimeric cooperation between two independent substrate receptors for CUL4-based E3 ligases.

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Section: Discussionmentioning

confidence: 99%

“…The most abundant family uses cullins as scaffold proteins to form a framework for assembling the Cullin-RING ubiquitin E3 ligase (CRL), the ubiquitination machinery (Petroski and Deshaies, 2005;Thomann et al, 2005). All cullin family members commonly possess two essential modules assembled on the cullin protein.…”

Section: Introductionmentioning

confidence: 99%

DWA1 and DWA2, Two Arabidopsis DWD Protein Components of CUL4-Based E3 Ligases, Act Together as Negative Regulators in ABA Signal Transduction

et al. 2010

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“…In addition to cullin proteins, two other modules are required for the complex: the RING finger protein, RBX1, which recruits E2, and the substrate-recognition module that contains the adaptor and substrate receptor. After all proteins are assembled, the complex acts as an E3 ligase for subsequent target modification (Petroski and Deshaies, 2005;Schwechheimer and Calderon Villalobos, 2004;Thomann et al, 2005) (Fig. 1B).…”

Section: Single-subunit E3 Ligasesmentioning

confidence: 99%

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

Lee

Kim

2011

Molecules and Cells

160

105

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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.

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“…Most of the E3 ubiquitin ligases characterised up-to-date act in regulating plant development and hormone signaling [74,75] (Table 2). Notably, an effect frequently observed in E3 ligase Arabidopsis insertional mutants is the arrest of embryo development.…”

Section: Ubiquitin-mediated Degradation: a Re-current Theme In Plant mentioning

confidence: 99%

The E3 Ubiquitin Ligase Gene Family in Plants: Regulation by Degradation

Mazzucotelli

Belloni²,

Marone³

et al. 2006

238

178

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Abstract:The regulation of protein expression and activity has been for long time considered only in terms of transcription/translation efficiency. In the last years, the discovery of post-transcriptional and post-translational regulation mechanisms pointed out that the key factor in determining transcript/protein amount is the synthesis/degradation ratio, together with post-translational modifications of proteins. Polyubiquitinaytion marks target proteins directed to degradation mediated by 26S-proteasome. Recent functional genomics studies pointed out that about 5% of Arabidopsis genome codes for proteins of ubiquitination pathway. The most of them (more than one thousand genes) correspond to E3 ubiquitin ligases that specifically recognise target proteins. The huge size of this gene family, whose members are involved in regulation of a number of biological processes including hormonal control of vegetative growth, plant reproduction, light response, biotic and abiotic stress tolerance and DNA repair, indicates a major role for protein degradation in control of plant life.

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Plant CULLIN‐based E3s: Phytohormones come first

Cited by 44 publications

References 66 publications

DWA1 and DWA2, Two Arabidopsis DWD Protein Components of CUL4-Based E3 Ligases, Act Together as Negative Regulators in ABA Signal Transduction

DWA1 and DWA2, Two Arabidopsis DWD Protein Components of CUL4-Based E3 Ligases, Act Together as Negative Regulators in ABA Signal Transduction

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

The E3 Ubiquitin Ligase Gene Family in Plants: Regulation by Degradation

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