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

Lee, Jae‐Hoon; Yoon, Hye‐Jin; Terzaghi, William; Martı́nez, Consuelo; Dai, Mingqiu; Li, Jigang; Byun, Myung-Ok; Deng, Xing Wang

doi:10.1105/tpc.109.073783

Cited by 236 publications

(280 citation statements)

References 69 publications

Supporting

Mentioning

268

Contrasting

Unclassified

Order By: Relevance

“…ABI5, for example, is also targeted by the CUL4-based E3 ligases ABSCISIC ACID-HYPERSENSITIVE DAMAGED DNA BINDING PRO-TEIN1 (DDB1)-CULLIN4-associated factor1 (ABD1) and DDB1 binding WD40 HYPERSENSITIVE TO ABSCISIC ACID2 (DWA1)/DWA2 besides KEG (Lee et al, 2010;Seo et al, 2014). Unexpectedly, however, our results did not support our intuitive hypothesis of KEG as an instigator of JAZ12 ubiquitination and subsequent degradation.…”

Section: Toward a Functional Role For The Keg-jaz12 Interactioncontrasting

confidence: 57%

The RING E3 Ligase KEEP ON GOING Modulates JASMONATE ZIM-DOMAIN12 Stability

et al. 2015

View full text Add to dashboard Cite

Jasmonate (JA) signaling in plants is mediated by the JASMONATE ZIM-DOMAIN (JAZ) proteins that repress the activity of several transcription factors regulating JA-inducible gene expression. The hormone JA-isoleucine triggers the interaction of JAZ repressor proteins with the F-box protein CORONATINE INSENSITIVE1 (COI1), part of an S-phase kinase-associated protein1/Cullin1/F-box protein COI1 (SCF COI1 ) E3 ubiquitin ligase complex, and their degradation by the 26S proteasome. In Arabidopsis (Arabidopsis thaliana), the JAZ family consists of 13 members. The level of redundancy or specificity among these members is currently not well understood. Here, we characterized JAZ12, encoded by a highly expressed JAZ gene. JAZ12 interacted with the transcription factors MYC2, MYC3, and MYC4 in vivo and repressed MYC2 activity. Using tandem affinity purification, we found JAZ12 to interact with SCF COI1 components, matching with observed in vivo ubiquitination and with rapid degradation after treatment with JA. In contrast to the other JAZ proteins, JAZ12 also interacted directly with the E3 RING ligase KEEP ON GOING (KEG), a known repressor of the ABSCISIC ACID INSENSITIVE5 transcription factor in abscisic acid signaling. To study the functional role of this interaction, we circumvented the lethality of keg loss-of-function mutants by silencing KEG using an artificial microRNA approach. Abscisic acid treatment promoted JAZ12 degradation, and KEG knockdown led to a decrease in JAZ12 protein levels. Correspondingly, KEG overexpression was capable of partially inhibiting COI1-mediated JAZ12 degradation. Our results provide additional evidence for KEG as an important factor in plant hormone signaling and a positive regulator of JAZ12 stability.

show abstract

Section: Toward a Functional Role For The Keg-jaz12 Interactioncontrasting

confidence: 57%

The RING E3 Ligase KEEP ON GOING Modulates JASMONATE ZIM-DOMAIN12 Stability

et al. 2015

View full text Add to dashboard Cite

show abstract

“…A Cullin-based RING E3 ligase complex, which utilize DWD hypersensitive to ABA 1 (DWA1) and DWA2 as substrate receptors has also been identified as a negative regulator of ABI5 protein abundance (32). Evidence for DWA1/2 involvement in regulating ABI5 abundance comes from the observation that dwa1 or dwa2 single or double mutant plants accumulate higher levels of ABI5 than wild type plants following treatment with ABA (32). Although KEG and DWA1/2 regulate ABI5 stability they do so under different circumstances.…”

Section: Discussionmentioning

confidence: 99%

Cytoplasmic Degradation of the Arabidopsis Transcription Factor ABSCISIC ACID INSENSITIVE 5 Is Mediated by the RING-type E3 Ligase KEEP ON GOING

Liu

Stone

2013

Journal of Biological Chemistry

113

105

View full text Add to dashboard Cite

Background: KEEP ON GOING (KEG) is required to maintain low levels of the nuclear-localized transcription factor ABI5. Results: KEG-mediated degradation of ABI5 occurs in the cytoplasm/trans-Golgi network/early endosome and requires a C-terminal lysine residue. Conclusion: Cytoplasmic degradation prevents nuclear accumulation of ABI5 so as to prohibit ABA signaling. Significance: Knowing how ABI5 stability is controlled is crucial to understanding ABA signaling and plant survival of environmental stress.

show abstract

“…Thus, DOR is thought to function as a negative regulator in ABA-mediated guard cell signaling (Zhang et al, 2008c). DWD hypersensitive to ABA1 (DWA1) and DWA2 have also been reported as negative regulators in ABA signal transduction pathways (Lee et al, 2010). Both proteins possess DWD domains, the conserved domain found in most substrate receptors for Cullin4-RING ubiquitin E3 ligases (CRL4), and interact with components of the CRL4 complex such as DDB1 and CUL4 in vivo, indicating they function as substrate receptors for CRL4.…”

Section: A B C Dmentioning

confidence: 99%

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

Lee

Kim

2011

Molecules and Cells

Self Cite

163

105

View full text Add to dashboard Cite

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.

show abstract

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

Cited by 236 publications

References 69 publications

The RING E3 Ligase KEEP ON GOING Modulates JASMONATE ZIM-DOMAIN12 Stability

The RING E3 Ligase KEEP ON GOING Modulates JASMONATE ZIM-DOMAIN12 Stability

Cytoplasmic Degradation of the Arabidopsis Transcription Factor ABSCISIC ACID INSENSITIVE 5 Is Mediated by the RING-type E3 Ligase KEEP ON GOING

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

Contact Info

Product

Resources

About