ABD1 Is an<i>Arabidopsis</i>DCAF Substrate Receptor for CUL4-DDB1–Based E3 Ligases That Acts as a Negative Regulator of Abscisic Acid Signaling

Seo, Kyoung‐In; Lee, Jae‐Hoon; Nezames, Cynthia D.; Zhong, Shangwei; Song, Eun-Young; Byun, Myung-Ok; Deng, Xing Wang

doi:10.1105/tpc.113.119974

Cited by 148 publications

(146 citation statements)

References 72 publications

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“…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

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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.

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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

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“…Although the half-life of MYC2 is prolonged in pub10 mutant, this factor continues to be unstable, suggesting that it is likely targeted by other E3 ligases. In addition, there have been several reports that a single transcription factor may be targeted by several E3 ligases (e.g., ABI5; Lee et al, 2010;Liu and Stone, 2010;Seo et al, 2014), whereas an E3 ligase may mediate degradation of several transcription factors (e.g., COP1; reviewed in Lau and Deng, 2012). Based on this scenario, we would expect MYC2 to be targeted by several E3 ligases and PUB10 to ubiquitinate other substrates.…”

Section: Pub10 Level or Activity Determines Myc2 Stability In Vivomentioning

confidence: 99%

PLANT U-BOX PROTEIN10 Regulates MYC2 Stability in Arabidopsis

et al. 2015

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MYC2 is an important regulator for jasmonic acid (JA) signaling, but little is known about its posttranslational regulation. Here, we show that the MYC2 C-terminal region interacted with the PLANT U-BOX PROTEIN10 (PUB10) armadillo repeats in vitro. MYC2 was efficiently polyubiquitinated by PUB10 with UBC8 as an E2 enzyme and the conserved C249 in PUB10 was required for activity. The inactive PUB10(C249A) mutant protein retained its ability to heterodimerize with PUB10, thus blocking PUB10 E3 activity as a dominant-negative mutant. Both MYC2 and PUB10 were nucleus localized and coimmunoprecipitation experiments confirmed their interaction in vivo. Although unstable in the wild type, MYC2 stability was enhanced in pub10, suggesting destabilization by PUB10. Moreover, MYC2 half-life was shortened or prolonged by induced expression of PUB10 or the dominant-negative PUB10(C249A) mutant, respectively. Root growth of pub10 seedlings phenocopied 35S:MYC2 seedlings and was hypersensitive to methyl jasmonate, whereas 35S:PUB10 and jin1-9 (myc2) seedlings were hyposensitive. In addition, the root phenotype conferred by MYC2 overexpression in double transgenic plants was reversed or enhanced by induced expression of PUB10 or PUB10(C249A), respectively. Similar results were obtained with three other JA-regulated genes, TAT, JR2, and PDF1.2. Collectively, our results show that MYC2 is targeted by PUB10 for degradation during JA responses.

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“…Although the ); therefore, it is probable that AFP functions as a co-effector in the process of ABI5 3 degradation mediated by ubiquitination. 4 The predicted mechanism of AFP in the ABA pathway makes it essential to identify the 5 E3 ligase responsible for ubiquitination of ABI5 in the nucleus. It seems that Cul4-based E3 In particular, a demonstration of the interaction between ABD1 and ABI5 in the nucleus 18 provided direct evidence that ABD1 affects ABI5 stability in the nucleus (Seo et al, 2014).…”

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confidence: 99%

Ubiquitin–Proteasome System in ABA Signaling: From Perception to Action

2016

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Protein post-translational modification (PTM) by ubiquitination has been observed during many aspects of plant growth, development, and stress responses. The ubiquitin-proteasome system precisely regulates phytohormone signaling by affecting protein activity, localization, assembly, and interaction ability. Abscisic acid (ABA) is a major phytohormone, and plays important roles in plants under normal or stressed growth conditions. The ABA signaling pathway is composed of phosphatases, kinases, transcription factors, and membrane ion channels. It has been reported that multiple ABA signaling transducers are subjected to the regulations by ubiquitination. In particular, recent studies have identified different types of E3 ligases that mediate ubiquitination of ABA receptors in different cell compartments. This review focuses on modulation of these components by monoubiquitination or polyubiquitination that occurs in the plasma membrane, endomembranes, and from the cytosol to the nucleus; this implies the existence of retrograde and trafficking processes that are regulated by ubiquitination in ABA signaling. A number of single-unit E3 ligases, components of multi-subunit E3 ligases, E2s, and specific subunits of the 26S proteasome involved in ABA signal regulation are discussed. Dissecting the precise functions of ubiquitination in the ABA pathway may help us understand key factors in the signaling of other phytohormones regulated by ubiquitination and other types of PTMs.

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ABD1 Is anArabidopsisDCAF Substrate Receptor for CUL4-DDB1–Based E3 Ligases That Acts as a Negative Regulator of Abscisic Acid Signaling

Cited by 148 publications

References 72 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

PLANT U-BOX PROTEIN10 Regulates MYC2 Stability in Arabidopsis

Ubiquitin–Proteasome System in ABA Signaling: From Perception to Action

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