Biochemical Characterization of<i>Arabidopsis</i>Complexes Containing CONSTITUTIVELY PHOTOMORPHOGENIC1 and SUPPRESSOR OF PHYA Proteins in Light Control of Plant Development

Zhu, Danmeng; Maier, Alexander G.; Lee, Jae‐Hoon; Laubinger, Sascha; Saijo, Yusuke; Wang, Haiyang; Liu, Qu; Hoecker, Ute; Deng, Xing Wang

doi:10.1105/tpc.107.056580

Cited by 196 publications

(229 citation statements)

References 57 publications

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“…Similarly, SPAs (for SUPPRESSOR OF PHYA) 1, 2, 3, and 4 are highly homologous proteins that can form homo-or heterodimers. The diverse SPA complexes help repress photomorphogenesis by interacting with CONSTITUTIVELY PHOTOMORPHOGENIC1 (COP1), a central regulator in light signaling (Zhu et al, 2008).…”

Section: Discussionmentioning

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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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%

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 light signaling, the action of positive signaling factors is counterbalanced by a set of important repressor proteins, including COP1 and the four members of the SUPPRESSOR OF PHYA-105 (SPA) gene family, which interact and form complexes in vivo [29]. BBX24 was believed to form a negative regulatory network with these repressor proteins to fine-tune light-regulated gene expression and thereby preventing an exaggerated light response [16].…”

Section: Bbx24 May Function As a New Component Of The Negative Feedbamentioning

confidence: 99%

Arabidopsis STO/BBX24 negatively regulates UV-B signaling by interacting with COP1 and repressing HY5 transcriptional activity

et al. 2012

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UV-B (280-315 nm)is an integral part of solar radiation and can act either as a stress inducer or as a developmental signal. In recent years, increasing attention has been paid to the low-fluence UV-B-induced photomorphogenic response and several key players in this response have been identified, which include UVR8 (a UV-B-specific photoreceptor), COP1 (a WD40-repeat-containing RING finger protein), HY5 (a basic zipper transcription factor), and RUP1/2 (two UVR8-interacting proteins). Here we report that Arabidopsis SALT TOLERANCE (STO/BBX24), a known regulator for light signaling in plants, defines a new signaling component in UV-B-mediated photomorphogenesis. The bbx24 mutant is hypersensitive to UV-B radiation and becomes extremely dwarfed under UV-B treatment. By contrast, BBX24 overexpression transgenic lines respond much more weakly to UV-B than the bbx24 and wild-type plants. BBX24 expression is UV-B-inducible and its accumulation under UV-B requires COP1. Co-immunoprecipitation experiments indicate that BBX24 interacts with COP1

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“…COP1 forms multiple complexes with SUPPRESSOR OF PHYA-105 (SPA1-4) family members 5 . These complexes, either by themselves or by forming CUL4 COP1-SPA E3 ubiquitin ligases, degrade the positively acting transcription factors through the ubiquitin proteasome system (UPS) to repress photomorphogenesis in the dark 6 .…”

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CUL4 forms an E3 ligase with COP1 and SPA to promote light-induced degradation of PIF1

et al. 2015

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Plants undergo contrasting developmental programs in dark and light. Photomorphogenesis, a light-adapted programme is repressed in the dark by the synergistic actions of CUL4 COP1-SPA E3 ubiquitin ligase and a subset of basic helix-loop-helix transcription factors called phytochrome interacting factors (PIFs). To promote photomorphogenesis, light activates the phytochrome family of sensory photoreceptors, which inhibits these repressors by poorly understood mechanisms. Here, we show that the CUL4 COP1-SPA E3 ubiquitin ligase is necessary for the light-induced degradation of PIF1 in Arabidopsis. The light-induced ubiquitylation and subsequent degradation of PIF1 is reduced in the cop1, spaQ and cul4 backgrounds. COP1, SPA1 and CUL4 preferentially form complexes with the phosphorylated forms of PIF1 in response to light. The cop1 and spaQ seeds display strong hyposensitive response to far-red light-mediated seed germination and light-regulated gene expression. These data show a mechanism by which an E3 ligase attenuates its activity by degrading its cofactor in response to light.

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Biochemical Characterization ofArabidopsisComplexes Containing CONSTITUTIVELY PHOTOMORPHOGENIC1 and SUPPRESSOR OF PHYA Proteins in Light Control of Plant Development

Cited by 196 publications

References 57 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

Arabidopsis STO/BBX24 negatively regulates UV-B signaling by interacting with COP1 and repressing HY5 transcriptional activity

CUL4 forms an E3 ligase with COP1 and SPA to promote light-induced degradation of PIF1

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