<i>Arabidopsis</i> COP10 forms a complex with DDB1 and DET1 in vivo and enhances the activity of ubiquitin conjugating enzymes

Yanagawa, Yuki; Sullivan, Jerome L.; Komatsu, Setsuko; Gusmaroli, Giuliana; Suzuki, Genki; Yin, Jingjing; Ishibashi, Toyotaka; Saijo, Yusuke; Rubio, Vicente; Kimura, Seisuke; Wang, Jian; Deng, Xing Wang

doi:10.1101/gad.1229504

Cited by 189 publications

(263 citation statements)

References 42 publications

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“…COP1 was shown to be modulated by light-activated photoreceptors, the COP9 signalosome, and the CDD complex (Saijo et al, 2003;Yanagawa et al, 2004;Chen et al, 2006;Yang and Wang, 2006). In this study, we showed that not only SPA1 but all four SPA Protein gel blot analysis showing the effects of cop1-6, cop9-1, cop10-1, and det1-1 mutations on the accumulation of COP1 and SPA proteins.…”

Section: Spa Proteins Are Critical For the Activity Of Cop1 In Vivomentioning

confidence: 68%

“…Biochemically, these COP/DET/FUS proteins belong to three groups of protein complexes: the COP1 complex(es), the COP9 signalosome (CSN), and the CDD complex (COP10, DDB1, and DET1). It has been hypothesized that all three complexes function collectively in the ubiquitination/proteasomemediated degradation of key photomorphogenesis-promoting transcription factors, thus achieving their repression of photomorphogenesis (Yanagawa et al, 2004;Chen et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2008

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COP1 (for CONSTITUTIVELY PHOTOMORPHOGENIC1) and the four partially redundant SPA (for SUPPRESSOR OF PHYA) proteins work in concert to repress photomorphogenesis in Arabidopsis thaliana by targeting key transcription factors and phytochrome A for degradation via the 26S proteasome. Here, we report a detailed biochemical characterization of the SPA-COP1 complexes. The four endogenous SPA proteins can form stable complexes with COP1 in vivo regardless of light conditions but exhibit distinct expression profiles in different tissues and light conditions. The SPA proteins can self-associate or interact with each other, forming a heterogeneous group of SPA-COP1 complexes in which the exact SPA protein compositions vary depending on the abundance of individual SPA proteins. The four SPA proteins could be divided into two functional groups depending on their interaction affinities, their regulation of ELONGATED HYPOCOTYL5 degradation, and their opposite effects on COP1 protein accumulation. Loss-of-function mutations in a predominant SPA protein may cause a significant reduction in the overall SPA-COP1 E3 ligase activity, resulting in a partial constitutive photomorphogenic phenotype. This study thus provides an in-depth biochemical view of the SPA-COP1 E3 ligase complexes and offers new insights into the molecular basis for their distinct roles in the light control of plant development.

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Section: Spa Proteins Are Critical For the Activity Of Cop1 In Vivomentioning

confidence: 68%

Section: Introductionmentioning

confidence: 99%

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

et al. 2008

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“…In Arabidopsis, the E3 ubiquitin ligase activity of the COP1 complex was recently proposed to be supported by direct interaction with the COP9 signalosome and the CDD (for COP10, DDB1, DET1) complexes (Yanagawa et al, 2004). These three complexes are defined by the COP/DET/FUS group of genes that share the cop phenotypes when mutated (e.g., Hoecker, 2005;.…”

Section: Introductionmentioning

confidence: 99%

CONSTITUTIVELY PHOTOMORPHOGENIC1 Is Required for the UV-B Response in Arabidopsis

et al. 2006

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CONSTITUTIVELY PHOTOMORPHOGENIC1 (COP1) is a negative regulator of photomorphogenesis in Arabidopsis thaliana. COP1 functions as an E3 ubiquitin ligase, targeting select proteins for proteasomal degradation in plants as well as in mammals. Among its substrates is the basic domain/leucine zipper (bZIP) transcription factor ELONGATED HYPOCOTYL5 (HY5), one of the key regulators of photomorphogenesis under all light qualities, including UV-B responses required for tolerance to this environmental threat. Here, we report that, in contrast with the situation in visible light, COP1 is a critical positive regulator of responses to low levels of UV-B. We show that in the cop1-4 mutant, flavonoid accumulation and genome-wide expression changes in response to UV-B are blocked to a large extent. COP1 is required for HY5 gene activation, and both COP1 and HY5 proteins accumulate in the nucleus under supplementary UV-B. SUPPRESSOR OF PHYTOCHROME A-105 family proteins (SPA1 to SPA4) that are required for COP1 function in dark and visible light are not essential in the response to UV-B. We conclude that COP1 performs a specific and novel role in the plants' photomorphogenic response to UV-B, coordinating HY5-dependent and -independent pathways, which eventually results in UV-B tolerance.

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“…Besides SCF TIR1/AFB1-3 , CUL1-type E3s have been implicated in the degradation of DELLA regulators in response to the phytohormone GA [SCF SLEEPY(SLY1) ; Dill et al, 2004] and the cell cycle inhibitor KIP1-RELATED PROTEIN1 (KRP1; [SCF SKP2b ]; Ren et al, 2008). The best-characterized CUL4 CRL from Arabidopsis acts together with DDB1, CONSTITUTIVELY PHOTOMORPHOGENIC1, DEETIOLATED1, and SUPRESSOR-OF-phyA-1051 to promote the degradation of the transcription factor ELONGATED HYPOCOT-YL5 (HY5) that normally represses hypocotyl elongation in light-grown Arabidopsis seedlings (Osterlund et al, 2000;Yanagawa et al, 2004;Chen et al, 2006Chen et al, , 2010.…”

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confidence: 99%

MLN4924 Is an Efficient Inhibitor of NEDD8 Conjugation in Plants

et al. 2011

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The conjugation of the ubiquitin-like modifier NEURAL PRECURSOR CELL-EXPRESSED DEVELOPMENTALLY DOWN-REGULATED PROTEIN8/RELATED TO UBIQUITIN1 (NEDD8/RUB1; neddylation) is best known as an important posttranslational modification of the cullin subunits of cullin-RING-type E3 ubiquitin ligases (CRLs). MLN4924 has recently been described as an inhibitor of NEDD8-ACTIVATING ENZYME1 (NAE1) in human. Here, we show that MLN4924 is also an effective and specific inhibitor of NAE1 enzymes from Arabidopsis (Arabidopsis thaliana) and other plant species. We found that MLN4924-treated wild-type seedlings have phenotypes that are highly similar to phenotypes of mutants with a partial defect in neddylation and that such neddylation-defective mutants are hypersensitive to MLN4924 treatment. We further found that MLN4924 efficiently blocks the neddylation of cullins in Arabidopsis and that MLN4924 thereby interferes with the degradation of CRL substrates and their downstream responses. MLN4924 treatments also induce characteristic phenotypes in tomato (Solanum lycopersicum), Cardamine hirsuta, and Brachypodium distachyon. Interestingly, MLN4924 also blocks the neddylation of a number of other NEDD8-modified proteins. In summary, we show that MLN4924 is a versatile and specific neddylation inhibitor that will be a useful tool to examine the role of NEDD8-and CRL-dependent processes in a wide range of plant species.

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Arabidopsis COP10 forms a complex with DDB1 and DET1 in vivo and enhances the activity of ubiquitin conjugating enzymes

Cited by 189 publications

References 42 publications

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

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

CONSTITUTIVELY PHOTOMORPHOGENIC1 Is Required for the UV-B Response in Arabidopsis

MLN4924 Is an Efficient Inhibitor of NEDD8 Conjugation in Plants

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