Biochemical evidence for ubiquitin ligase activity of the <i>Arabidopsis</i> COP1 interacting protein 8 (CIP8)

Hardtke, Christian S.; Okamoto, Haruko; Stoop, Chatanika; Deng, Xing Wang

doi:10.1046/j.1365-313x.2002.01298.x

Cited by 100 publications

(79 citation statements)

References 38 publications

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“…These proteins have a similar RING-H2 domain and the GLD motif found in ATLs, but lack the hydrophobic N-terminus, having instead a BZF motif, a C2 zinc finger (Guzmán, 2012). Several BTL proteins have been described previously; they are CIP8 (CONSTITUTIVE PHOTOMORPHOGENIC [COP] INTER-ACTING PROTEIN 8, At5g64920, BTL12, (Hardtke et al, 2002)), RDUF1 (RING DOMAIN OF UNKNOWN FUNCTION 1117, At3g46620, BTL10, (Kim et al, 2012)), RDUF2 (At5g59550, BTL9, (Kim et al, 2012)) and RZF1 (RING ZINC FINGER 1, At3g56580) (Ju et al, 2013). While the ATLs appear to be plantspecific, relatives of the BTLs are found in animals and fungi (Aguilar-Hernández et al, 2013).…”

Section: The Atl and Btl Ring E3smentioning

confidence: 99%

“…The BZF region of one BTL, BTL4 (At5g56340), interacts with ubiquitin in a Y2H assay, while the region in between the BZF and the RING-H2 motif interacts with a number of potential substrates (Aguilar-Hernández et al, 2013). CIP8 interacts with COP1, and ubiquitinates HY5 linking it to light signaling (Hardtke et al, 2002). In contrast, RDUF1 and RDUF2 function in drought response pathways (Kim et al, 2012) and RZF1 mRNA is drought inducible (Ju et al, 2013).…”

Section: The Atl and Btl Ring E3smentioning

confidence: 99%

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The Ubiquitination Machinery of the Ubiquitin System

Callis

2014

The Arabidopsis Book

293

269

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The protein ubiquitin is a covalent modifier of proteins, including itself. The ubiquitin system encompasses the enzymes required for catalysing attachment of ubiquitin to substrates as well as proteins that bind to ubiquitinated proteins leading them to their final fate. Also included are activities that remove ubiquitin independent of, or in concert with, proteolysis of the substrate, either by the proteasome or proteases in the vacuole. In addition to ubiquitin encoded by a family of fusion proteins, there are proteins with ubiquitin-like domains, likely forming ubiquitin's β-grasp fold, but incapable of covalent modification. However, they serve as protein-protein interaction platforms within the ubiquitin system. Multi-gene families encode all of these types of activities. Within the ubiquitination machinery "half" of the ubiquitin system are redundant, partially redundant, and unique components affecting diverse developmental and environmental responses in plants. Notably, multiple aspects of biotic and abiotic stress responses require, or are modulated by, ubiquitination. Finally, aspects of the ubiquitin system have broad utility: as components to enhance gene expression or to regulate protein abundance. This review focuses on the ubiquitination machinery: ubiquitin, unique aspects about the synthesis of ubiquitin and organization of its gene family, ubiquitin activating enzymes (E1), ubiquitin conjugating enzymes (E2) and ubiquitin ligases, or E3s. Given the large number of E3s in Arabidopsis this review covers the U box, HECT and RING type E3s, with the exception of the cullin-based E3s.

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Section: The Atl and Btl Ring E3smentioning

confidence: 99%

Section: The Atl and Btl Ring E3smentioning

confidence: 99%

The Ubiquitination Machinery of the Ubiquitin System

Callis

2014

The Arabidopsis Book

293

269

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“…The other five proteins could be more directly involved in the control of flowering date. CIP8 is a protein that binds to COP1 (Torii et al, 1999) similar to SPA proteins, and possess ubiquitin ligase activity (Hardtke et al, 2002). PhyA is a light-labile cytoplasmic red/far-red light photoreceptor involved in the regulation of photomorphogenesis.…”

Section: (Supplementarymentioning

confidence: 99%

Comparison of the genetic determinism of two key phenological traits, flowering and maturity dates, in three Prunus species: peach, apricot and sweet cherry

et al. 2012

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The present study investigates the genetic determinism of flowering and maturity dates, two traits highly affected by global climate change. Flowering and maturity dates were evaluated on five progenies from three Prunus species, peach, apricot and sweet cherry, during 3-8 years. Quantitative trait locus (QTL) detection was performed separately for each year and also by integrating data from all years together. High heritability estimates were obtained for flowering and maturity dates. Several QTLs for flowering and maturity dates were highly stable, detected each year of evaluation, suggesting that they were not affected by climatic variations. For flowering date, major QTLs were detected on linkage groups (LG) 4 for apricot and sweet cherry and on LG6 for peach. QTLs were identified on LG2, LG3, LG4 and LG7 for the three species. For maturity date, a major QTL was detected on LG4 in the three species. Using the peach genome sequence data, candidate genes underlying the major QTLs on LG4 and LG6 were investigated and key genes were identified. Our results provide a basis for the identification of genes involved in flowering and maturity dates that could be used to develop cultivar ideotypes adapted to future climatic conditions. Heredity (2012) 109, 280-292; doi:10.1038/hdy.2012.38; published online 25 July 2012Keywords: Prunus; phenology; flowering date; maturity date; QTL analyses; candidate gene INTRODUCTIONIn the context of global climate change, flowering phenology of deciduous tree species is crucial as it may affect their productivity. In fruit tree orchards, flowering phenology has an indirect influence on spring frost damage, pollination, dormancy and maturity. Even though in a warming scenario, the current risk of frost damage might remain a preoccupation for growers subsequently to advanced flowering time and more irregularities of temperature conditions. Moreover, new risks are emerging as disruptions in floral phenology synchronization, which may disturb pollination for varieties that necessitate cross pollination. In addition, marked changes in the order of flowering time within a varietal range or between adjacent cropping areas may modify the orders of fruit maturity time and consequently disturb commercial specificities.The Prunus genus, within the Rosaceae family, is characterized by species that produce drupes as fruit, and can be divided into three major subgenera: Amygdalus (peach (Prunus persica (L.) Batsch) and almond (Prunus dulcis Mill.)), Prunophora (apricot (Prunus armeniaca L.)), Cerasus (sweet cherry (Prunus avium L.) and sour cherry (Prunus cerasus L.)). All these species are grown in climates with well-differentiated seasons where they have adapted to survive to low winter temperatures and summer drought. In Prunus, as in most woody perennials, the physiology and biochemistry of the flowering

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“…Protein extraction, protein gel blot, and gel filtration analyses were performed as described previously (Hardtke et al, 2002) with a modified lysis buffer: 50 mM Tris (pH 7.5), 150 mM NaCl, 1 mM EDTA, 10 mM NaF, 25 mM b-glycerophosphate, 2 mM Na 3 VO 4 , 10 mM NaF, 10% glycerol, 0.1% Tween 20, 1 mM DTT, 1 mM phenylmethylsulfonyl fluoride, and 13 complete protease inhibitor cocktail (Roche).…”

Section: Protein Extraction Immunoblot Analysis and Gel Filtration mentioning

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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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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Biochemical evidence for ubiquitin ligase activity of the Arabidopsis COP1 interacting protein 8 (CIP8)

Cited by 100 publications

References 38 publications

The Ubiquitination Machinery of the Ubiquitin System

The Ubiquitination Machinery of the Ubiquitin System

Comparison of the genetic determinism of two key phenological traits, flowering and maturity dates, in three Prunus species: peach, apricot and sweet cherry

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

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