The Blue Light-Dependent Phosphorylation of the CCE Domain Determines the Photosensitivity of Arabidopsis CRY2

Qin, Qin; Wang, Hong; William, .; Barshop,; Mingdi,; Bian,; Ajay, Ajay; Vashisht,; Reqing,; He, Jian; Xu-hong,; A, Yu; Liu, Ming; Paula, José Ricardo; Nguyen, Nguyen; Xuanming,; Xiaoying,; Zhao, Lei

doi:10.1016/j.molp.2016.12.009

Cited by 17 publications

(30 citation statements)

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“…The lack of involvement of ZTL-type blue light receptors in the blue light regulation of CRY2 degradation is interesting because ZTL is a known CUL1-based E3 ubiquitin ligase that regulates ubiquitination and degradation of not only clock proteins but also the CRY2-interacting protein CIBs (Liu et al 2013). This result, together with our finding that none of the genes closely associated with the function of the circadian clock, photobody formation or flowering time control is required for the blue lightdependent CRY2 degradation, supports the notion that CRY2 acts as the photoreceptor to mediate blue light regulation of its own ubiquitination and degradation (Yu et al 2007a, Wang et al 2015.…”

Section: Discussionsupporting

confidence: 84%

“…6D). Given that the stability of CRY2 is determined by the blue light-dependent ubiquitination and 26S-dependent proteolysis (Shalitin et al 2002, Yu et al 2007b, Yu et al 2009, Li et al 2011, Wang et al 2015, these results argue that a CUL1-based E3 ubiquitin ligase is probably also involved in the ubiquitination and degradation of CRY2 in response to blue light. We next compared the relative level of the CRY2 protein in the axr6-3 seedlings grown under continuous blue light (10 mmol m -2 s -1 ) (Fig.…”

Section: A Cul1-based E3 Ligase Is Involved In the Blue Light-dependementioning

confidence: 83%

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The Blue Light-Dependent Polyubiquitination and Degradation of Arabidopsis Cryptochrome2 Requires Multiple E3 Ubiquitin Ligases

et al. 2016

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Cryptochromes are blue light receptors regulated by lightdependent ubiquitination and degradation in both plant and animal lineages. The Arabidopsis genome encodes two cryptochromes, CRY1 and CRY2, of which CRY2 undergoes blue light-dependent ubiquitination and 26S proteasomedependent degradation. The molecular mechanism regulating blue light-dependent proteolysis of CRY2 is still not fully understood. We found that the F-box proteins ZEITLUPE (ZTL) and Lov Kelch Protein2 (LKP2), which mediate blue light suppression of degradation of the CRY2 signaling partner CIB1, are not required for the blue light-dependent CRY2 degradation. We further showed that the previously reported function of the COP1-SPA1 protein complex in blue light-dependent CRY2 degradation is more likely to be attributable to its cullin 4 (CUL4)-based E3 ubiquitin ligase activity than its activity as the cryptochrome signaling partner. However, the blue light-dependent CRY2 degradation is only partially impaired in the cul4 mutant, the cop1-5 null mutant and the spa1234 quadruple mutant, suggesting a possible involvement of additional E3 ubiquitin ligases in the regulation of CRY2. Consistent with this hypothesis, we demonstrated that the blue light-dependent CRY2 degradation is significantly impaired in the temperature-sensitive cul1 mutant allele (axr6-3), especially under the nonpermissive temperature. Based on these and other results presented, we propose that photoexcited CRY2 undergoes Lys48-linked polyubiquitination catalyzed by the CUL4-and CUL1-based E3 ubiquitin ligases.

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Section: Discussionsupporting

confidence: 84%

Section: A Cul1-based E3 Ligase Is Involved In the Blue Light-dependementioning

confidence: 83%

The Blue Light-Dependent Polyubiquitination and Degradation of Arabidopsis Cryptochrome2 Requires Multiple E3 Ubiquitin Ligases

et al. 2016

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“…In this structure, the adenine ring is sandwiched between Tyr-402 and Leu-296 within the activesite cleft, which is the DNA lesion-binding site in photolyases, the phosphates are exposed to the solvent, and hydrogen bonds are formed between ␤-phosphate and Arg-360 (37). Atcry1 and other crytochromes have autophosphorylation activity in vitro (34,36,38), but this activity does not explain the complete phosphorylation pattern of cry1 and cry2 (35).…”

Section: Plant Cryptochromes (Cry) Act As Uv-a/blue Light Receptorsmentioning

confidence: 98%

“…There is compelling evidence that plant cryptochromes are phosphorylated upon photoexcitation, in particular in the CCE (32), and that this phosphorylation is required for the biological activity of these photoreceptors (32)(33)(34)(35). Atcry1 (36,37) and other cryptochromes (38) bind ATP, even though Atcry1 lacks a canonical nucleotide-binding site, as revealed by the co-crystal structure of the Atcry1 PHR domain (Atcry1PHR) with the ATP analog AMP-PNP.…”

Section: Plant Cryptochromes (Cry) Act As Uv-a/blue Light Receptorsmentioning

confidence: 99%

Hyperactivity of the Arabidopsis cryptochrome (cry1) L407F mutant is caused by a structural alteration close to the cry1 ATP-binding site

Orth

Niemann

Hennig

et al. 2017

Journal of Biological Chemistry

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Plant cryptochromes (cry) act as UV-A/blue light receptors. The prototype, cry1, regulates several light responses during the life cycle, including de-etiolation, and is also involved in regulating flowering time. The cry1 photocycle is initiated by light absorption by its FAD chromophore, which is most likely fully oxidized (FAD) in the dark state and photoreduced to the neutral flavin semiquinone (FADH°) in its lit state. Cryptochromes lack the DNA-repair activity of the closely related DNA photolyases, but they retain the ability to bind nucleotides such as ATP. The previously characterized L407F mutant allele of cry1 is biologically hyperactive and seems to mimic the ATP-bound state of cry1, but the reason for this phenotypic change is unclear. Here, we show thatL407F can still bind ATP, has less pronounced photoreduction and formation of FADH° than wild-type cry1, and has a dark reversion rate 1.7 times lower than that of the wild type. The hyperactivity of L407F is not related to a higher FADH° occupancy of the photoreceptor but is caused by a structural alteration close to the ATP-binding site. Moreover, we show that ATP binds to cry1 in both the dark and the lit states. This binding was not affected by cry1's C-terminal extension, which is important for signal transduction. Finally, we show that a recently discovered chemical inhibitor of cry1, 3-bromo-7-nitroindazole, competes for ATP binding and thereby diminishes FADH° formation, which demonstrates that both processes are important for cry1 function.

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“…For CRY biochemistry, blue light stimulates both CRY1 and CRY2 phosphorylation (Shalitin et al, 2002(Shalitin et al, , 2003. The phosphorylation status of CRY2 further determines CRY2 degradation in the nucleus (Yu et al, 2007;Wang et al, 2015a). In searching for the kinase(s) responsive to CRY2 phosphorylation, mass spectrometry analysis was performed to detect the CRY2-interacting proteins by purifying GFP-CRY2 recombinant proteins.…”

Section: Crys Repress Thermomorphogenesismentioning

confidence: 99%

Dark, Light, and Temperature: Key Players in Plant Morphogenesis

Jin

Zhu

2019

Plant Physiol.

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The Blue Light-Dependent Phosphorylation of the CCE Domain Determines the Photosensitivity of Arabidopsis CRY2

Cited by 17 publications

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The Blue Light-Dependent Polyubiquitination and Degradation of Arabidopsis Cryptochrome2 Requires Multiple E3 Ubiquitin Ligases

The Blue Light-Dependent Polyubiquitination and Degradation of Arabidopsis Cryptochrome2 Requires Multiple E3 Ubiquitin Ligases

Hyperactivity of the Arabidopsis cryptochrome (cry1) L407F mutant is caused by a structural alteration close to the cry1 ATP-binding site

Dark, Light, and Temperature: Key Players in Plant Morphogenesis

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