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CRY2-CIB1 (show CIB1 Proteins) and CRY2-CRY2 interactions are governed by well-separated protein interfaces at the two termini of CRY2.
Exposure to blue light is required for an in vivo-association of CRY1 (show CRY1 Proteins) and CRY2 with COP1.
Data show that the effect of 3-bromo-7-nitroindazole (3B7N) treatment on gene expression in cryptochromes cry1cry2 is considerably smaller than that in the wild type, indicating that 3B7N specifically interrupts cryptochrome function in the control of seedling development in a light-dependent manner.
It describes minimal functional CRY2 and CIB1 (show CIB1 Proteins) domains maintaining light-dependent interaction and new signaling mutations affecting Arabidopsis thaliana cryptochrome 2 (AtCRY2) photocycle kinetics.
this study identified BIC1 (blue-light inhibitor of cryptochromes 1) as an inhibitor of plant cryptochromes that binds to CRY2 to suppress the blue light-dependent dimerization, photobody formation, phosphorylation, degradation, and physiological activities of CRY2.
the blue light-dependent CRY2 degradation is significantly impaired in the temperature-sensitive cul1 (show CUL1 Proteins) mutant allele (axr6 (show CUL1 Proteins)-3), especially under the non-permissive temperature.
For growth under a canopy, where blue light is diminished, CRY1 and CRY2 perceive this change and respond by directly contacting two bHLH transcription factors, PIF4 and PIF5.
Arabidopsis thaliana cry2 proteins containing Trp (show TBPL1 Proteins) triad mutations indeed undergo robust photoreduction in living cultured insect cells.
data showed that mutations in the serine residues within and outside the serine cluster diminished blue light-dependent CRY2 phosphorylation, degradation, and physiological activities.
Our study demonstrates that CIBs function redundantly in regulating CRY2-dependent flowering, and that different CIBs form heterodimers to interact with the non-canonical E-box DNA in vivo.
In the longitudinal analysis, CRY2 SNP rs61884508 was protective from worsening of problematicity of seasonal variations of mood disorder. In the cross-sectional analysis, CRY2 SNP rs72902437 showed evidence of association with problematicity of seasonal variations, as did SNP rs1554338 (in the MAPK8IP1 (show MAPK8IP1 Proteins) and downstream of CRY2).
The earlier reported association of CRY2 variants with dysthymia was confirmed and extended to major depressive disorder.
These results demonstrate that CRY2 stability controlled by FBXL3 (show FBXL3 Proteins) plays a key role in the regulation of human sleep wake behavior.
The FOXM1 (show FOXM1 Proteins) is a negative regulator of CRY2 in breast cancer via enhancing methylation in CRY2 promoter and its high expression is an independent predictor of favorable MR-free survival in ER+ breast cancer patients.
CRY2 and FBXL3 (show FBXL3 Proteins) cooperatively degrade c-MYC (show MYC Proteins) preventing the development of cancer.
The present study identified USP7 (show USP7 Proteins) and TDP-43 (show TARDBP Proteins) as the regulators of CRY1 (show CRY1 Proteins) and CRY2, underscoring the significance of the stability control process of CRY proteins for period determination in the mammalian circadian clockwork.
For the first time, we show that Cry 2 rs2292910 and MTNR1B rs3781638 are associated with osteoporosis in a Chinese geriatric cohort.
Altered CRY1 (show CRY1 Proteins) and CRY2 expression patterns and the interplay with the genetic landscape in colon cancer cells may underlie phenotypic divergence.
Given the distinct characteristics of the C-terminal tails of the CRY1 (show CRY1 Proteins) and CRY2 proteins, our study addresses a long-standing hypothesis that the ratio of these two CRY molecules affects the clock period.
data may point to CRY2 as a novel switch in hepatic fuel metabolism promoting triglyceride storage and, concomitantly, limiting glucose production
In vivo knockdown of Rfk (show RFK Proteins), Riboflavin (vitamin B2) kinase essential for FAD synthesis, altered the expression rhythms of CRY1 (show CRY1 Proteins), CRY2, and PER1 (show PER1 Proteins)
Data show that cryptochrome Cry1 (show CRY1 Proteins) and Cry2 expression must be circadian and appropriately phased to support rhythms, and arginine vasopressin (AVP (show AVP Proteins)) receptor signaling is required to impose circuit-level circadian function.
Data suggest that cryptochromes (Cry1 (show CRY1 Proteins) and Cry2) mediate periodic binding of Ck2b (show CSNK2B Proteins) (casein kinase 2beta) to Bmal1 (aryl hydrocarbon receptor nuclear translocator-like (show ARNTL Proteins) protein) and thus inhibit Bmal1 (show ARNTL Proteins)-Ser90 phosphorylation by Ck2a (show CSNK2A1 Proteins) (casein kinase 2alpha).
Cry2 exerts a critical role in the control of depression-related emotional states and modulates the chronobiological gene expression profile in the mouse amygdala.
Cry1/Cry2-deficient mice had significantly lower N6- methyladenosine methylation of RNA and lost the circadian rhythm of N6-methyladenosine levels in RNA.
Data show that the intermolecular zinc finger is important for period circadian protein (PER2 (show PER2 Proteins))-cryptochrome 2 (CRY2) complex formation.
Report compression of daily activity time in Cry2 mutant mice.
Data show that Ser557 phosphorylation of CRY2 promotes CRY2 degradation and inhibits the overaccumulation of the CRY2-PER2 (show PER2 Proteins) complex in the nucleus.
member of a family of blue-light photoreceptors\; may regulate circadian rhythm
, cryptochrome 2
, cryptochrome Cry2
, cryptochrome 2 (photolyase-like)
, growth-inhibiting protein 37