Cryptochrome 2 (CRY2) is a critical component of the circadian clock
First-pass extracted concept
cryptochrome 2
Aliases
Arabidopsis cryptochrome 2, cry2, CRY2
Evidence Snippets
Optogenetic Control of Gene Expression Using Cryptochrome 2 and a Light-Activated Degron
Advances in optogenetic regulation of gene expression in mammalian cells using cryptochrome 2 (CRY2)
the clock gene, cryptochrome 2 (CRY2)
Glucose-Raising Polymorphisms in the Human Clock Gene Cryptochrome 2 (CRY2) Affect Hepatic Lipid Content
Cryptochrome 2 (CRY2) is a circadian clock protein involved in cell cycle
the light-sensitive cryptochrome 2 protein
blue light photoreceptor Cryptochrome 2 (CRY2)
The blue-light photoreceptors, cryptochrome (CRY) 2 and phototropin (PHOT) 2, are required for the stability of the R protein HRT
CIB1 is a well characterized transcriptional factor which promotes flowering through the physical interaction with the blue light receptor CRYPTOCHROME 2 (CRY2) in Arabidopsis.
Here, we report a study of the day-length-dependent response of cryptochrome 2 (cry2) and phytochrome A (phyA) and their role as day-length sensors in Arabidopsis.
The known photoreceptors for UV-A/blue light are cryptochrome (cry)1 and cry2
Cryptochrome 2 is a flavin-type blue light receptor
The function of Arabidopsis cryptochrome 2 in the early photomorphogenesis of seedlings was studied
the two blue-light photoreceptors, cryptochromes 1 and 2 (CRY1 and CRY2)
Supporting Sources
Linked Claims
CRY2 is essential in regulating skeletal muscle repair.
Therefore, CRY2 is essential in regulating skeletal muscle repair.
Loss of CRY2 increases the number of PAX7-positive cells associated with myotubes, suggesting increased reserve cell production.
Immunostaining revealed that the number of mononucleated paired box protein 7 (PAX7+) cells associated with myotubes formed by CRY2-/- cells was increased compared with CRY2+/+ cells, suggesting that more reserve cells were produced in the absence of CRY2.
CRY2-deficient myoblasts survive better in ischemic muscle.
CRY2 deficient myoblasts survived better in ischemic muscle.
Deletion of CRY2 enhances muscle regeneration.
Using the skeletal muscle lineage and satellite cell-specific CRY2 knockout mice (CRY2scko), we show that the deletion of CRY2 enhances muscle regeneration.
Deletion of CRY2 stimulates myoblast proliferation.
Single myofiber analysis revealed that deletion of CRY2 stimulates the proliferation of myoblasts.
Loss of CRY2 enhances myoblast differentiation, evidenced by increased MyHC expression and myotube formation.
The differentiation potential of myoblasts was enhanced by the loss of CRY2 evidenced by increased expression of myosin heavy chain (MyHC) and myotube formation in CRY2-/- cells versus CRY2+/+ cells.
Loss of CRY2 activates ERK1/2 signaling and ETS1, and ETS1 binds the PAX7 promoter to induce PAX7 transcription.
Loss of CRY2 leads to the activation of the ERK1/2 signaling pathway and ETS1, which binds to the promoter of PAX7 to induce its transcription.
Cryptochrome 2 and a light-activated degron are used for optogenetic control of gene expression.
Optogenetic Control of Gene Expression Using Cryptochrome 2 and a Light-Activated Degron
The paper concerns optogenetic regulation of gene expression in mammalian cells using cryptochrome 2 (CRY2).
CRY2 knockdown increases S phase cell population and reduces G1 phase cell population in HOS osteosarcoma cells.
CRY2 knockdown increased the S phase cell population and reduced the G1 phase cell population.
CRY2 knockdown increases mRNA expression of CRY1, PER1, PER2, BMAL1, and CLOCK in HOS osteosarcoma cells.
knockdown of CRY2 significantly increased the mRNA expression of CRY1, Period (PER) 1, PER2, BMAL1, and CLOCK.
CRY2 may function as an anti-oncogene in osteosarcoma.
Our results suggest that CRY2 may be an anti-oncogene in OS
CRY2 knockdown decreases P53 expression and increases c-myc and cyclin D1 expression in HOS osteosarcoma cells.
CRY2 knockdown decreased P53 expression and increased expression of c-myc and cyclin D1.
CRY2 suppresses proliferation and migration in HOS osteosarcoma cells.
CRY2 knockdown promoted HOS OS cell proliferation and migration.
CRY2 knockdown increases ERK1/2 phosphorylation but does not change JNK and P38 phosphorylation in HOS osteosarcoma cells.
CRY2 knockdown increased the phosphorylation of extracellular signal-regulated kinase (ERK) 1/2, but did not change the phosphorylation of c-Jun N terminal kinase (JNK) and P38.
CRY2 knockdown increases MMP-2 and β-catenin expression and promotes MAPK and Wnt/β-catenin signaling in HOS osteosarcoma cells.
CRY2 knockdown also increased the expression of matrix metalloproteinase (MMP)-2 and β-catenin, and increased OS cell proliferation and migration by inducing cell cycle progression and promoting mitogen-activated protein kinase (MAPK) and Wnt/β-catenin signaling pathways.
CRY2 mRNA expression in human liver tissue samples was directly associated with hepatic triglyceride content.
In human liver tissue samples, CRY2 mRNA expression was directly associated with hepatic triglyceride content.
CRY2 may act as a switch in hepatic fuel metabolism that promotes triglyceride storage and limits glucose production.
Our data may point to CRY2 as a novel switch in hepatic fuel metabolism promoting triglyceride storage and, concomitantly, limiting glucose production.
Four CRY2 SNPs were associated with fasting glycaemia in non-diabetic individuals.
Four CRY2 SNPs were associated with fasting glycaemia, as reported earlier.
Minor alleles of the CRY2 SNPs associated with fasting glycaemia were associated with elevated fasting glycaemia and reduced liver fat content.
Importantly, carriers of these SNPs' minor alleles revealed elevated fasting glycaemia and, concomitantly, reduced liver fat content.
The tested clock gene SNPs were not associated with body fat content, insulin sensitivity, or insulin secretion.
None of the tested SNPs was associated with body fat content, insulin sensitivity, or insulin secretion.
FBXW7 binds directly to phosphorylated Thr300 of CRY2.
FBXW7 binds directly to phosphorylated Thr300 of CRY2
Upregulation of CRY2 caused by downregulation of FBXW7 may be a novel prognostic biomarker and therapeutic target in colorectal cancer.
Taken together, our findings indicate that the upregulation of CRY2 caused by downregulation of FBXW7 may be a novel prognostic biomarker and may represent a new therapeutic target in colorectal cancer.
High FBXW7 expression downregulates CRY2 and increases colorectal cancer cell sensitivity to chemotherapy.
High FBXW7 expression downregulates CRY2 and increases colorectal cancer cells' sensitivity to chemotherapy.
Knockdown of CRY2 increases colorectal cancer cell sensitivity to oxaliplatin.
Knockdown of CRY2 increased colorectal cancer sensitivity to oxaliplatin in colorectal cancer cells.
CRY2 is overexpressed in chemoresistant colorectal cancer samples.
Here, we report that CRY2 is overexpressed in chemoresistant colorectal cancer samples
Low FBXW7 expression is correlated with high CRY2 expression in colorectal cancer patient samples.
Low FBXW7 expression is correlated with high CRY2 expression in colorectal cancer patient samples.
FBXW7 is a novel E3 ubiquitin ligase that targets CRY2 for proteasomal degradation.
We also identify FBXW7 as a novel E3 ubiquitin ligase for targeting CRY2 through proteasomal degradation.
FBXW7 expression promotes CRY2 degradation by enhancing CRY2 ubiquitination and accelerating CRY2 turnover.
FBXW7 expression leads to degradation of CRY2 through enhancing CRY2 ubiquitination and accelerating the CRY2's turnover rate.
CRY2 overexpression is correlated with poor patient survival in colorectal cancer.
CRY2 overexpression is correlated with poor patient survival
The paper describes development of LITEs, an optogenetic two-hybrid system integrating a TALE DNA-binding domain with cryptochrome 2 and CIB1.
Here we describe the development of light-inducible transcriptional effectors (LITEs), an optogenetic two-hybrid system integrating the customizable TALE DNA-binding domain with the light-sensitive cryptochrome 2 protein and its interacting partner CIB1 from Arabidopsis thaliana.
The blue light-induced transcription system used in this study is based on the blue light-dependent interaction between CRY2 and CIB1.
Here we exploited the blue light-induced transcription system in yeast and zebrafish, based on the blue light dependent interaction between two plant proteins, blue light photoreceptor Cryptochrome 2 (CRY2) and the bHLH transcription factor CIB1 (CRY-interacting bHLH 1).
Exposure to darkness or blue light induces degradation of CRY2 and subsequently HRT, resulting in susceptibility.
Exposure to darkness or blue-light induces degradation of CRY2, and in turn HRT, resulting in susceptibility.
CRY2 and PHOT2 are required for HRT stability and thereby resistance to Turnip Crinkle virus.
The blue-light photoreceptors, cryptochrome (CRY) 2 and phototropin (PHOT) 2, are required for the stability of the R protein HRT, and thereby resistance to Turnip Crinkle virus (TCV).
HRT overexpression compensates for absence of PHOT2 but not absence of CRY2.
Overexpression of HRT can compensate for the absence of PHOT2 but not CRY2.
CRY2 and PHOT2 negatively regulate proteasome-mediated degradation of HRT, likely via COP1, and blue light relieves this repression resulting in HRT degradation.
We propose that CRY2/PHOT2 negatively regulate the proteasome-mediated degradation of HRT, likely via COP1, and blue-light relieves this repression resulting in HRT degradation.
HRT does not directly associate with CRY2 or PHOT2 but does bind COP1.
HRT does not directly associate with either CRY2 or PHOT2 but does bind the CRY2-/PHOT2-interacting E3 ubiquitin ligase, COP1.
phyA mediates far-red light promotion of flowering with modes of action similar to cry2.
we show that phyA mediates far-red light promotion of flowering with modes of action similar to that of cry2.
The short-day-specific diurnal rhythm of cry2 is determined primarily by blue light-dependent cry2 turnover.
The short-day-specific diurnal rhythm of cry2 is determined primarily by blue light-dependent cry2 turnover.
Individual phytochromes and cryptochromes work together to confer photoperiodic responsiveness in Arabidopsis, and this responsiveness depends on light quality.
Based on these results and a finding that the photoperiodic responsiveness of plants depends on light quality, a model is proposed to explain how individual phytochromes and cryptochromes work together to confer photoperiodic responsiveness in Arabidopsis.
cry2 and phyA protein abundance show a diurnal rhythm in plants grown in short-day but not in plants grown in long-day.
The protein abundance of cry2 and phyA showed a diurnal rhythm in plants grown in short-day but not in plants grown in long-day.
cryptochrome 2 and phytochrome A act as day-length sensors in Arabidopsis.
Here, we report a study of the day-length-dependent response of cryptochrome 2 (cry2) and phytochrome A (phyA) and their role as day-length sensors in Arabidopsis.
The C-terminal domain of CRY2 containing a basic bipartite nuclear localization signal is sufficient to confer nuclear localization of the fusion protein.
The C-terminal domain of cry2 that contains the basic bipartite nuclear localization signal was sufficient to confer nuclear localization of the fusion protein.
CRY2 is a nuclear protein.
These results strongly suggest that cry2 is a nuclear protein.
In contrast to CRY1, CRY2 functions primarily under low light during early seedling development.
In contrast to CRY1 ... cryptochrome 2 functions primarily under low light during the early development of seedlings.
CRY1 and CRY2 are specifically expressed in the ganglion cell and inner nuclear layers of the mouse retina.
We have found that the two blue-light photoreceptors, cryptochromes 1 and 2 (CRY1 and CRY2), recently discovered in mammals are specifically expressed in the ganglion cell and inner nuclear layers of the mouse retina.
Cryptochrome 2 mediates blue light-dependent inhibition of hypocotyl elongation in Arabidopsis seedlings under low blue light intensities.
It is found that cryptochrome 2 mediates blue light-dependent inhibition of hypocotyl elongation ... under low intensities of blue light.
Cryptochrome 2 mediates blue light-dependent stimulation of cotyledon opening in Arabidopsis seedlings under low blue light intensities.
It is found that cryptochrome 2 mediates ... stimulation of cotyledon opening under low intensities of blue light.
CRY2 expression is rapidly down-regulated by blue light in a light-intensity dependent manner.
the expression of CRY2 is rapidly down-regulated by blue light in a light-intensity dependent manner