First-pass extracted concept

cryptochrome 2

Candidate: toolkit itemType: protein domain15 source documents49 linked claims
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Aliases

Arabidopsis cryptochrome 2, cry2, CRY2

Evidence Snippets

Cryptochrome 2 (CRY2) is a critical component of the circadian clock
Evidence 1Source 1DOIPubMedprovenance
Optogenetic Control of Gene Expression Using Cryptochrome 2 and a Light-Activated Degron
Evidence 2Source 2DOIPubMedprovenance
Advances in optogenetic regulation of gene expression in mammalian cells using cryptochrome 2 (CRY2)
Evidence 3Source 3DOIprovenance
the clock gene, cryptochrome 2 (CRY2)
Evidence 4Source 4DOIPubMedprovenance
Glucose-Raising Polymorphisms in the Human Clock Gene Cryptochrome 2 (CRY2) Affect Hepatic Lipid Content
Evidence 5Source 5DOIPubMedprovenance
Cryptochrome 2 (CRY2) is a circadian clock protein involved in cell cycle
Evidence 6Source 6DOIPubMedprovenance
the light-sensitive cryptochrome 2 protein
Evidence 7Source 7DOIPubMedprovenance
blue light photoreceptor Cryptochrome 2 (CRY2)
Evidence 8Source 8DOIPubMedprovenance
The blue-light photoreceptors, cryptochrome (CRY) 2 and phototropin (PHOT) 2, are required for the stability of the R protein HRT
Evidence 9Source 9DOIPubMedprovenance
CIB1 is a well characterized transcriptional factor which promotes flowering through the physical interaction with the blue light receptor CRYPTOCHROME 2 (CRY2) in Arabidopsis.
Evidence 10Source 10DOIprovenance
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.
Evidence 11Source 11DOIPubMedprovenance
The known photoreceptors for UV-A/blue light are cryptochrome (cry)1 and cry2
Evidence 12Source 12DOIPubMedprovenance
Cryptochrome 2 is a flavin-type blue light receptor
Evidence 13Source 13DOIPubMedprovenance
The function of Arabidopsis cryptochrome 2 in the early photomorphogenesis of seedlings was studied
Evidence 14Source 14DOIPubMedprovenance
the two blue-light photoreceptors, cryptochromes 1 and 2 (CRY1 and CRY2)
Evidence 15Source 15DOIPubMedprovenance

Supporting Sources

Source 15primary paper1998Proceedings of the National Academy of SciencesDOIPubMed

Linked Claims

Claim 1biological rolesupports2023Source 1DOIPubMed

CRY2 is essential in regulating skeletal muscle repair.

Quoted textsource-backed
Therefore, CRY2 is essential in regulating skeletal muscle repair.
Claim 2expression regulationsupports2023Source 1DOIPubMed

Loss of CRY2 increases the number of PAX7-positive cells associated with myotubes, suggesting increased reserve cell production.

Quoted textsource-backed
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.
Claim 3functional effectsupports2023Source 1DOIPubMed

CRY2-deficient myoblasts survive better in ischemic muscle.

Quoted textsource-backed
CRY2 deficient myoblasts survived better in ischemic muscle.
Claim 4functional effectsupports2023Source 1DOIPubMed

Deletion of CRY2 enhances muscle regeneration.

Quoted textsource-backed
Using the skeletal muscle lineage and satellite cell-specific CRY2 knockout mice (CRY2scko), we show that the deletion of CRY2 enhances muscle regeneration.
Claim 5functional effectsupports2023Source 1DOIPubMed

Deletion of CRY2 stimulates myoblast proliferation.

Quoted textsource-backed
Single myofiber analysis revealed that deletion of CRY2 stimulates the proliferation of myoblasts.
Claim 6functional effectsupports2023Source 1DOIPubMed

Loss of CRY2 enhances myoblast differentiation, evidenced by increased MyHC expression and myotube formation.

Quoted textsource-backed
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.
Claim 7mechanismsupports2023Source 1DOIPubMed

Loss of CRY2 activates ERK1/2 signaling and ETS1, and ETS1 binds the PAX7 promoter to induce PAX7 transcription.

Quoted textsource-backed
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.
Claim 8applicationsupports2020Source 2DOIPubMed

Cryptochrome 2 and a light-activated degron are used for optogenetic control of gene expression.

Quoted textsource-backed
Optogenetic Control of Gene Expression Using Cryptochrome 2 and a Light-Activated Degron
Claim 9topic scopesupports2019Source 3DOI

The paper concerns optogenetic regulation of gene expression in mammalian cells using cryptochrome 2 (CRY2).

Claim 10cell cycle effectsupports2018Source 4DOIPubMed

CRY2 knockdown increases S phase cell population and reduces G1 phase cell population in HOS osteosarcoma cells.

Quoted textsource-backed
CRY2 knockdown increased the S phase cell population and reduced the G1 phase cell population.
Claim 11clock gene network regulationsupports2018Source 4DOIPubMed

CRY2 knockdown increases mRNA expression of CRY1, PER1, PER2, BMAL1, and CLOCK in HOS osteosarcoma cells.

Quoted textsource-backed
knockdown of CRY2 significantly increased the mRNA expression of CRY1, Period (PER) 1, PER2, BMAL1, and CLOCK.
Claim 12disease rolesupports2018Source 4DOIPubMed

CRY2 may function as an anti-oncogene in osteosarcoma.

Quoted textsource-backed
Our results suggest that CRY2 may be an anti-oncogene in OS
Claim 13expression changesupports2018Source 4DOIPubMed

CRY2 knockdown decreases P53 expression and increases c-myc and cyclin D1 expression in HOS osteosarcoma cells.

Quoted textsource-backed
CRY2 knockdown decreased P53 expression and increased expression of c-myc and cyclin D1.
Claim 14functional rolesupports2018Source 4DOIPubMed

CRY2 suppresses proliferation and migration in HOS osteosarcoma cells.

Quoted textsource-backed
CRY2 knockdown promoted HOS OS cell proliferation and migration.
Claim 15signaling effectsupports2018Source 4DOIPubMed

CRY2 knockdown increases ERK1/2 phosphorylation but does not change JNK and P38 phosphorylation in HOS osteosarcoma cells.

Quoted textsource-backed
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.
Claim 16signaling effectsupports2018Source 4DOIPubMed

CRY2 knockdown increases MMP-2 and β-catenin expression and promotes MAPK and Wnt/β-catenin signaling in HOS osteosarcoma cells.

Quoted textsource-backed
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.
Claim 17expression phenotype associationsupports2016Source 5DOIPubMed

CRY2 mRNA expression in human liver tissue samples was directly associated with hepatic triglyceride content.

Quoted textsource-backed
In human liver tissue samples, CRY2 mRNA expression was directly associated with hepatic triglyceride content.
Claim 18functional hypothesissupports2016Source 5DOIPubMed

CRY2 may act as a switch in hepatic fuel metabolism that promotes triglyceride storage and limits glucose production.

Quoted textsource-backed
Our data may point to CRY2 as a novel switch in hepatic fuel metabolism promoting triglyceride storage and, concomitantly, limiting glucose production.
Claim 19genotype phenotype associationsupports2016Source 5DOIPubMed

Four CRY2 SNPs were associated with fasting glycaemia in non-diabetic individuals.

Quoted textsource-backed
Four CRY2 SNPs were associated with fasting glycaemia, as reported earlier.
Claim 20genotype phenotype associationsupports2016Source 5DOIPubMed

Minor alleles of the CRY2 SNPs associated with fasting glycaemia were associated with elevated fasting glycaemia and reduced liver fat content.

Quoted textsource-backed
Importantly, carriers of these SNPs' minor alleles revealed elevated fasting glycaemia and, concomitantly, reduced liver fat content.
Claim 21negative association resultsupports2016Source 5DOIPubMed

The tested clock gene SNPs were not associated with body fat content, insulin sensitivity, or insulin secretion.

Quoted textsource-backed
None of the tested SNPs was associated with body fat content, insulin sensitivity, or insulin secretion.
Claim 22binding mechanismsupports2015Source 6DOIPubMed

FBXW7 binds directly to phosphorylated Thr300 of CRY2.

Quoted textsource-backed
FBXW7 binds directly to phosphorylated Thr300 of CRY2
Claim 23biomarker implicationsupports2015Source 6DOIPubMed

Upregulation of CRY2 caused by downregulation of FBXW7 may be a novel prognostic biomarker and therapeutic target in colorectal cancer.

Quoted textsource-backed
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.
Claim 24chemosensitivity effectsupports2015Source 6DOIPubMed

High FBXW7 expression downregulates CRY2 and increases colorectal cancer cell sensitivity to chemotherapy.

Quoted textsource-backed
High FBXW7 expression downregulates CRY2 and increases colorectal cancer cells' sensitivity to chemotherapy.
Claim 25chemosensitivity effectsupports2015Source 6DOIPubMed

Knockdown of CRY2 increases colorectal cancer cell sensitivity to oxaliplatin.

Quoted textsource-backed
Knockdown of CRY2 increased colorectal cancer sensitivity to oxaliplatin in colorectal cancer cells.
Claim 26disease associationsupports2015Source 6DOIPubMed

CRY2 is overexpressed in chemoresistant colorectal cancer samples.

Quoted textsource-backed
Here, we report that CRY2 is overexpressed in chemoresistant colorectal cancer samples
Claim 27inverse correlationsupports2015Source 6DOIPubMed

Low FBXW7 expression is correlated with high CRY2 expression in colorectal cancer patient samples.

Quoted textsource-backed
Low FBXW7 expression is correlated with high CRY2 expression in colorectal cancer patient samples.
Claim 28molecular interactionsupports2015Source 6DOIPubMed

FBXW7 is a novel E3 ubiquitin ligase that targets CRY2 for proteasomal degradation.

Quoted textsource-backed
We also identify FBXW7 as a novel E3 ubiquitin ligase for targeting CRY2 through proteasomal degradation.
Claim 29post translational regulationsupports2015Source 6DOIPubMed

FBXW7 expression promotes CRY2 degradation by enhancing CRY2 ubiquitination and accelerating CRY2 turnover.

Quoted textsource-backed
FBXW7 expression leads to degradation of CRY2 through enhancing CRY2 ubiquitination and accelerating the CRY2's turnover rate.
Claim 30prognostic associationsupports2015Source 6DOIPubMed

CRY2 overexpression is correlated with poor patient survival in colorectal cancer.

Quoted textsource-backed
CRY2 overexpression is correlated with poor patient survival
Claim 31tool developmentsupports2013Source 7DOIPubMed

The paper describes development of LITEs, an optogenetic two-hybrid system integrating a TALE DNA-binding domain with cryptochrome 2 and CIB1.

Quoted textsource-backed
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.
Claim 32system basissupports2012Source 8DOIPubMed

The blue light-induced transcription system used in this study is based on the blue light-dependent interaction between CRY2 and CIB1.

Quoted textsource-backed
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).
Claim 33degradation responsesupports2010Source 9DOIPubMed

Exposure to darkness or blue light induces degradation of CRY2 and subsequently HRT, resulting in susceptibility.

Quoted textsource-backed
Exposure to darkness or blue-light induces degradation of CRY2, and in turn HRT, resulting in susceptibility.
Claim 34functional requirementsupports2010Source 9DOIPubMed

CRY2 and PHOT2 are required for HRT stability and thereby resistance to Turnip Crinkle virus.

Quoted textsource-backed
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).
Claim 35genetic compensationsupports2010Source 9DOIPubMed

HRT overexpression compensates for absence of PHOT2 but not absence of CRY2.

Quoted textsource-backed
Overexpression of HRT can compensate for the absence of PHOT2 but not CRY2.
Claim 36mechanistic modelsupports2010Source 9DOIPubMed

CRY2 and PHOT2 negatively regulate proteasome-mediated degradation of HRT, likely via COP1, and blue light relieves this repression resulting in HRT degradation.

Quoted textsource-backed
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.
Claim 37physical interactionsupports2010Source 9DOIPubMed

HRT does not directly associate with CRY2 or PHOT2 but does bind COP1.

Quoted textsource-backed
HRT does not directly associate with either CRY2 or PHOT2 but does bind the CRY2-/PHOT2-interacting E3 ubiquitin ligase, COP1.
Claim 38functional effectsupports2003Source 11DOIPubMed

phyA mediates far-red light promotion of flowering with modes of action similar to cry2.

Quoted textsource-backed
we show that phyA mediates far-red light promotion of flowering with modes of action similar to that of cry2.
Claim 39mechanistic determinantsupports2003Source 11DOIPubMed

The short-day-specific diurnal rhythm of cry2 is determined primarily by blue light-dependent cry2 turnover.

Quoted textsource-backed
The short-day-specific diurnal rhythm of cry2 is determined primarily by blue light-dependent cry2 turnover.
Claim 40model proposalsupports2003Source 11DOIPubMed

Individual phytochromes and cryptochromes work together to confer photoperiodic responsiveness in Arabidopsis, and this responsiveness depends on light quality.

Quoted textsource-backed
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.
Claim 41protein abundance patternsupports2003Source 11DOIPubMed

cry2 and phyA protein abundance show a diurnal rhythm in plants grown in short-day but not in plants grown in long-day.

Quoted textsource-backed
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.
Claim 42role in biological processsupports2003Source 11DOIPubMed

cryptochrome 2 and phytochrome A act as day-length sensors in Arabidopsis.

Quoted textsource-backed
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.
Claim 43domain functionsupports1999Source 13DOIPubMed

The C-terminal domain of CRY2 containing a basic bipartite nuclear localization signal is sufficient to confer nuclear localization of the fusion protein.

Quoted textsource-backed
The C-terminal domain of cry2 that contains the basic bipartite nuclear localization signal was sufficient to confer nuclear localization of the fusion protein.
Claim 44subcellular localizationsupports1999Source 13DOIPubMed

CRY2 is a nuclear protein.

Quoted textsource-backed
These results strongly suggest that cry2 is a nuclear protein.
Claim 45comparative functionsupports1998Source 14DOIPubMed

In contrast to CRY1, CRY2 functions primarily under low light during early seedling development.

Quoted textsource-backed
In contrast to CRY1 ... cryptochrome 2 functions primarily under low light during the early development of seedlings.
Claim 46expression localizationsupports1998Source 15DOIPubMed

CRY1 and CRY2 are specifically expressed in the ganglion cell and inner nuclear layers of the mouse retina.

Quoted textsource-backed
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.
Claim 47functional rolesupports1998Source 14DOIPubMed

Cryptochrome 2 mediates blue light-dependent inhibition of hypocotyl elongation in Arabidopsis seedlings under low blue light intensities.

Quoted textsource-backed
It is found that cryptochrome 2 mediates blue light-dependent inhibition of hypocotyl elongation ... under low intensities of blue light.
Claim 48functional rolesupports1998Source 14DOIPubMed

Cryptochrome 2 mediates blue light-dependent stimulation of cotyledon opening in Arabidopsis seedlings under low blue light intensities.

Quoted textsource-backed
It is found that cryptochrome 2 mediates ... stimulation of cotyledon opening under low intensities of blue light.
Claim 49regulationsupports1998Source 14DOIPubMed

CRY2 expression is rapidly down-regulated by blue light in a light-intensity dependent manner.

Quoted textsource-backed
the expression of CRY2 is rapidly down-regulated by blue light in a light-intensity dependent manner