Arabidopsis thaliana CRY2 (cryptochrome 2; At1g04400) is a nuclear, FAD-binding plant cryptochrome that functions as a blue-light photoreceptor. Blue-light excitation promotes CRY2 phosphorylation, homodimerization/oligomerization, nuclear photobody formation, and interactions with signaling partners including SPA/COP1, CIB transcription factors, PIF4/PIF5, BIC proteins, and flowering regulators. Its principal biological outputs are blue-light signaling, low-blue-light growth responses, and photoperiodic promotion of flowering through CO/FT and CIB-dependent pathways; broader effects on chromatin state, stomata, circadian rhythms, ROS, pathogen defense, and hormone responses are treated as downstream or context-specific outputs rather than the core molecular function.
Definition: A nuclear body formed by photoactivated cryptochrome photoreceptors in response to blue light and associated with cryptochrome signaling, phosphorylation, ubiquitination, partner colocalization, or turnover.
Justification: CRY2 annotations currently use the broad nuclear body term, while the UniProt-derived PML body mapping is inappropriate for Arabidopsis. A plant cryptochrome photobody term would capture the specific light-induced CRY2 compartment supported by multiple studies.
Parent term: nuclear body
Supporting Evidence:
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0016301 kinase activity | IDA NOT PMID:17073458 Analysis of autophosphorylating kinase activities of Arabido... | ACCEPT | Summary: Correct negated annotation: Arabidopsis CRY2 is not an autokinase. Reason: PMID:17073458 directly tested AtCry2 and found that it lacked kinase activity despite FAD binding; retaining the NOT kinase annotation prevents propagation of the older cryptochrome autokinase model to CRY2. Supporting Evidence: PMID:17073458 AtCry2 which is known to be phosphorylated upon light exposure in vivo ( 16 ) lacked kinase activity. |
| GO:0046777 protein autophosphorylation | IDA NOT PMID:17073458 Analysis of autophosphorylating kinase activities of Arabido... | ACCEPT | Summary: Correct negated annotation: AtCRY2 does not carry out protein autophosphorylation. Reason: The same biochemical study found AtCry2 lacks autokinase/autophosphorylating activity, so the NOT annotation is appropriate. Supporting Evidence: PMID:17073458 AtCry2, which also contains stoichiometric amounts of FAD does not. |
| GO:0006325 chromatin organization | IMP PMID:20935177 Photoreceptors CRYTOCHROME2 and phytochrome B control chroma... | KEEP AS NON CORE | Summary: Supported downstream chromatin phenotype, not the core molecular role of CRY2. Reason: CRY2 contributes to light-dependent chromatin compaction/decompaction, but as a photoreceptor signaling input rather than a chromatin-organizing factor. Supporting Evidence: PMID:20935177 Photoreceptors CRYTOCHROME2 and phytochrome B control chromatin compaction in Arabidopsis. file:ARATH/CRY2/CRY2-uniprot.txt Photoreceptor that mediates primarily blue light inhibition of hypocotyl elongation and photoperiodic control of floral initiation |
| GO:0006338 chromatin remodeling | IMP PMID:17470059 Light-regulated large-scale reorganization of chromatin duri... | KEEP AS NON CORE | Summary: Supported as a downstream flowering-transition chromatin phenotype. Reason: The annotation uses acts_upstream_of_or_within and is best treated as a non-core consequence of CRY2 signaling during floral transition, not as chromatin-remodeling activity by CRY2 itself. Supporting Evidence: PMID:17470059 Light-regulated large-scale reorganization of chromatin during the floral transition in Arabidopsis. file:ARATH/CRY2/CRY2-uniprot.txt Photoreceptor that mediates primarily blue light inhibition of hypocotyl elongation and photoperiodic control of floral initiation |
| GO:0009414 response to water deprivation | IGI PMID:16093319 From The Cover: A role for Arabidopsis cryptochromes and COP... | KEEP AS NON CORE | Summary: Water-deprivation phenotypes arise through CRY-dependent stomatal regulation. Reason: CRY2 contributes to water-loss and drought-related phenotypes through stomatal opening, but this is a physiological output of blue-light signaling and not the core function of the photoreceptor. Supporting Evidence: PMID:16093319 CRY functions additively with PHOT in mediating blue light-induced stomatal opening |
| GO:0009416 response to light stimulus | IEP PMID:20935177 Photoreceptors CRYTOCHROME2 and phytochrome B control chroma... | MODIFY | Summary: The evidence supports a blue-light photoreceptor/signaling role; this term is too broad. Reason: CRY2 senses blue light and signals through CIB, SPA/COP1, PIF, and related partners. The generic response to light stimulus term should be replaced by blue-light-specific terms. Proposed replacements: response to blue light blue light signaling pathway Supporting Evidence: PMID:22311776 CRY2 is a constitutive nuclear protein that undergoes blue-light-dependent phosphorylation, ubiquitination, photobody formation, and degradation in the nucleus PMID:26724867 CRY1 and CRY2 perceive this change and respond by directly contacting two bHLH transcription factors, PIF4 and PIF5. PMID:36508461 A role for brassinosteroid signalling in decision-making processes in the Arabidopsis seedling. |
| GO:0009416 response to light stimulus | IMP PMID:36508461 A role for brassinosteroid signalling in decision-making pro... | MODIFY | Summary: The evidence supports a blue-light photoreceptor/signaling role; this term is too broad. Reason: CRY2 senses blue light and signals through CIB, SPA/COP1, PIF, and related partners. The generic response to light stimulus term should be replaced by blue-light-specific terms. Proposed replacements: response to blue light blue light signaling pathway Supporting Evidence: PMID:22311776 CRY2 is a constitutive nuclear protein that undergoes blue-light-dependent phosphorylation, ubiquitination, photobody formation, and degradation in the nucleus PMID:26724867 CRY1 and CRY2 perceive this change and respond by directly contacting two bHLH transcription factors, PIF4 and PIF5. PMID:36508461 A role for brassinosteroid signalling in decision-making processes in the Arabidopsis seedling. |
| GO:0009637 response to blue light | IMP PMID:9565033 Cryptochrome blue-light photoreceptors of Arabidopsis implic... | ACCEPT | Summary: Core biological process: CRY2 mediates blue-light responses. Reason: Multiple genetic, biochemical, and cell biological studies support CRY2 as a blue-light photoreceptor controlling phototropism, flowering, clock, and growth outputs. Supporting Evidence: PMID:9565033 cryptochrome is one of the photoreceptors mediating phototropism in plants. PMID:12857830 phototropins and cryptochromes function together to enhance phototropism under low fluence rates PMID:21514160 CRY2 undergoes blue light-dependent physical interaction with SPA1. PMID:24130508 CIB1 (CRY2-interacting bHLH 1) specifically interacts with CRY2 in response to blue light to activate the transcription of FT PMID:24780222 Upon illumination, CRY2 is photoactivated to contact and associate with CIB1. PMID:23511208 reducing the fluence rate of either light quality or mutating the phy or cry photoreceptors lengthens the circadian period |
| GO:0009785 blue light signaling pathway | IGI PMID:27846570 Photoactivation and inactivation of Arabidopsis cryptochrome... | ACCEPT | Summary: Core pathway annotation: CRY2 is a blue-light signaling photoreceptor. Reason: CRY2 photoactivation, homodimerization, photobody formation, and interaction with signaling partners such as BIC1, SPA1, and CIBs are central to blue-light signaling. Supporting Evidence: PMID:27846570 Arabidopsis cryptochrome 2 (CRY2) undergoes blue light-dependent homodimerization to become physiologically active. PMID:27846570 BICs also inhibit the blue light-induced formation of CRY2 photobodies PMID:21514160 CRY2 undergoes blue light-dependent physical interaction with SPA1. |
| GO:0009909 regulation of flower development | IDA PMID:17259260 CRYPTOCHROME2 in vascular bundles regulates flowering in Ara... | ACCEPT | Summary: CRY2 regulates flowering through vascular-bundle FT expression. Reason: CRY2 in vascular bundles promotes FT expression and flowering, making regulation of flower development a major supported developmental output. Supporting Evidence: PMID:17259260 cry2-GFP expressed in vascular bundles increased FT expression only in vascular bundles. |
| GO:0009911 positive regulation of flower development | IMP PMID:17259260 CRYPTOCHROME2 in vascular bundles regulates flowering in Ara... | ACCEPT | Summary: CRY2 positively regulates flowering in appropriate light/photoperiod contexts. Reason: CRY2-GFP expression in vascular bundles rescues late flowering and increases FT expression; this supports a positive flowering role. Supporting Evidence: PMID:17259260 cry2-GFP expressed in vascular bundles increased FT expression only in vascular bundles. |
| GO:0010075 regulation of meristem growth | IGI PMID:18424613 Distinct light-initiated gene expression and cell cycle prog... | KEEP AS NON CORE | Summary: Supported light-dependent shoot apex/meristem phenotype, not core photoreceptor function. Reason: CRY2 affects meristem/cell-cycle programs downstream of light perception, but its core role remains blue-light photoreceptor signaling. Supporting Evidence: file:ARATH/CRY2/CRY2-uniprot.txt Photoreceptor that mediates primarily blue light inhibition of hypocotyl elongation and photoperiodic control of floral initiation |
| GO:0010118 stomatal movement | IGI PMID:16093319 From The Cover: A role for Arabidopsis cryptochromes and COP... | KEEP AS NON CORE | Summary: Supported stomatal output of CRY signaling. Reason: CRY2 participates with CRY1/PHOT/COP1 pathways in blue-light-induced stomatal opening, but stomatal movement is a downstream physiological response. Supporting Evidence: PMID:16093319 CRY functions additively with PHOT in mediating blue light-induced stomatal opening |
| GO:0010617 circadian regulation of calcium ion oscillation | IMP PMID:17982000 Distinct light and clock modulation of cytosolic free Ca2+ o... | KEEP AS NON CORE | Summary: Circadian calcium oscillation is a downstream clock/light-signaling phenotype. Reason: The evidence links cryptochrome light input to clock-regulated calcium rhythms; this is not the primary molecular function of CRY2. Supporting Evidence: PMID:11743105 Photoreceptors, phytochromes, and cryptochromes are involved in setting the clock by transducing the light signal to the central oscillator. |
| GO:0003904 deoxyribodipyrimidine photo-lyase activity | IBA GO_REF:0000033 | REMOVE | Summary: Over-propagated photolyase-family annotation; CRY2 is a signaling cryptochrome, not a DNA photolyase. Reason: PANTHER PTHR11455 mixes cryptochromes and DNA photolyases, and UniProt explicitly cautions that CRY2 was originally thought to be a DNA photolyase. The Arabidopsis CRY2 literature supports FAD-dependent blue-light signaling rather than deoxyribodipyrimidine repair activity. Propagation Review Root cause: PROPAGATION BAD Failure modes: FUNCTIONAL DIVERGENCE PSEUDO OR SUBACTIVITY LOSS Sources checked: PANTHER:PTN000155848 · photolyase/cryptochrome family node SUPPORTS SOURCE BUT NOT TARGET The photolyase IBD is seeded by genuine DNA photolyases; the family mixes photolyases and catalytically inactive cryptochromes. PAINT already carries an IRD pruning this term for the metazoan cryptochrome clade (PTN000894457), but the plant cryptochrome clade lacks an equivalent IRD/IKR, so the term still reaches CRY2; an IRD for plant CRYs would fix this at source. UniProtKB:P00914 · E. coli DNA photolyase SUPPORTS SOURCE BUT NOT TARGET A genuine photolyase seed; plant cryptochromes retained the fold but lost repair activity. Supporting Evidence: file:interpro/panther/PTHR11455/PTHR11455-notes.md The family contains both cryptochromes and photolyases; subfamilies separate circadian cryptochromes from repair enzymes. file:ARATH/CRY2/CRY2-uniprot.txt Photoreceptor that mediates primarily blue light inhibition of hypocotyl elongation and photoperiodic control of floral initiation |
| GO:0005515 protein binding | IPI PMID:11089975 Functional interaction of phytochrome B and cryptochrome 2. | REMOVE | Summary: PHYB interaction supports photoreceptor crosstalk, but GO:0005515 is too generic for CRY2. Reason: The evidence supports light-dependent CRY2-PHYB crosstalk in flowering, hypocotyl, and clock outputs. It does not define a distinct CRY2 molecular function beyond blue-light photoreceptor signaling, so generic protein binding should not be retained. Supporting Evidence: PMID:11089975 PhyB interacts directly with cry2 as observed in co-immunoprecipitation experiments with transgenic Arabidopsis plants overexpressing cry2. |
| GO:0005515 protein binding | IPI PMID:11509693 Direct interaction of Arabidopsis cryptochromes with COP1 in... | MODIFY | Summary: COP1 binding is real and mechanistically important, but generic protein binding should be replaced. Reason: COP1 is the E3 ubiquitin ligase repressed by photoactivated cryptochromes. Ubiquitin protein ligase binding captures the relevant molecular interaction better than GO:0005515. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: PMID:11509693 Photoactivated cryptochromes repress COP1 activity through a direct protein-protein contact. |
| GO:0005515 protein binding | IPI PMID:18988809 Photoexcited CRY2 interacts with CIB1 to regulate transcript... | MODIFY | Summary: CIB1 interaction should be captured as bHLH transcription factor binding, not generic protein binding. Reason: CIB1 is a CRY2-interacting basic helix-loop-helix transcription factor that promotes FT expression and floral initiation. The more specific bHLH transcription factor binding term captures this interaction. Proposed replacements: bHLH transcription factor binding Supporting Evidence: PMID:18988809 CIB1 interacts with CRY2 (cryptochrome 2) in a blue light-specific manner in yeast and Arabidopsis cells PMID:18988809 CIB1 binds to G box (CACGTG) in vitro with a higher affinity than its interaction with other E-box elements (CANNTG). |
| GO:0005515 protein binding | IPI PMID:20624951 Cryptochrome 2 and phototropin 2 regulate resistance protein... | MODIFY | Summary: The defense-context interaction is mediated through COP1, so generic protein binding should be replaced. Reason: The paper links CRY2/PHOT2 control of resistance protein stability to COP1, an E3 ubiquitin ligase. Ubiquitin protein ligase binding is more informative than retaining GO:0005515. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: PMID:20624951 HRT does not directly associate with either CRY2 or PHOT2 but does bind the CRY2-/PHOT2-interacting E3 ubiquitin ligase, COP1. |
| GO:0005515 protein binding | IPI PMID:21511872 Blue-light-dependent interaction of cryptochrome 1 with SPA1... | REMOVE | Summary: This SPA1 paper is CRY1-focused and does not justify retaining generic CRY2 protein binding. Reason: The source title and evidence concern cryptochrome 1-SPA1 signaling. Even if related to the broader cryptochrome mechanism, GO:0005515 is not an informative CRY2 molecular function and should not remain as a non-core annotation. Supporting Evidence: PMID:21511872 Blue-light-dependent interaction of cryptochrome 1 with SPA1 defines a dynamic signaling mechanism. |
| GO:0005515 protein binding | IPI PMID:21514160 Blue light-dependent interaction of CRY2 with SPA1 regulates... | MODIFY | Summary: CRY2-SPA1/COP1 complex formation should be captured with a COP1 ligase-binding term. Reason: SPA1 acts through the COP1 E3 ubiquitin ligase, and the study shows CRY2-SPA1 interaction enhances CRY2-COP1 interaction and suppresses COP1-dependent CO degradation. Ubiquitin protein ligase binding is more informative than GO:0005515. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: PMID:21514160 CRY2 undergoes blue light-dependent physical interaction with SPA1. PMID:21514160 The blue light-dependent CRY2-SPA1 interaction enhances the CRY2-COP1 interaction to suppress the COP1 activity. |
| GO:0005515 protein binding | IPI PMID:22139370 Arabidopsis cryptochrome 2 (CRY2) functions by the photoacti... | REMOVE | Summary: Photoactivation mechanism evidence does not require retaining generic protein binding. Reason: The paper supports CRY2 photoactivation biology, which is already represented by blue-light photoreceptor activity and blue-light signaling annotations. GO:0005515 is too broad to retain. Supporting Evidence: PMID:22139370 Arabidopsis cryptochrome 2 (CRY2) functions by the photoactivation mechanism distinct from the tryptophan (trp) triad-dependent photoreduction. |
| GO:0005515 protein binding | IPI PMID:22739826 Degradation of Arabidopsis CRY2 is regulated by SPA proteins... | REMOVE | Summary: SPA-dependent CRY2 degradation is pathway regulation, not a useful generic binding annotation. Reason: The evidence supports control of CRY2 abundance by SPA proteins and phyA. This is already captured in CRY2 signaling/degradation context, while GO:0005515 adds no informative molecular function. Supporting Evidence: PMID:22739826 Studies showed a robust physical interaction of cry2 with SPA1 in nuclei of living cells. |
| GO:0005515 protein binding | IPI PMID:24130508 Multiple bHLH proteins form heterodimers to mediate CRY2-dep... | MODIFY | Summary: CIB-family interactions should be represented as bHLH transcription factor binding. Reason: CIB proteins are bHLH transcription factors that act redundantly downstream of CRY2 in flowering. The specific bHLH transcription factor binding term is more informative than GO:0005515. Proposed replacements: bHLH transcription factor binding Supporting Evidence: PMID:24130508 Our study demonstrates that CIBs function redundantly in regulating CRY2-dependent flowering. |
| GO:0005515 protein binding | IPI PMID:24780222 Quantitative real-time kinetics of optogenetic proteins CRY2... | MODIFY | Summary: CRY2-CIB1 kinetic interaction should be replaced by bHLH transcription factor binding. Reason: CIB1 is a bHLH transcription factor and the evidence measures blue-light-driven CRY2 association with CIB1. GO:0043425 is more specific than generic protein binding. Proposed replacements: bHLH transcription factor binding Supporting Evidence: PMID:24780222 Upon illumination, CRY2 is photoactivated to contact and associate with CIB1. |
| GO:0005515 protein binding | IPI PMID:26724867 Cryptochromes Interact Directly with PIFs to Control Plant G... | MODIFY | Summary: PIF4/PIF5 contacts should be represented as bHLH transcription factor binding. Reason: PIF4 and PIF5 are bHLH transcription factors contacted by CRY2 during low-blue-light growth regulation. GO:0043425 is the informative replacement for generic protein binding. Proposed replacements: bHLH transcription factor binding Supporting Evidence: PMID:26724867 CRY1 and CRY2 perceive this change and respond by directly contacting two bHLH transcription factors, PIF4 and PIF5. |
| GO:0005515 protein binding | IPI PMID:27846570 Photoactivation and inactivation of Arabidopsis cryptochrome... | REMOVE | Summary: BIC1 interaction explains CRY2 inactivation but does not warrant retaining GO:0005515. Reason: BIC1 is an inhibitory regulator of CRY2 homodimerization and photobody formation. The biology belongs in the blue-light signaling description, while generic protein binding remains uninformative. Supporting Evidence: PMID:27846570 BICs also inhibit the blue light-induced formation of CRY2 photobodies. |
| GO:0005515 protein binding | IPI PMID:28492234 Molecular basis for blue light-dependent phosphorylation of ... | MODIFY | Summary: PPK interaction should be captured as protein kinase binding. Reason: The study identifies photoregulatory protein kinases that bind photoexcited CRY2 and catalyze blue-light-dependent CRY2 phosphorylation. Protein kinase binding is more informative than GO:0005515. Proposed replacements: protein kinase binding Supporting Evidence: PMID:28492234 Photoregulatory Protein Kinases (previously referred to as MUT9-like kinases) interact with and phosphorylate photoexcited CRY2. |
| GO:0005515 protein binding | IPI PMID:28633330 The asparagine-rich protein NRP interacts with the Verticill... | REMOVE | Summary: NRP-dependent localization effects are not an informative CRY2 protein binding annotation. Reason: The evidence links NRP/PevD1 context to CRY2 subcellular localization. No more specific CRY2 molecular function term is supported, and generic protein binding should not be retained. Supporting Evidence: PMID:28633330 The asparagine-rich protein NRP interacts with the Verticillium effector PevD1 and regulates the subcellular localization of cryptochrome 2. |
| GO:0005515 protein binding | IPI PMID:32661061 Photoexcited Cryptochrome2 Interacts Directly with TOE1 and ... | MODIFY | Summary: TOE1/TOE2 interactions should be represented as DNA-binding transcription factor binding. Reason: TOE1 and TOE2 are AP2-like DNA-binding transcription factors that interact with photoexcited CRY2 in flowering regulation. GO:0140297 is more informative than generic protein binding. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:32661061 Photoexcited Cryptochrome2 Interacts Directly with TOE1 and TOE2 in Flowering Regulation. PMID:32661061 The AP2-like transcriptional factor TOE1 negatively regulates FT expression and flowering by indirectly inhibiting CO transcriptional activation activity and directly binding to FT. |
| GO:0005515 protein binding | IPI PMID:36396657 CRY2 interacts with CIS1 to regulate thermosensory flowering... | REMOVE | Summary: CIS1 interaction supports thermosensory flowering signaling, but generic protein binding should not be retained. Reason: CIS1 is a splicing/RNA-binding factor whose activity is regulated in a CRY2-dependent pathway. The evidence is important for biological process interpretation, but GO:0005515 is not an informative CRY2 molecular function. Supporting Evidence: PMID:36396657 CRY2 interacts with CIS1 to regulate thermosensory flowering via FLM alternative splicing. |
| GO:0005524 ATP binding | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ATP binding is supported but is an accessory biochemical property of the photoreceptor. Reason: UniProt and biochemical literature support ATP binding as influencing CRY2 conformation/photochemistry, but ATP binding is not the central GO molecular function; blue-light photoreceptor activity is the core MF. Supporting Evidence: file:ARATH/CRY2/CRY2-uniprot.txt Binding to ATP mediates conformational changes which facilitate flavin binding file:ARATH/CRY2/CRY2-deep-research-falcon.md Arabidopsis thaliana CRY2 (UniProt: Q96524) is a plant blue-light photoreceptor |
| GO:0005524 ATP binding | IDA PMID:17073458 Analysis of autophosphorylating kinase activities of Arabido... | KEEP AS NON CORE | Summary: ATP binding is supported but is an accessory biochemical property of the photoreceptor. Reason: UniProt and biochemical literature support ATP binding as influencing CRY2 conformation/photochemistry, but ATP binding is not the central GO molecular function; blue-light photoreceptor activity is the core MF. Supporting Evidence: file:ARATH/CRY2/CRY2-uniprot.txt Binding to ATP mediates conformational changes which facilitate flavin binding file:ARATH/CRY2/CRY2-deep-research-falcon.md Arabidopsis thaliana CRY2 (UniProt: Q96524) is a plant blue-light photoreceptor |
| GO:0009882 blue light photoreceptor activity | IEA GO_REF:0000002 | ACCEPT | Summary: Core molecular function: CRY2 is a blue-light photoreceptor. The crystal structure of the CRY2 PHR/photolyase-homology region (CRY2N) with bound FAD (PDB 6K8I) directly visualizes the FAD-bound photosensory module underlying this activity. Reason: CRY2 is a plant cryptochrome whose FAD-dependent blue-light photoactivation drives dimerization, photobody formation, and downstream signaling. Supporting Evidence: PMID:22311776 CRY2 is a constitutive nuclear protein that undergoes blue-light-dependent phosphorylation, ubiquitination, photobody formation, and degradation in the nucleus PMID:27846570 Arabidopsis cryptochrome 2 (CRY2) undergoes blue light-dependent homodimerization to become physiologically active. PMID:32398826 Cryptochromes (CRYs) are blue-light receptors in plants that harbor FAD as a cofactor and regulate various physiological responses. file:ARATH/CRY2/CRY2-deep-research-falcon.md Arabidopsis thaliana CRY2 (UniProt: Q96524) is a plant blue-light photoreceptor |
| GO:0009882 blue light photoreceptor activity | ISS PMID:11493548 Hierarchical coupling of phytochromes and cryptochromes reco... | ACCEPT | Summary: Core molecular function: CRY2 is a blue-light photoreceptor. Reason: CRY2 is a plant cryptochrome whose FAD-dependent blue-light photoactivation drives dimerization, photobody formation, and downstream signaling. Supporting Evidence: PMID:22311776 CRY2 is a constitutive nuclear protein that undergoes blue-light-dependent phosphorylation, ubiquitination, photobody formation, and degradation in the nucleus PMID:27846570 Arabidopsis cryptochrome 2 (CRY2) undergoes blue light-dependent homodimerization to become physiologically active. PMID:32398826 Cryptochromes (CRYs) are blue-light receptors in plants that harbor FAD as a cofactor and regulate various physiological responses. file:ARATH/CRY2/CRY2-deep-research-falcon.md Arabidopsis thaliana CRY2 (UniProt: Q96524) is a plant blue-light photoreceptor |
| GO:0042802 identical protein binding | IPI PMID:15805487 N-terminal domain-mediated homodimerization is required for ... | KEEP AS NON CORE | Summary: Self-association is an important activation mechanism but not the primary MF term. Reason: CRY2 homodimerization/oligomerization is physiologically important for photoactivation and photobody formation, but this term should support the photoreceptor mechanism rather than replace blue-light photoreceptor activity as the core MF. Supporting Evidence: PMID:27846570 Arabidopsis cryptochrome 2 (CRY2) undergoes blue light-dependent homodimerization to become physiologically active. PMID:22311776 photoexcited cryptochromes form oligomers, preceding other biochemical changes of CRY2 |
| GO:0042802 identical protein binding | IPI PMID:17438275 Derepression of the NC80 motif is critical for the photoacti... | KEEP AS NON CORE | Summary: Self-association is an important activation mechanism but not the primary MF term. Reason: CRY2 homodimerization/oligomerization is physiologically important for photoactivation and photobody formation, but this term should support the photoreceptor mechanism rather than replace blue-light photoreceptor activity as the core MF. Supporting Evidence: PMID:27846570 Arabidopsis cryptochrome 2 (CRY2) undergoes blue light-dependent homodimerization to become physiologically active. PMID:22311776 photoexcited cryptochromes form oligomers, preceding other biochemical changes of CRY2 |
| GO:0042803 protein homodimerization activity | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Homodimerization is supported mechanistically but is secondary to photoreceptor activity. Reason: CRY2 becomes physiologically active through blue-light-dependent homodimerization, but the core molecular function is blue-light photoreceptor activity. Supporting Evidence: PMID:27846570 Arabidopsis cryptochrome 2 (CRY2) undergoes blue light-dependent homodimerization to become physiologically active. |
| GO:0042803 protein homodimerization activity | IPI PMID:15805487 N-terminal domain-mediated homodimerization is required for ... | KEEP AS NON CORE | Summary: Homodimerization is supported mechanistically but is secondary to photoreceptor activity. Reason: CRY2 becomes physiologically active through blue-light-dependent homodimerization, but the core molecular function is blue-light photoreceptor activity. Supporting Evidence: PMID:27846570 Arabidopsis cryptochrome 2 (CRY2) undergoes blue light-dependent homodimerization to become physiologically active. |
| GO:0071949 FAD binding | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: FAD binding is an essential chromophore-binding property of CRY2. The crystal structures of CRY2N (PDB 6K8I; and 6K8K with FAD plus Mg/AMP) resolve the bound FAD cofactor in the photolyase-homology region. Reason: CRY2 is an FAD-containing photoreceptor; FAD binding supports photochemistry but is best treated as a non-core cofactor-binding annotation relative to blue-light photoreceptor activity. Supporting Evidence: PMID:17073458 Cryptochromes are FAD-based blue-light photoreceptors that regulate growth and development in plants and the circadian clock in animals. PMID:32398826 Cryptochromes (CRYs) are blue-light receptors in plants that harbor FAD as a cofactor and regulate various physiological responses. file:ARATH/CRY2/CRY2-uniprot.txt Binds 1 FAD per subunit. |
| GO:0071949 FAD binding | IDA PMID:17073458 Analysis of autophosphorylating kinase activities of Arabido... | KEEP AS NON CORE | Summary: FAD binding is an essential chromophore-binding property of CRY2. The crystal structures of CRY2N (PDB 6K8I; and 6K8K with FAD plus Mg/AMP) resolve the bound FAD cofactor in the photolyase-homology region. Reason: CRY2 is an FAD-containing photoreceptor; FAD binding supports photochemistry but is best treated as a non-core cofactor-binding annotation relative to blue-light photoreceptor activity. Supporting Evidence: PMID:17073458 Cryptochromes are FAD-based blue-light photoreceptors that regulate growth and development in plants and the circadian clock in animals. PMID:32398826 Cryptochromes (CRYs) are blue-light receptors in plants that harbor FAD as a cofactor and regulate various physiological responses. file:ARATH/CRY2/CRY2-uniprot.txt Binds 1 FAD per subunit. |
| GO:0007623 circadian rhythm | IEP PMID:11743105 Circadian clock-regulated expression of phytochrome and cryp... | KEEP AS NON CORE | Summary: CRY2 expression and signaling are connected to the circadian system, but this is not the core CRY2 role. Reason: Cryptochromes provide light input to circadian regulation, while CRY2 core function is blue-light photoreceptor signaling. Supporting Evidence: PMID:11743105 Photoreceptors, phytochromes, and cryptochromes are involved in setting the clock by transducing the light signal to the central oscillator. |
| GO:0009414 response to water deprivation | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Water-deprivation phenotypes arise through CRY-dependent stomatal regulation. Reason: CRY2 contributes to water-loss and drought-related phenotypes through stomatal opening, but this is a physiological output of blue-light signaling and not the core function of the photoreceptor. Supporting Evidence: PMID:16093319 CRY functions additively with PHOT in mediating blue light-induced stomatal opening |
| GO:0009416 response to light stimulus | IMP PMID:21296763 Double loss-of-function mutation in EARLY FLOWERING 3 and CR... | MODIFY | Summary: The evidence supports a blue-light photoreceptor/signaling role; this term is too broad. Reason: CRY2 senses blue light and signals through CIB, SPA/COP1, PIF, and related partners. The generic response to light stimulus term should be replaced by blue-light-specific terms. Proposed replacements: response to blue light blue light signaling pathway Supporting Evidence: PMID:22311776 CRY2 is a constitutive nuclear protein that undergoes blue-light-dependent phosphorylation, ubiquitination, photobody formation, and degradation in the nucleus PMID:26724867 CRY1 and CRY2 perceive this change and respond by directly contacting two bHLH transcription factors, PIF4 and PIF5. PMID:36508461 A role for brassinosteroid signalling in decision-making processes in the Arabidopsis seedling. |
| GO:0009637 response to blue light | IMP PMID:12857830 Second positive phototropism results from coordinated co-act... | ACCEPT | Summary: Core biological process: CRY2 mediates blue-light responses. Reason: Multiple genetic, biochemical, and cell biological studies support CRY2 as a blue-light photoreceptor controlling phototropism, flowering, clock, and growth outputs. Supporting Evidence: PMID:9565033 cryptochrome is one of the photoreceptors mediating phototropism in plants. PMID:12857830 phototropins and cryptochromes function together to enhance phototropism under low fluence rates PMID:21514160 CRY2 undergoes blue light-dependent physical interaction with SPA1. PMID:24130508 CIB1 (CRY2-interacting bHLH 1) specifically interacts with CRY2 in response to blue light to activate the transcription of FT PMID:24780222 Upon illumination, CRY2 is photoactivated to contact and associate with CIB1. PMID:23511208 reducing the fluence rate of either light quality or mutating the phy or cry photoreceptors lengthens the circadian period |
| GO:0009637 response to blue light | IEP PMID:20624951 Cryptochrome 2 and phototropin 2 regulate resistance protein... | ACCEPT | Summary: Core biological process: CRY2 mediates blue-light responses. Reason: Multiple genetic, biochemical, and cell biological studies support CRY2 as a blue-light photoreceptor controlling phototropism, flowering, clock, and growth outputs. Supporting Evidence: PMID:20624951 The blue-light photoreceptors, cryptochrome (CRY) 2 and phototropin (PHOT) 2, are required for the stability of the R protein HRT PMID:9565033 cryptochrome is one of the photoreceptors mediating phototropism in plants. PMID:12857830 phototropins and cryptochromes function together to enhance phototropism under low fluence rates PMID:21514160 CRY2 undergoes blue light-dependent physical interaction with SPA1. PMID:24130508 CIB1 (CRY2-interacting bHLH 1) specifically interacts with CRY2 in response to blue light to activate the transcription of FT PMID:24780222 Upon illumination, CRY2 is photoactivated to contact and associate with CIB1. PMID:23511208 reducing the fluence rate of either light quality or mutating the phy or cry photoreceptors lengthens the circadian period |
| GO:0009637 response to blue light | IDA PMID:21511872 Blue-light-dependent interaction of cryptochrome 1 with SPA1... | ACCEPT | Summary: Core biological process: CRY2 mediates blue-light responses. Reason: Multiple genetic, biochemical, and cell biological studies support CRY2 as a blue-light photoreceptor controlling phototropism, flowering, clock, and growth outputs. Supporting Evidence: PMID:21514160 blue light enhances colocalization of the CRY2 and MycSPA1 proteins in the nuclear bodies PMID:9565033 cryptochrome is one of the photoreceptors mediating phototropism in plants. PMID:12857830 phototropins and cryptochromes function together to enhance phototropism under low fluence rates PMID:21514160 CRY2 undergoes blue light-dependent physical interaction with SPA1. PMID:24130508 CIB1 (CRY2-interacting bHLH 1) specifically interacts with CRY2 in response to blue light to activate the transcription of FT PMID:24780222 Upon illumination, CRY2 is photoactivated to contact and associate with CIB1. PMID:23511208 reducing the fluence rate of either light quality or mutating the phy or cry photoreceptors lengthens the circadian period |
| GO:0009637 response to blue light | IDA PMID:21514160 Blue light-dependent interaction of CRY2 with SPA1 regulates... | ACCEPT | Summary: Core biological process: CRY2 mediates blue-light responses. Reason: Multiple genetic, biochemical, and cell biological studies support CRY2 as a blue-light photoreceptor controlling phototropism, flowering, clock, and growth outputs. Supporting Evidence: PMID:9565033 cryptochrome is one of the photoreceptors mediating phototropism in plants. PMID:12857830 phototropins and cryptochromes function together to enhance phototropism under low fluence rates PMID:21514160 CRY2 undergoes blue light-dependent physical interaction with SPA1. PMID:24130508 CIB1 (CRY2-interacting bHLH 1) specifically interacts with CRY2 in response to blue light to activate the transcription of FT PMID:24780222 Upon illumination, CRY2 is photoactivated to contact and associate with CIB1. PMID:23511208 reducing the fluence rate of either light quality or mutating the phy or cry photoreceptors lengthens the circadian period |
| GO:0009637 response to blue light | IDA PMID:22739826 Degradation of Arabidopsis CRY2 is regulated by SPA proteins... | ACCEPT | Summary: Core biological process: CRY2 mediates blue-light responses. Reason: Multiple genetic, biochemical, and cell biological studies support CRY2 as a blue-light photoreceptor controlling phototropism, flowering, clock, and growth outputs. Supporting Evidence: PMID:22739826 Degradation of Arabidopsis CRY2 is regulated by SPA proteins and phytochrome A. PMID:9565033 cryptochrome is one of the photoreceptors mediating phototropism in plants. PMID:12857830 phototropins and cryptochromes function together to enhance phototropism under low fluence rates PMID:21514160 CRY2 undergoes blue light-dependent physical interaction with SPA1. PMID:24130508 CIB1 (CRY2-interacting bHLH 1) specifically interacts with CRY2 in response to blue light to activate the transcription of FT PMID:24780222 Upon illumination, CRY2 is photoactivated to contact and associate with CIB1. PMID:23511208 reducing the fluence rate of either light quality or mutating the phy or cry photoreceptors lengthens the circadian period |
| GO:0009637 response to blue light | IMP PMID:23511208 Network balance via CRY signalling controls the Arabidopsis ... | ACCEPT | Summary: Core biological process: CRY2 mediates blue-light responses. Reason: Multiple genetic, biochemical, and cell biological studies support CRY2 as a blue-light photoreceptor controlling phototropism, flowering, clock, and growth outputs. Supporting Evidence: PMID:9565033 cryptochrome is one of the photoreceptors mediating phototropism in plants. PMID:12857830 phototropins and cryptochromes function together to enhance phototropism under low fluence rates PMID:21514160 CRY2 undergoes blue light-dependent physical interaction with SPA1. PMID:24130508 CIB1 (CRY2-interacting bHLH 1) specifically interacts with CRY2 in response to blue light to activate the transcription of FT PMID:24780222 Upon illumination, CRY2 is photoactivated to contact and associate with CIB1. PMID:23511208 reducing the fluence rate of either light quality or mutating the phy or cry photoreceptors lengthens the circadian period |
| GO:0009637 response to blue light | IDA PMID:24130508 Multiple bHLH proteins form heterodimers to mediate CRY2-dep... | ACCEPT | Summary: Core biological process: CRY2 mediates blue-light responses. Reason: Multiple genetic, biochemical, and cell biological studies support CRY2 as a blue-light photoreceptor controlling phototropism, flowering, clock, and growth outputs. Supporting Evidence: PMID:9565033 cryptochrome is one of the photoreceptors mediating phototropism in plants. PMID:12857830 phototropins and cryptochromes function together to enhance phototropism under low fluence rates PMID:21514160 CRY2 undergoes blue light-dependent physical interaction with SPA1. PMID:24130508 CIB1 (CRY2-interacting bHLH 1) specifically interacts with CRY2 in response to blue light to activate the transcription of FT PMID:24780222 Upon illumination, CRY2 is photoactivated to contact and associate with CIB1. PMID:23511208 reducing the fluence rate of either light quality or mutating the phy or cry photoreceptors lengthens the circadian period |
| GO:0009637 response to blue light | IDA PMID:24780222 Quantitative real-time kinetics of optogenetic proteins CRY2... | ACCEPT | Summary: Core biological process: CRY2 mediates blue-light responses. Reason: Multiple genetic, biochemical, and cell biological studies support CRY2 as a blue-light photoreceptor controlling phototropism, flowering, clock, and growth outputs. Supporting Evidence: PMID:9565033 cryptochrome is one of the photoreceptors mediating phototropism in plants. PMID:12857830 phototropins and cryptochromes function together to enhance phototropism under low fluence rates PMID:21514160 CRY2 undergoes blue light-dependent physical interaction with SPA1. PMID:24130508 CIB1 (CRY2-interacting bHLH 1) specifically interacts with CRY2 in response to blue light to activate the transcription of FT PMID:24780222 Upon illumination, CRY2 is photoactivated to contact and associate with CIB1. PMID:23511208 reducing the fluence rate of either light quality or mutating the phy or cry photoreceptors lengthens the circadian period |
| GO:0009638 phototropism | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: CRY2 contributes to phototropism with phototropins, but this is a downstream response. Reason: Cryptochromes modulate phototropism depending on blue-light fluence; the core CRY2 role is light perception/signaling rather than tropic growth execution. Supporting Evidence: PMID:9565033 cryptochrome is one of the photoreceptors mediating phototropism in plants. PMID:12857830 phototropins and cryptochromes function together to enhance phototropism under low fluence rates |
| GO:0009638 phototropism | IMP PMID:12857830 Second positive phototropism results from coordinated co-act... | KEEP AS NON CORE | Summary: CRY2 contributes to phototropism with phototropins, but this is a downstream response. Reason: Cryptochromes modulate phototropism depending on blue-light fluence; the core CRY2 role is light perception/signaling rather than tropic growth execution. Supporting Evidence: PMID:9565033 cryptochrome is one of the photoreceptors mediating phototropism in plants. PMID:12857830 phototropins and cryptochromes function together to enhance phototropism under low fluence rates |
| GO:0009646 response to absence of light | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Darkness affects CRY2 abundance and signaling state, but this is not a core process annotation. Reason: CRY2 expression/protein stability changes in darkness and light; the underlying core function is blue-light photoreception and light-regulated signaling. Supporting Evidence: PMID:11743105 Photoreceptors, phytochromes, and cryptochromes are involved in setting the clock by transducing the light signal to the central oscillator. PMID:20624951 The blue-light photoreceptors, cryptochrome (CRY) 2 and phototropin (PHOT) 2, are required for the stability of the R protein HRT |
| GO:0009646 response to absence of light | IEP PMID:11743105 Circadian clock-regulated expression of phytochrome and cryp... | KEEP AS NON CORE | Summary: Darkness affects CRY2 abundance and signaling state, but this is not a core process annotation. Reason: CRY2 expression/protein stability changes in darkness and light; the underlying core function is blue-light photoreception and light-regulated signaling. Supporting Evidence: PMID:11743105 Photoreceptors, phytochromes, and cryptochromes are involved in setting the clock by transducing the light signal to the central oscillator. PMID:20624951 The blue-light photoreceptors, cryptochrome (CRY) 2 and phototropin (PHOT) 2, are required for the stability of the R protein HRT |
| GO:0009646 response to absence of light | IEP PMID:20624951 Cryptochrome 2 and phototropin 2 regulate resistance protein... | KEEP AS NON CORE | Summary: Darkness affects CRY2 abundance and signaling state, but this is not a core process annotation. Reason: CRY2 expression/protein stability changes in darkness and light; the underlying core function is blue-light photoreception and light-regulated signaling. Supporting Evidence: PMID:11743105 Photoreceptors, phytochromes, and cryptochromes are involved in setting the clock by transducing the light signal to the central oscillator. PMID:20624951 The blue-light photoreceptors, cryptochrome (CRY) 2 and phototropin (PHOT) 2, are required for the stability of the R protein HRT |
| GO:0009785 blue light signaling pathway | IEA GO_REF:0000002 | ACCEPT | Summary: Core pathway annotation: CRY2 is a blue-light signaling photoreceptor. Reason: CRY2 photoactivation, homodimerization, photobody formation, and interaction with signaling partners such as BIC1, SPA1, and CIBs are central to blue-light signaling. Supporting Evidence: PMID:27846570 Arabidopsis cryptochrome 2 (CRY2) undergoes blue light-dependent homodimerization to become physiologically active. PMID:21514160 CRY2 undergoes blue light-dependent physical interaction with SPA1. PMID:24130508 CIB1 (CRY2-interacting bHLH 1) specifically interacts with CRY2 in response to blue light to activate the transcription of FT |
| GO:0009785 blue light signaling pathway | IEA GO_REF:0000117 | ACCEPT | Summary: Core pathway annotation: CRY2 is a blue-light signaling photoreceptor. Reason: CRY2 photoactivation, homodimerization, photobody formation, and interaction with signaling partners such as BIC1, SPA1, and CIBs are central to blue-light signaling. Supporting Evidence: PMID:27846570 Arabidopsis cryptochrome 2 (CRY2) undergoes blue light-dependent homodimerization to become physiologically active. PMID:21514160 CRY2 undergoes blue light-dependent physical interaction with SPA1. PMID:24130508 CIB1 (CRY2-interacting bHLH 1) specifically interacts with CRY2 in response to blue light to activate the transcription of FT |
| GO:0009791 post-embryonic development | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: Too broad; CRY2 affects several post-embryonic traits through light signaling. Reason: Post-embryonic development is a broad phenotypic umbrella. More specific CRY2 annotations to blue-light signaling, flowering, phototropism, and low-blue-light growth are preferable. Supporting Evidence: file:ARATH/CRY2/CRY2-uniprot.txt Photoreceptor that mediates primarily blue light inhibition of hypocotyl elongation and photoperiodic control of floral initiation |
| GO:0010075 regulation of meristem growth | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Supported light-dependent shoot apex/meristem phenotype, not core photoreceptor function. Reason: CRY2 affects meristem/cell-cycle programs downstream of light perception, but its core role remains blue-light photoreceptor signaling. Supporting Evidence: file:ARATH/CRY2/CRY2-uniprot.txt Photoreceptor that mediates primarily blue light inhibition of hypocotyl elongation and photoperiodic control of floral initiation |
| GO:0010118 stomatal movement | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Supported stomatal output of CRY signaling. Reason: CRY2 participates with CRY1/PHOT/COP1 pathways in blue-light-induced stomatal opening, but stomatal movement is a downstream physiological response. Supporting Evidence: PMID:16093319 CRY functions additively with PHOT in mediating blue light-induced stomatal opening |
| GO:0010244 response to low fluence blue light stimulus by blue low-fluence system | IEA GO_REF:0000117 | ACCEPT | Summary: CRY2 is important for limiting/low-blue-light growth responses. Reason: CRY1/CRY2 perceive reduced blue light and directly contact PIF4/PIF5 to control growth under limiting blue light. Supporting Evidence: PMID:26724867 CRY1 and CRY2 perceive this change and respond by directly contacting two bHLH transcription factors, PIF4 and PIF5. PMID:19558423 Differential petiole growth in Arabidopsis thaliana: photocontrol and hormonal regulation. |
| GO:0010244 response to low fluence blue light stimulus by blue low-fluence system | IMP PMID:19558423 Differential petiole growth in Arabidopsis thaliana: photoco... | ACCEPT | Summary: CRY2 is important for limiting/low-blue-light growth responses. Reason: CRY1/CRY2 perceive reduced blue light and directly contact PIF4/PIF5 to control growth under limiting blue light. Supporting Evidence: PMID:26724867 CRY1 and CRY2 perceive this change and respond by directly contacting two bHLH transcription factors, PIF4 and PIF5. PMID:19558423 Differential petiole growth in Arabidopsis thaliana: photocontrol and hormonal regulation. |
| GO:0010244 response to low fluence blue light stimulus by blue low-fluence system | IEP PMID:26724867 Cryptochromes Interact Directly with PIFs to Control Plant G... | ACCEPT | Summary: CRY2 is important for limiting/low-blue-light growth responses. Reason: CRY1/CRY2 perceive reduced blue light and directly contact PIF4/PIF5 to control growth under limiting blue light. Supporting Evidence: PMID:26724867 CRY1 and CRY2 perceive this change and respond by directly contacting two bHLH transcription factors, PIF4 and PIF5. |
| GO:0010617 circadian regulation of calcium ion oscillation | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Circadian calcium oscillation is a downstream clock/light-signaling phenotype. Reason: The evidence links cryptochrome light input to clock-regulated calcium rhythms; this is not the primary molecular function of CRY2. Supporting Evidence: PMID:11743105 Photoreceptors, phytochromes, and cryptochromes are involved in setting the clock by transducing the light signal to the central oscillator. |
| GO:0032922 circadian regulation of gene expression | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Phylogenetic circadian gene-expression annotation is plausible but not the main plant CRY2 function. Reason: Cryptochromes are light inputs to clock gene expression, but Arabidopsis CRY2 is primarily a blue-light signaling photoreceptor for flowering and growth responses. Supporting Evidence: PMID:23511208 reducing the fluence rate of either light quality or mutating the phy or cry photoreceptors lengthens the circadian period |
| GO:0042752 regulation of circadian rhythm | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Supported CRY contribution to clock period/rhythmicity, not core CRY2 function. Reason: CRY signaling affects circadian period and temperature/light input balance, but this is a downstream regulatory output of photoreceptor signaling. Supporting Evidence: PMID:23511208 reducing the fluence rate of either light quality or mutating the phy or cry photoreceptors lengthens the circadian period |
| GO:0042752 regulation of circadian rhythm | IMP PMID:23511208 Network balance via CRY signalling controls the Arabidopsis ... | KEEP AS NON CORE | Summary: Supported CRY contribution to clock period/rhythmicity, not core CRY2 function. Reason: CRY signaling affects circadian period and temperature/light input balance, but this is a downstream regulatory output of photoreceptor signaling. Supporting Evidence: PMID:23511208 reducing the fluence rate of either light quality or mutating the phy or cry photoreceptors lengthens the circadian period |
| GO:0043153 entrainment of circadian clock by photoperiod | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Photoperiodic clock entrainment is a plausible cryptochrome output, not core molecular activity. Reason: Cryptochromes are light inputs to clock entrainment, but the annotation is phylogenetically inferred and broader than the experimentally established CRY2 photoreceptor mechanism. Supporting Evidence: PMID:11743105 Photoreceptors, phytochromes, and cryptochromes are involved in setting the clock by transducing the light signal to the central oscillator. |
| GO:0048574 long-day photoperiodism, flowering | IMP PMID:21296763 Double loss-of-function mutation in EARLY FLOWERING 3 and CR... | ACCEPT | Summary: CRY2 promotes flowering under photoperiodic/continuous-light contexts. Reason: Loss and rescue experiments support CRY2 promotion of flowering through FT and photoperiodic signaling pathways. Supporting Evidence: PMID:21296763 an important role for Arabidopsis CRY2 to accelerate flowering time in continuous light. PMID:17259260 cry2-GFP expressed in vascular bundles increased FT expression only in vascular bundles. |
| GO:0048580 regulation of post-embryonic development | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: Overly broad developmental-process annotation. Reason: CRY2 regulates specific light-responsive developmental outputs; broad regulation of post-embryonic development is less informative than blue-light signaling and flowering terms. Supporting Evidence: file:ARATH/CRY2/CRY2-uniprot.txt Photoreceptor that mediates primarily blue light inhibition of hypocotyl elongation and photoperiodic control of floral initiation |
| GO:0048731 system development | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: Overly broad system-development annotation. Reason: System development does not capture the CRY2 mechanism and should not be used when specific light signaling and flowering annotations are available. Supporting Evidence: file:ARATH/CRY2/CRY2-uniprot.txt Photoreceptor that mediates primarily blue light inhibition of hypocotyl elongation and photoperiodic control of floral initiation |
| GO:0051607 defense response to virus | IMP PMID:20624951 Cryptochrome 2 and phototropin 2 regulate resistance protein... | KEEP AS NON CORE | Summary: Supported antiviral-defense output of CRY2/PHOT2 regulation of HRT stability. Reason: CRY2 contributes to R-protein-mediated viral defense via COP1/HRT stability, but this is a specialized downstream output rather than the conserved core photoreceptor function. Supporting Evidence: PMID:20624951 The blue-light photoreceptors, cryptochrome (CRY) 2 and phototropin (PHOT) 2, are required for the stability of the R protein HRT |
| GO:0072387 flavin adenine dinucleotide metabolic process | IEA GO_REF:0000117 | MODIFY | Summary: FAD is the CRY2 chromophore, but CRY2 is not an FAD metabolic enzyme. Reason: The evidence concerns FAD redox photochemistry and light sensitivity, not FAD biosynthesis, catabolism, or metabolism. Replace with FAD binding and blue-light photoreceptor activity. Proposed replacements: FAD binding blue light photoreceptor activity Supporting Evidence: PMID:25428980 Cellular metabolites enhance the light sensitivity of Arabidopsis cryptochrome through alternate electron transfer pathways. file:ARATH/CRY2/CRY2-uniprot.txt Binds 1 FAD per subunit. |
| GO:0072387 flavin adenine dinucleotide metabolic process | IMP PMID:25428980 Cellular metabolites enhance the light sensitivity of Arabid... | MODIFY | Summary: FAD is the CRY2 chromophore, but CRY2 is not an FAD metabolic enzyme. Reason: The evidence concerns FAD redox photochemistry and light sensitivity, not FAD biosynthesis, catabolism, or metabolism. Replace with FAD binding and blue-light photoreceptor activity. Proposed replacements: FAD binding blue light photoreceptor activity Supporting Evidence: PMID:25428980 Cellular metabolites enhance the light sensitivity of Arabidopsis cryptochrome through alternate electron transfer pathways. file:ARATH/CRY2/CRY2-uniprot.txt Binds 1 FAD per subunit. |
| GO:1901371 regulation of leaf morphogenesis | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Leaf/petiole morphogenesis is a low-blue-light growth output. Reason: CRY2 affects petiole/leaf morphogenesis through light and hormone-regulated growth responses, but this is downstream of photoreceptor signaling. Supporting Evidence: PMID:19558423 Differential petiole growth in Arabidopsis thaliana: photocontrol and hormonal regulation. |
| GO:1901371 regulation of leaf morphogenesis | IMP PMID:19558423 Differential petiole growth in Arabidopsis thaliana: photoco... | KEEP AS NON CORE | Summary: Leaf/petiole morphogenesis is a low-blue-light growth output. Reason: CRY2 affects petiole/leaf morphogenesis through light and hormone-regulated growth responses, but this is downstream of photoreceptor signaling. Supporting Evidence: PMID:19558423 Differential petiole growth in Arabidopsis thaliana: photocontrol and hormonal regulation. |
| GO:1902347 response to strigolactone | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Strigolactone response is a hormone/light crosstalk phenotype. Reason: The strigolactone annotation reflects hypocotyl-growth crosstalk with photoreceptor pathways; it is not a core CRY2 molecular function. Supporting Evidence: PMID:24126495 Strigolactone-regulated hypocotyl elongation is dependent on cryptochrome and phytochrome signaling pathways in Arabidopsis. |
| GO:1902347 response to strigolactone | IMP PMID:24126495 Strigolactone-regulated hypocotyl elongation is dependent on... | KEEP AS NON CORE | Summary: Strigolactone response is a hormone/light crosstalk phenotype. Reason: The strigolactone annotation reflects hypocotyl-growth crosstalk with photoreceptor pathways; it is not a core CRY2 molecular function. Supporting Evidence: PMID:24126495 Strigolactone-regulated hypocotyl elongation is dependent on cryptochrome and phytochrome signaling pathways in Arabidopsis. |
| GO:2000028 regulation of photoperiodism, flowering | IDA PMID:21514160 Blue light-dependent interaction of CRY2 with SPA1 regulates... | ACCEPT | Summary: CRY2 regulates photoperiodic flowering via SPA1/COP1/CO/FT signaling. Reason: Blue-light-dependent CRY2-SPA1 interaction suppresses COP1-dependent CO degradation and promotes FT expression and floral initiation. Supporting Evidence: PMID:21514160 SPA1 acts as a signaling molecule to mediate CRY2-dependent control of CO protein stability, FT transcription, and floral initiation in response to blue light. PMID:21514160 CRY2 undergoes blue light-dependent physical interaction with SPA1. |
| GO:2000377 regulation of reactive oxygen species metabolic process | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ROS regulation is a reported CRY2 signaling output, not the central function. Reason: CRY2 may promote blue-light-dependent ROS formation, but this is downstream of photoreceptor activation and remains less central than blue-light signaling/flowering. Supporting Evidence: PMID:26179959 Blue-light dependent ROS formation by Arabidopsis cryptochrome-2 may contribute toward its signaling role. |
| GO:2000379 positive regulation of reactive oxygen species metabolic process | IDA PMID:26179959 Blue-light dependent ROS formation by Arabidopsis cryptochro... | KEEP AS NON CORE | Summary: Positive ROS regulation is supported but non-core. Reason: Blue-light-dependent ROS formation may contribute to CRY2 signaling, but it is not the primary molecular function of CRY2. Supporting Evidence: PMID:26179959 Blue-light dependent ROS formation by Arabidopsis cryptochrome-2 may contribute toward its signaling role. |
| GO:0000325 plant-type vacuole | HDA PMID:15539469 The vegetative vacuole proteome of Arabidopsis thaliana reve... | REMOVE | Summary: High-throughput vacuole localization conflicts with the established nuclear photoreceptor localization. Reason: CRY2 is repeatedly localized to the nucleus and nuclear bodies, with only limited/transient cytosolic evidence. A single HDA vacuole proteomics annotation is likely incidental contamination or overinterpretation. Supporting Evidence: PMID:10476076 CRY2 is localized in the nucleus and that nuclear localization is mediated by the C-terminal region of CRY2. PMID:22311776 CRY2 is a constitutive nuclear protein that undergoes blue-light-dependent phosphorylation, ubiquitination, photobody formation, and degradation in the nucleus |
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: Correct cellular component: CRY2 acts predominantly in the nucleus. Reason: CRY2 nuclear localization is supported by direct localization experiments and by multiple studies of nuclear partner interactions, phosphorylation, photobody formation, and transcriptional outputs. Supporting Evidence: PMID:10476076 CRY2 is localized in the nucleus and that nuclear localization is mediated by the C-terminal region of CRY2. PMID:17438275 These CRY2 fusion proteins were all found in the nucleus PMID:22311776 CRY2 is a constitutive nuclear protein that undergoes blue-light-dependent phosphorylation, ubiquitination, photobody formation, and degradation in the nucleus PMID:25792146 all CRY2 mutant proteins examined located in the nucleus of Arabidopsis cells as the endogenous CRY2 or the wild-type GFP-CRY2 PMID:26724867 CRY2 likely localizes to chromatin indirectly, via associations with PIFs or other TFs |
| GO:0005634 nucleus | ISM GO_REF:0000122 | ACCEPT | Summary: Correct cellular component: CRY2 acts predominantly in the nucleus. Reason: CRY2 nuclear localization is supported by direct localization experiments and by multiple studies of nuclear partner interactions, phosphorylation, photobody formation, and transcriptional outputs. Supporting Evidence: PMID:10476076 CRY2 is localized in the nucleus and that nuclear localization is mediated by the C-terminal region of CRY2. PMID:17438275 These CRY2 fusion proteins were all found in the nucleus PMID:22311776 CRY2 is a constitutive nuclear protein that undergoes blue-light-dependent phosphorylation, ubiquitination, photobody formation, and degradation in the nucleus PMID:25792146 all CRY2 mutant proteins examined located in the nucleus of Arabidopsis cells as the endogenous CRY2 or the wild-type GFP-CRY2 PMID:26724867 CRY2 likely localizes to chromatin indirectly, via associations with PIFs or other TFs |
| GO:0005634 nucleus | IDA PMID:10476076 Nuclear localization of the Arabidopsis blue light receptor ... | ACCEPT | Summary: Correct cellular component: CRY2 acts predominantly in the nucleus. Reason: CRY2 nuclear localization is supported by direct localization experiments and by multiple studies of nuclear partner interactions, phosphorylation, photobody formation, and transcriptional outputs. Supporting Evidence: PMID:10476076 CRY2 is localized in the nucleus and that nuclear localization is mediated by the C-terminal region of CRY2. PMID:17438275 These CRY2 fusion proteins were all found in the nucleus PMID:22311776 CRY2 is a constitutive nuclear protein that undergoes blue-light-dependent phosphorylation, ubiquitination, photobody formation, and degradation in the nucleus PMID:25792146 all CRY2 mutant proteins examined located in the nucleus of Arabidopsis cells as the endogenous CRY2 or the wild-type GFP-CRY2 PMID:26724867 CRY2 likely localizes to chromatin indirectly, via associations with PIFs or other TFs |
| GO:0005634 nucleus | EXP PMID:17438275 Derepression of the NC80 motif is critical for the photoacti... | ACCEPT | Summary: Correct cellular component: CRY2 acts predominantly in the nucleus. Reason: CRY2 nuclear localization is supported by direct localization experiments and by multiple studies of nuclear partner interactions, phosphorylation, photobody formation, and transcriptional outputs. Supporting Evidence: PMID:10476076 CRY2 is localized in the nucleus and that nuclear localization is mediated by the C-terminal region of CRY2. PMID:17438275 These CRY2 fusion proteins were all found in the nucleus PMID:22311776 CRY2 is a constitutive nuclear protein that undergoes blue-light-dependent phosphorylation, ubiquitination, photobody formation, and degradation in the nucleus PMID:25792146 all CRY2 mutant proteins examined located in the nucleus of Arabidopsis cells as the endogenous CRY2 or the wild-type GFP-CRY2 PMID:26724867 CRY2 likely localizes to chromatin indirectly, via associations with PIFs or other TFs |
| GO:0005634 nucleus | IDA PMID:18988809 Photoexcited CRY2 interacts with CIB1 to regulate transcript... | ACCEPT | Summary: Correct cellular component: CRY2 acts predominantly in the nucleus. Reason: CRY2 nuclear localization is supported by direct localization experiments and by multiple studies of nuclear partner interactions, phosphorylation, photobody formation, and transcriptional outputs. Supporting Evidence: PMID:18988809 CIB1 interacts with CRY2 (cryptochrome 2) in a blue light-specific manner in yeast and Arabidopsis cells PMID:10476076 CRY2 is localized in the nucleus and that nuclear localization is mediated by the C-terminal region of CRY2. PMID:17438275 These CRY2 fusion proteins were all found in the nucleus PMID:22311776 CRY2 is a constitutive nuclear protein that undergoes blue-light-dependent phosphorylation, ubiquitination, photobody formation, and degradation in the nucleus PMID:25792146 all CRY2 mutant proteins examined located in the nucleus of Arabidopsis cells as the endogenous CRY2 or the wild-type GFP-CRY2 PMID:26724867 CRY2 likely localizes to chromatin indirectly, via associations with PIFs or other TFs |
| GO:0005634 nucleus | EXP PMID:20624951 Cryptochrome 2 and phototropin 2 regulate resistance protein... | ACCEPT | Summary: Correct cellular component: CRY2 acts predominantly in the nucleus. Reason: CRY2 nuclear localization is supported by direct localization experiments and by multiple studies of nuclear partner interactions, phosphorylation, photobody formation, and transcriptional outputs. Supporting Evidence: PMID:20624951 The blue-light photoreceptors, cryptochrome (CRY) 2 and phototropin (PHOT) 2, are required for the stability of the R protein HRT PMID:10476076 CRY2 is localized in the nucleus and that nuclear localization is mediated by the C-terminal region of CRY2. PMID:17438275 These CRY2 fusion proteins were all found in the nucleus PMID:22311776 CRY2 is a constitutive nuclear protein that undergoes blue-light-dependent phosphorylation, ubiquitination, photobody formation, and degradation in the nucleus PMID:25792146 all CRY2 mutant proteins examined located in the nucleus of Arabidopsis cells as the endogenous CRY2 or the wild-type GFP-CRY2 PMID:26724867 CRY2 likely localizes to chromatin indirectly, via associations with PIFs or other TFs |
| GO:0005634 nucleus | EXP PMID:22311776 A study of the blue-light-dependent phosphorylation, degrada... | ACCEPT | Summary: Correct cellular component: CRY2 acts predominantly in the nucleus. Reason: CRY2 nuclear localization is supported by direct localization experiments and by multiple studies of nuclear partner interactions, phosphorylation, photobody formation, and transcriptional outputs. Supporting Evidence: PMID:10476076 CRY2 is localized in the nucleus and that nuclear localization is mediated by the C-terminal region of CRY2. PMID:17438275 These CRY2 fusion proteins were all found in the nucleus PMID:22311776 CRY2 is a constitutive nuclear protein that undergoes blue-light-dependent phosphorylation, ubiquitination, photobody formation, and degradation in the nucleus PMID:25792146 all CRY2 mutant proteins examined located in the nucleus of Arabidopsis cells as the endogenous CRY2 or the wild-type GFP-CRY2 PMID:26724867 CRY2 likely localizes to chromatin indirectly, via associations with PIFs or other TFs |
| GO:0005634 nucleus | IDA PMID:22739826 Degradation of Arabidopsis CRY2 is regulated by SPA proteins... | ACCEPT | Summary: Correct cellular component: CRY2 acts predominantly in the nucleus. Reason: CRY2 nuclear localization is supported by direct localization experiments and by multiple studies of nuclear partner interactions, phosphorylation, photobody formation, and transcriptional outputs. Supporting Evidence: PMID:22739826 Degradation of Arabidopsis CRY2 is regulated by SPA proteins and phytochrome A. PMID:10476076 CRY2 is localized in the nucleus and that nuclear localization is mediated by the C-terminal region of CRY2. PMID:17438275 These CRY2 fusion proteins were all found in the nucleus PMID:22311776 CRY2 is a constitutive nuclear protein that undergoes blue-light-dependent phosphorylation, ubiquitination, photobody formation, and degradation in the nucleus PMID:25792146 all CRY2 mutant proteins examined located in the nucleus of Arabidopsis cells as the endogenous CRY2 or the wild-type GFP-CRY2 PMID:26724867 CRY2 likely localizes to chromatin indirectly, via associations with PIFs or other TFs |
| GO:0005634 nucleus | IDA PMID:25792146 The blue light-dependent phosphorylation of the CCE domain d... | ACCEPT | Summary: Correct cellular component: CRY2 acts predominantly in the nucleus. Reason: CRY2 nuclear localization is supported by direct localization experiments and by multiple studies of nuclear partner interactions, phosphorylation, photobody formation, and transcriptional outputs. Supporting Evidence: PMID:10476076 CRY2 is localized in the nucleus and that nuclear localization is mediated by the C-terminal region of CRY2. PMID:17438275 These CRY2 fusion proteins were all found in the nucleus PMID:22311776 CRY2 is a constitutive nuclear protein that undergoes blue-light-dependent phosphorylation, ubiquitination, photobody formation, and degradation in the nucleus PMID:25792146 all CRY2 mutant proteins examined located in the nucleus of Arabidopsis cells as the endogenous CRY2 or the wild-type GFP-CRY2 PMID:26724867 CRY2 likely localizes to chromatin indirectly, via associations with PIFs or other TFs |
| GO:0005634 nucleus | IDA PMID:26179959 Blue-light dependent ROS formation by Arabidopsis cryptochro... | ACCEPT | Summary: Correct cellular component: CRY2 acts predominantly in the nucleus. Reason: CRY2 nuclear localization is supported by direct localization experiments and by multiple studies of nuclear partner interactions, phosphorylation, photobody formation, and transcriptional outputs. Supporting Evidence: PMID:26179959 Blue-light dependent ROS formation by Arabidopsis cryptochrome-2 may contribute toward its signaling role. PMID:10476076 CRY2 is localized in the nucleus and that nuclear localization is mediated by the C-terminal region of CRY2. PMID:17438275 These CRY2 fusion proteins were all found in the nucleus PMID:22311776 CRY2 is a constitutive nuclear protein that undergoes blue-light-dependent phosphorylation, ubiquitination, photobody formation, and degradation in the nucleus PMID:25792146 all CRY2 mutant proteins examined located in the nucleus of Arabidopsis cells as the endogenous CRY2 or the wild-type GFP-CRY2 PMID:26724867 CRY2 likely localizes to chromatin indirectly, via associations with PIFs or other TFs |
| GO:0005634 nucleus | IDA PMID:26724867 Cryptochromes Interact Directly with PIFs to Control Plant G... | ACCEPT | Summary: Correct cellular component: CRY2 acts predominantly in the nucleus. Reason: CRY2 nuclear localization is supported by direct localization experiments and by multiple studies of nuclear partner interactions, phosphorylation, photobody formation, and transcriptional outputs. Supporting Evidence: PMID:10476076 CRY2 is localized in the nucleus and that nuclear localization is mediated by the C-terminal region of CRY2. PMID:17438275 These CRY2 fusion proteins were all found in the nucleus PMID:22311776 CRY2 is a constitutive nuclear protein that undergoes blue-light-dependent phosphorylation, ubiquitination, photobody formation, and degradation in the nucleus PMID:25792146 all CRY2 mutant proteins examined located in the nucleus of Arabidopsis cells as the endogenous CRY2 or the wild-type GFP-CRY2 PMID:26724867 CRY2 likely localizes to chromatin indirectly, via associations with PIFs or other TFs |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Cytoplasmic CRY2 can be detected/translocate, but the principal signaling site is nuclear. Reason: CRY2 may be present in the cytoplasm in some contexts, yet the core photoreceptor signaling annotations are best assigned to nucleus/nuclear body. Supporting Evidence: PMID:26179959 Blue-light dependent ROS formation by Arabidopsis cryptochrome-2 may contribute toward its signaling role. PMID:10476076 CRY2 is localized in the nucleus and that nuclear localization is mediated by the C-terminal region of CRY2. |
| GO:0005737 cytoplasm | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Cytoplasmic CRY2 can be detected/translocate, but the principal signaling site is nuclear. Reason: CRY2 may be present in the cytoplasm in some contexts, yet the core photoreceptor signaling annotations are best assigned to nucleus/nuclear body. Supporting Evidence: PMID:26179959 Blue-light dependent ROS formation by Arabidopsis cryptochrome-2 may contribute toward its signaling role. PMID:10476076 CRY2 is localized in the nucleus and that nuclear localization is mediated by the C-terminal region of CRY2. |
| GO:0005737 cytoplasm | IDA PMID:26179959 Blue-light dependent ROS formation by Arabidopsis cryptochro... | KEEP AS NON CORE | Summary: Cytoplasmic CRY2 can be detected/translocate, but the principal signaling site is nuclear. Reason: CRY2 may be present in the cytoplasm in some contexts, yet the core photoreceptor signaling annotations are best assigned to nucleus/nuclear body. Supporting Evidence: PMID:26179959 Blue-light dependent ROS formation by Arabidopsis cryptochrome-2 may contribute toward its signaling role. PMID:10476076 CRY2 is localized in the nucleus and that nuclear localization is mediated by the C-terminal region of CRY2. |
| GO:0016604 nuclear body | IEA GO_REF:0000117 | ACCEPT | Summary: Correct cellular component: blue light induces CRY2-containing nuclear photobodies. Reason: CRY2 forms nuclear bodies/photobodies after blue-light activation, and these are linked to phosphorylation, degradation, signal amplification, and partner colocalization. Supporting Evidence: PMID:21514160 blue light enhances colocalization of the CRY2 and MycSPA1 proteins in the nuclear bodies PMID:22311776 CRY2 is a constitutive nuclear protein that undergoes blue-light-dependent phosphorylation, ubiquitination, photobody formation, and degradation in the nucleus PMID:27846570 BICs also inhibit the blue light-induced formation of CRY2 photobodies |
| GO:0016604 nuclear body | IDA PMID:21511872 Blue-light-dependent interaction of cryptochrome 1 with SPA1... | ACCEPT | Summary: Correct cellular component: blue light induces CRY2-containing nuclear photobodies. Reason: CRY2 forms nuclear bodies/photobodies after blue-light activation, and these are linked to phosphorylation, degradation, signal amplification, and partner colocalization. Supporting Evidence: PMID:21514160 blue light enhances colocalization of the CRY2 and MycSPA1 proteins in the nuclear bodies PMID:22311776 CRY2 is a constitutive nuclear protein that undergoes blue-light-dependent phosphorylation, ubiquitination, photobody formation, and degradation in the nucleus PMID:27846570 BICs also inhibit the blue light-induced formation of CRY2 photobodies |
| GO:0016604 nuclear body | IMP PMID:22311776 A study of the blue-light-dependent phosphorylation, degrada... | ACCEPT | Summary: Correct cellular component: blue light induces CRY2-containing nuclear photobodies. Reason: CRY2 forms nuclear bodies/photobodies after blue-light activation, and these are linked to phosphorylation, degradation, signal amplification, and partner colocalization. Supporting Evidence: PMID:21514160 blue light enhances colocalization of the CRY2 and MycSPA1 proteins in the nuclear bodies PMID:22311776 CRY2 is a constitutive nuclear protein that undergoes blue-light-dependent phosphorylation, ubiquitination, photobody formation, and degradation in the nucleus PMID:27846570 BICs also inhibit the blue light-induced formation of CRY2 photobodies |
| GO:0016605 PML body | IEA GO_REF:0000044 | MODIFY | Summary: PML body is not the right plant-specific term for CRY2 photobodies. Reason: The evidence supports nuclear photobodies/nuclear bodies in Arabidopsis. PML bodies are an inappropriate or over-specific mapping for this plant photoreceptor. Proposed replacements: nuclear body Supporting Evidence: PMID:21514160 blue light enhances colocalization of the CRY2 and MycSPA1 proteins in the nuclear bodies PMID:22311776 CRY2 is a constitutive nuclear protein that undergoes blue-light-dependent phosphorylation, ubiquitination, photobody formation, and degradation in the nucleus |
Loading supporting content…
Download this section (compressed HTML)Q: Should GO represent Arabidopsis CRY2 photobodies with a dedicated cryptochrome photobody cellular-component term rather than PML body or generic nuclear body?
Suggested experts: Lin C, Zuo Z, Yu X
Q: For CRY2-mediated chromatin compaction/decompaction annotations, should curation prefer downstream regulation terms over direct chromatin remodeling terminology?
Suggested experts: Tessadori F, van Zanten M
Experiment: Compare CRY2 photobody composition, light dependence, dynamics, and partner colocalization across PMID:21514160, PMID:22311776, PMID:27846570, and recent condensate studies; define term boundaries and synonym needs.
Hypothesis: CRY2 photobodies are distinct enough from generic nuclear bodies to warrant a GO cellular-component child term.
Type: curation/ontology review
Experiment: Measure chromatin compaction and floral-transition markers in cry2, CIB/SPAs, and photobody-defective CRY2 mutants under matched blue-light conditions, paired with CRY2 chromatin-proximity or CUT&Tag assays.
Hypothesis: CRY2 affects chromatin organization indirectly through photoreceptor signaling partners rather than by direct chromatin remodeling activity.
Type: targeted genetic and imaging assay
Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)