2022
DOI: 10.3389/fpls.2022.844714
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Signaling Mechanisms by Arabidopsis Cryptochromes

Abstract: Cryptochromes (CRYs) are blue light photoreceptors that regulate growth, development, and metabolism in plants. In Arabidopsis thaliana (Arabidopsis), CRY1 and CRY2 possess partially redundant and overlapping functions. Upon exposure to blue light, the monomeric inactive CRYs undergo phosphorylation and oligomerization, which are crucial to CRY function. Both the N- and C-terminal domains of CRYs participate in light-induced interaction with multiple signaling proteins. These include the COP1/SPA E3 ubiquitin … Show more

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Cited by 39 publications
(33 citation statements)
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References 158 publications
(251 reference statements)
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“…Hence, the WDrepeat domain of PpSPAa is both necessary and sufficient for the interaction with the CCE domain of PpCRY1b. Moreover, the results suggest that PpCRY1b, as it was proposed for Arabidopsis CRYs (Ponnu & Hoecker, 2022), exhibits a 'closed conformation' in darkness that is opened by blue light exposure, thereby exposing the CCE domain for PpCOP1/PpSPA interaction.…”
Section: Ppspaa and Ppcop1a Interact With The Cce Domain Of Ppcry1bmentioning
confidence: 58%
See 1 more Smart Citation
“…Hence, the WDrepeat domain of PpSPAa is both necessary and sufficient for the interaction with the CCE domain of PpCRY1b. Moreover, the results suggest that PpCRY1b, as it was proposed for Arabidopsis CRYs (Ponnu & Hoecker, 2022), exhibits a 'closed conformation' in darkness that is opened by blue light exposure, thereby exposing the CCE domain for PpCOP1/PpSPA interaction.…”
Section: Ppspaa and Ppcop1a Interact With The Cce Domain Of Ppcry1bmentioning
confidence: 58%
“…In that regard, PpCRY1 behaved similar to Arabidopsis CRY1 and differently from Arabidopsis CRY2. In angiosperms, cryptochromes underwent a gene duplication event resulting in CRY1 and CRY2 with partially overlapping but distinct functions in Arabidopsis (Deppisch et al., 2022; Lariguet & Dunand, 2005; Ponnu & Hoecker, 2022). Importantly, they differ in their interactions with the SPA proteins: although the CCE domain of CRY1 interacts with the WD‐repeat domain of SPA1, CRY2 interacts via its PHR domain with the kinase domain of SPA1 (Lian et al., 2011; Liu et al., 2011; Zuo et al., 2011).…”
Section: Discussionmentioning
confidence: 99%
“…This includes mitogen-activated protein kinase (MAPK) signaling ( Karia et al, 2021 ). The role of phosphorylation cascades during the interactions between photosynthesis and respiration, in particular, includes the participation of phytochrome and cryptochrome systems, in which the first step represents light-dependent phosphorylation of the protein moiety of phytochrome and cryptochrome ( Igamberdiev et al, 2014a , 2014b ; Ponnu and Hoecker, 2022 ).…”
Section: Multilevel Regulation Of Respiration In the Lightmentioning
confidence: 99%
“…The cryptochrome photolyase family (CPF) includes: DNA photolyases—enzymes that repair DNA damaged by UVB (280–320 nm) under the action of near UV and blue light (320–480 nm) [ 222 , 232 , 233 , 234 ] and cryptochromes—receptor proteins for near UV and blue light. Cryptochromes carry out photoregulation of transcription for various genes and also participate in circadian rhythms [ 232 , 234 , 235 ] and magnitoreception [ 236 ].…”
Section: Biochemical and Physiological Application Of Pterin Photoche...mentioning
confidence: 99%