Phosphorylation by CK2 Enhances the Rapid Light-induced Degradation of Phytochrome Interacting Factor 1 in Arabidopsis

Bu, Qingyun; Zhu, Ling; Dennis, Michael D.; Lu, Yu; Lu, Sheen X.; Person, Maria D.; Tobin, Elaine M.; Browning, Karen S.; Huq, Enamul

doi:10.1074/jbc.m110.186882

Cited by 89 publications

(105 citation statements)

References 53 publications

(110 reference statements)

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“…The light-induced degradation of PIFs is UPS-mediated and involves phosphorylation and polyubiquitylation of PIFs 16,17,20,23 . We examined whether the phosphorylation or ubiquitylation of PIF1 is affected in the cop1-4, spaQ and cul4cs seedlings.…”

Section: Cop1mentioning

confidence: 99%

“…The TAP-PIF1, TAP-SPA1, Flag-CUL4, TAP-SPA1/PIF1-HA and TAP-PIF1/COP1-HA transgenic plants have been previously described 6,7,20,29 . The PIF1-HA-pGWB14 plasmid was described 7 .…”

Section: T a P -P I F 1 / C O P 1 -H A T A P -P I F 1 T A P -P I F 1 mentioning

confidence: 99%

“…Two kinases have been shown to phosphorylate PIFs in vitro 19 . For example, CK2 was shown to phosphorylate PIF1 in vitro 20 . A mutant form of PIF1 deficient in CK2 phosphorylation sites displayed reduced degradation in response to light in vivo, suggesting CK2 promotes PIF1 degradation.…”

mentioning

confidence: 99%

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CUL4 forms an E3 ligase with COP1 and SPA to promote light-induced degradation of PIF1

et al. 2015

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Plants undergo contrasting developmental programs in dark and light. Photomorphogenesis, a light-adapted programme is repressed in the dark by the synergistic actions of CUL4 COP1-SPA E3 ubiquitin ligase and a subset of basic helix-loop-helix transcription factors called phytochrome interacting factors (PIFs). To promote photomorphogenesis, light activates the phytochrome family of sensory photoreceptors, which inhibits these repressors by poorly understood mechanisms. Here, we show that the CUL4 COP1-SPA E3 ubiquitin ligase is necessary for the light-induced degradation of PIF1 in Arabidopsis. The light-induced ubiquitylation and subsequent degradation of PIF1 is reduced in the cop1, spaQ and cul4 backgrounds. COP1, SPA1 and CUL4 preferentially form complexes with the phosphorylated forms of PIF1 in response to light. The cop1 and spaQ seeds display strong hyposensitive response to far-red light-mediated seed germination and light-regulated gene expression. These data show a mechanism by which an E3 ligase attenuates its activity by degrading its cofactor in response to light.

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Section: Cop1mentioning

confidence: 99%

“…The TAP-PIF1, TAP-SPA1, Flag-CUL4, TAP-SPA1/PIF1-HA and TAP-PIF1/COP1-HA transgenic plants have been previously described 6,7,20,29 . The PIF1-HA-pGWB14 plasmid was described 7 .…”

Section: T a P -P I F 1 / C O P 1 -H A T A P -P I F 1 T A P -P I F 1 mentioning

confidence: 99%

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CUL4 forms an E3 ligase with COP1 and SPA to promote light-induced degradation of PIF1

et al. 2015

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“…CK2 phosphorylates PIF1 (Bu et al, 2011b), while BIN2 phosphorylates PIF3 and PIF4 (Ling et al, 2017;Bernardo-García et al, 2014). However, these kinases are not necessary for the light-induced phosphorylation of PIFs in vivo.…”

Section: Kinases That Phosphorylate Pifsmentioning

confidence: 99%

Phytochromes and Phytochrome Interacting Factors

2017

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The basic helix-loop-helix domain-containing transcription factors that interact physically with the red and far-red light photoreceptors, phytochromes, are called PHYTOCHROME INTERACTING FACTORS (PIFs). In the last two decades, the phytochrome-PIF signaling module has been shown to be conserved from Physcomitrella patens to higher plants. Exciting recent studies highlight the discovery of at least four distinct kinases (PPKs, CK2, BIN2, and phytochrome itself) and four families of ubiquitin ligases (SCF EBF 1/2 , CUL3 LRB , CUL3 BOP , and CUL4 COP1-SPA ) that regulate PIF abundance both in dark and light conditions. This review discusses these recent discoveries with a focus on the central phytochrome signaling mechanisms that have a profound impact on plant growth and development in response to light.

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“…There is still no direct evidence showing that PIF3 degradation occurs on photobodies. Therefore, we cannot exclude the possibility that photobodies are only involved in a posttranslational modification of PIFs, such as phosphorylation (Al-Sady et al, 2006;Lorrain et al, 2008;Shen et al, 2008;Bu et al, 2011;Ni et al, 2013), and that PIF degradation occurs elsewhere . It is also important to note that although our data show a clear separation between PIF3 degradation and the regulation of its transcriptional activity in the R-FR-D transition (Fig.…”

Section: Photobody Localization Of Phyb Tightly Correlates With the Rmentioning

confidence: 99%

Photobody Localization of Phytochrome B Is Tightly Correlated with Prolonged and Light-Dependent Inhibition of Hypocotyl Elongation in the Dark

et al. 2014

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Photobody localization of Arabidopsis (Arabidopsis thaliana) phytochrome B (phyB) fused to green fluorescent protein (PBG) correlates closely with the photoinhibition of hypocotyl elongation. However, the amino-terminal half of phyB fused to green fluorescent protein (NGB) is hypersensitive to light despite its inability to localize to photobodies. Therefore, the significance of photobodies in regulating hypocotyl growth remains debatable. Accumulating evidence indicates that under diurnal conditions, photoactivated phyB persists into darkness to inhibit hypocotyl elongation. Here, we examine whether photobodies are involved in inhibiting hypocotyl growth in darkness by comparing the PBG and NGB lines after the red light-to-dark transition. Surprisingly, after the transition from 10 mmol m 22 s 21 red light to darkness, PBG inhibits hypocotyl elongation three times longer than NGB. The disassembly of photobodies in PBG hypocotyl nuclei correlates tightly with the accumulation of the growth-promoting transcription factor PHYTOCHROME-INTERACTING FACTOR3 (PIF3). Destabilizing photobodies by either decreasing the light intensity or adding monochromatic far-red light treatment before the light-to-dark transition leads to faster PIF3 accumulation and a dramatic reduction in the capacity for hypocotyl growth inhibition in PBG. In contrast, NGB is defective in PIF3 degradation, and its hypocotyl growth in the dark is nearly unresponsive to changes in light conditions. Together, our results support the model that photobodies are required for the prolonged, light-dependent inhibition of hypocotyl elongation in the dark by repressing PIF3 accumulation and by stabilizing the far-red light-absorbing form of phyB. Our study suggests that photobody localization patterns of phyB could serve as instructive cues that control light-dependent photomorphogenetic responses in the dark.

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Phosphorylation by CK2 Enhances the Rapid Light-induced Degradation of Phytochrome Interacting Factor 1 in Arabidopsis

Cited by 89 publications

References 53 publications

CUL4 forms an E3 ligase with COP1 and SPA to promote light-induced degradation of PIF1

CUL4 forms an E3 ligase with COP1 and SPA to promote light-induced degradation of PIF1

Phytochromes and Phytochrome Interacting Factors

Photobody Localization of Phytochrome B Is Tightly Correlated with Prolonged and Light-Dependent Inhibition of Hypocotyl Elongation in the Dark

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