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A mutually assured destruction mechanism attenuates light signaling in Arabidopsis.


ABSTRACT: After light-induced nuclear translocation, phytochrome photoreceptors interact with and induce rapid phosphorylation and degradation of basic helix-loop-helix transcription factors, such as PHYTOCHROME-INTERACTING FACTOR 3 (PIF3), to regulate gene expression. Concomitantly, this interaction triggers feedback reduction of phytochrome B (phyB) levels. Light-induced phosphorylation of PIF3 is necessary for the degradation of both proteins. We report that this PIF3 phosphorylation induces, and is necessary for, recruitment of LRB [Light-Response Bric-a-Brack/Tramtrack/Broad (BTB)] E3 ubiquitin ligases to the PIF3-phyB complex. The recruited LRBs promote concurrent polyubiqutination and degradation of both PIF3 and phyB in vivo. These data reveal a linked signal-transmission and attenuation mechanism involving mutually assured destruction of the receptor and its immediate signaling partner.

SUBMITTER: Ni W 

PROVIDER: S-EPMC4414656 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature

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A mutually assured destruction mechanism attenuates light signaling in Arabidopsis.

Ni Weimin W   Xu Shou-Ling SL   Tepperman James M JM   Stanley David J DJ   Maltby Dave A DA   Gross John D JD   Burlingame Alma L AL   Wang Zhi-Yong ZY   Quail Peter H PH  

Science (New York, N.Y.) 20140601 6188


After light-induced nuclear translocation, phytochrome photoreceptors interact with and induce rapid phosphorylation and degradation of basic helix-loop-helix transcription factors, such as PHYTOCHROME-INTERACTING FACTOR 3 (PIF3), to regulate gene expression. Concomitantly, this interaction triggers feedback reduction of phytochrome B (phyB) levels. Light-induced phosphorylation of PIF3 is necessary for the degradation of both proteins. We report that this PIF3 phosphorylation induces, and is ne  ...[more]

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