A phyB-PIF1-SPA1 kinase regulatory complex promotes photomorphogenesis in Arabidopsis

Inyup Paik, Fulu Chen, Vinh Ngoc Pham, Ling Zhu, Jeong-Il Kim and Enamul Huq ()
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Inyup Paik: The University of Texas at Austin
Fulu Chen: The University of Texas at Austin
Vinh Ngoc Pham: The University of Texas at Austin
Ling Zhu: The University of Texas at Austin
Jeong-Il Kim: The University of Texas at Austin
Enamul Huq: The University of Texas at Austin

Nature Communications, 2019, vol. 10, issue 1, 1-17

Abstract: Abstract CONSTITUTIVELY PHOTOMORPHOGENIC1 (COP1) is a highly conserved E3 ubiquitin ligase from plants to animals and acts as a central repressor of photomorphogenesis in plants. SUPPRESSOR OF PHYA-105 1 family members (SPA1-SPA4) directly interact with COP1 and enhance COP1 activity. Despite the presence of a kinase domain at the N-terminus, no COP1-independent role of SPA proteins has been reported. Here we show that SPA1 acts as a serine/threonine kinase and directly phosphorylates PIF1 in vitro and in vivo. SPAs are necessary for the light-induced phosphorylation, ubiquitination and subsequent degradation of PIF1. Moreover, the red/far-red light photoreceptor phyB interacts with SPA1 through its C-terminus and enhances the recruitment of PIF1 for phosphorylation. These data provide a mechanistic view on how the COP1-SPA complexes serve as an example of a cognate kinase-E3 ligase complex that selectively triggers rapid phosphorylation and removal of its substrates, and how phyB modulates this process to promote photomorphogenesis.

Date: 2019
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DOI: 10.1038/s41467-019-12110-y

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