期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 286, 期 14, 页码 -出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110.186882
关键词
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资金
- National Institutes of Health [GM-23167]
- NIEHS National Institutes of Health [P30ES007784]
- Department of Energy [DE-FG02-04ER15575]
- National Science Foundation [MCB0214996, IOS-0822811, IOS-0849287]
- Welch Foundation [F1339]
- Direct For Biological Sciences
- Division Of Integrative Organismal Systems [0822811, 0849287] Funding Source: National Science Foundation
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1052530] Funding Source: National Science Foundation
The phytochrome family of sensory photoreceptors interacts with phytochrome interacting factors (PIFs), repressors of photomorphogenesis, in response to environmental light signals and induces rapid phosphorylation and degradation of PIFs to promote photomorphogenesis. However, the kinase that phosphorylates PIFs is still unknown. Here we show that CK2 directly phosphorylates PIF1 at multiple sites. alpha 1 and alpha 2 subunits individually phosphorylated PIF1 weakly in vitro. However, each of four beta subunits strongly stimulated phosphorylation of PIF1 by alpha 1 or alpha 2. Mapping of the phosphorylation sites identified seven Ser/Thr residues scattered throughout PIF1. Ser/Thr to Ala scanning mutations at all seven sites eliminated CK2-mediated phosphorylation of PIF1 in vitro. Moreover, the rate of degradation of the Ser/Thr to Ala mutant PIF1 was significantly reduced compared with wild-type PIF1 in transgenic plants. In addition, hypocotyl lengths of the mutant PIF1 transgenic plants were much longer than the wild-type PIF1 transgenic plants under light, suggesting that the mutant PIF1 is suppressing photomorphogenesis. Taken together, these data suggest that CK2-mediated phosphorylation enhances the light-induced degradation of PIF1 to promote photomorphogenesis.
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