期刊
PLANT JOURNAL
卷 87, 期 5, 页码 484-494出版社
WILEY-BLACKWELL
DOI: 10.1111/tpj.13213
关键词
Arabidopsis thaliana; light-harvesting complex; STN7; phosphoproteomics; selected reaction monitoring
资金
- Academy of Finland [272424, 271832, 273870]
- Doctoral Program in Molecular Life Sciences (DPMLS)
- Carl Tryggers Foundation
- Academy of Finland (AKA) [272424, 272424] Funding Source: Academy of Finland (AKA)
STN7 kinase catalyzes the phosphorylation of the globally most common membrane proteins, the light-harvesting complex II (LHCII) in plant chloroplasts. STN7 itself possesses one serine (Ser) and two threonine (Thr) phosphosites. We show that phosphorylation of the Thr residues protects STN7 against degradation in darkness, low light and red light, whereas increasing light intensity and far red illumination decrease phosphorylation and induce STN7 degradation. Ser phosphorylation, in turn, occurs under red and low intensity white light, coinciding with the client protein (LHCII) phosphorylation. Through analysis of the counteracting LHCII phosphatase mutant tap38/pph1, we show that Ser phosphorylation and activation of the STN7 kinase for subsequent LHCII phosphorylation are heavily affected by pre-illumination conditions. Transitions between the three activity states of the STN7 kinase (deactivated in darkness and far red light, activated in low and red light, inhibited in high light) are shown to modulate the phosphorylation of the STN7 Ser and Thr residues independently of each other. Such dynamic regulation of STN7 kinase phosphorylation is crucial for plant growth and environmental acclimation.
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