Serine and threonine residues of plant STN7 kinase are differentially phosphorylated upon changing light conditions and specifically influence the activity and stability of the kinase - UTU Research Portal

A1 Refereed original research article in a scientific journal

Serine and threonine residues of plant STN7 kinase are differentially phosphorylated upon changing light conditions and specifically influence the activity and stability of the kinase

Authors: Trotta Andrea, Suorsa Marjaana, Rantala Marjaana, Lundin Björn, Aro Eva-Mari

Publisher: WILEY-BLACKWELL

Publication year: 2016

Journal: Plant Journal

Journal name in source: PLANT JOURNAL

Journal acronym: PLANT J

Volume: 87

Issue: 5

First page : 484

Last page: 494

Number of pages: 11

ISSN: 0960-7412

eISSN: 1365-313X

DOI: https://doi.org/10.1111/tpj.13213

Web address : http://onlinelibrary.wiley.com/doi/10.1111/tpj.13213/full

Self-archived copy’s web address: https://research.utu.fi/converis/portal/detail/Publication/18133624

Abstract

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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