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PXD014703 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleDifferential light-dependent phosphorylation of Ser and Thr residues regulates plant STN7 kinase
DescriptionSTN7 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.
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterAndrea Trotta
SpeciesList scientific name: Arabidopsis thaliana; NCBI TaxID: 3702;
ModificationListS-carboxamidomethyl-L-cysteine; O-phospho-L-serine; O-phospho-L-threonine
InstrumentTSQ Vantage
Dataset History
RevisionDatetimeStatusChangeLog Entry
02019-07-22 10:12:23ID requested
12019-08-13 15:25:59announced
Publication List
Trotta A, Suorsa M, Rantala M, Lundin B, Aro EM, 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. Plant J, 87(5):484-94(2016) [pubmed]
Keyword List
curator keyword: selected reaction monitoring, SRM, targeted
Contact List
Andrea Trotta
contact affiliationUniversity of Turku
contact emailandrea.trotta@utu.fi
dataset submitter
Eva-Mari Aro
contact affiliationUniversity of Turku
contact emailevaaro@utu.fi
lab head
Full Dataset Link List
PeptideAtlas dataset URI
PASSEL experiment URI
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