PXD014703
PXD014703 is an original dataset announced via ProteomeXchange.
Dataset Summary
Title | Differential light-dependent phosphorylation of Ser and Thr residues regulates plant STN7 kinase |
Description | 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. |
HostingRepository | PeptideAtlas |
AnnounceDate | 2019-08-13 |
AnnouncementXML | Submission_2019-08-13_15:25:58.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Supported dataset by repository |
PrimarySubmitter | Andrea Trotta |
SpeciesList | scientific name: Arabidopsis thaliana; NCBI TaxID: 3702; |
ModificationList | S-carboxamidomethyl-L-cysteine; O-phospho-L-serine; O-phospho-L-threonine |
Instrument | TSQ Vantage |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
---|---|---|---|
0 | 2019-07-22 10:12:23 | ID requested | |
⏵ 1 | 2019-08-13 15:25:59 | announced |
Publication List
Trotta A, Suorsa M, Rantala M, Lundin B, Aro EM, 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 affiliation | University of Turku |
contact email | andrea.trotta@utu.fi |
dataset submitter | |
Eva-Mari Aro | |
contact affiliation | University of Turku |
contact email | evaaro@utu.fi |
lab head |
Full Dataset Link List
PeptideAtlas dataset URI |
PASSEL experiment URI |
PASSEL transition group browser URI |