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STN8 phosphoproteome

Phosphorylation in Arabidopsis thaliana

2015 modifications in 1943 peptides, found in 2345 proteins

Experiment Details

Exp 38


Experimental Setup
TissueRosette wild-type and stn8
ConditionControl
PTM EnrichmentIMAC/TiO2
MS InstrumentLTQ
MS/MS Search Parameters
Protein DatabaseTAIR9 + contaminants
Decoy StrategyReverse decoy database
FDR ThresholdFDR 0.15% estimated
Search Algorithm(s) MASCOT version 2.2.04
Precursor Mass Tolerance10 ppm
Identification ScoreMASCOT Score
ProteaseTrypsin
Fixed ModificationsCarbamidomethyl (C)
Variable ModificationsOxidation (M)
Acetylation (K)
Acetylation (Protein N-term)
Phosphorylation (STY)
Other Information
CommentsPhosphat 4.0 - Defined sites (pS/T/Y).


Publication Information

Reiland et al., 2011

PubMed ID: 21768351

ProteomeXchange: PRD000308

Abstract

Proc Natl Acad Sci U S A. 2011 Aug 2;108(31):12955-60. doi: 
10.1073/pnas.1104734108. Epub 2011 Jul 18.

Comparative phosphoproteome profiling reveals a function of the STN8 kinase in 
fine-tuning of cyclic electron flow (CEF).

Reiland S(1), Finazzi G, Endler A, Willig A, Baerenfaller K, Grossmann J, 
Gerrits B, Rutishauser D, Gruissem W, Rochaix JD, Baginsky S.

Author information:
(1)Department of Biology, Eidgenössische Technische Hochschule Zurich, 8092 
Zurich, Switzerland.

Important aspects of photosynthetic electron transport efficiency in 
chloroplasts are controlled by protein phosphorylation. Two thylakoid-associated 
kinases, STN7 and STN8, have distinct roles in short- and long-term 
photosynthetic acclimation to changes in light quality and quantity. Although 
some substrates of STN7 and STN8 are known, the complexity of this regulatory 
kinase system implies that currently unknown substrates connect photosynthetic 
performance with the regulation of metabolic and regulatory functions. We 
performed an unbiased phosphoproteome-wide screen with Arabidopsis WT and stn8 
mutant plants to identify unique STN8 targets. The phosphorylation status of 
STN7 was not affected in stn8, indicating that kinases other than STN8 
phosphorylate STN7 under standard growth conditions. Among several putative STN8 
substrates, PGRL1-A is of particular importance because of its possible role in 
the modulation of cyclic electron transfer. The STN8 phosphorylation site on 
PGRL1-A is absent in both monocotyledonous plants and algae. In dicots, 
spectroscopic measurements with Arabidopsis WT, stn7, stn8, and stn7/stn8 
double-mutant plants indicate a STN8-mediated slowing down of the transition 
from cyclic to linear electron flow at the onset of illumination. This finding 
suggests a possible link between protein phosphorylation by STN8 and fine-tuning 
of cyclic electron flow during this critical step of photosynthesis, when the 
carbon assimilation is not commensurate to the electron flow capacity of the 
chloroplast.

DOI: 10.1073/pnas.1104734108
PMCID: PMC3150903
PMID: 21768351 [Indexed for MEDLINE]

Conflict of interest statement: The authors declare no conflict of interest.