PMID- 19253305
OWN - NLM
STAT- MEDLINE
DCOM- 20090429
LR  - 20151119
IS  - 1615-9861 (Electronic)
IS  - 1615-9853 (Linking)
VI  - 9
IP  - 6
DP  - 2009 Mar
TI  - Phosphoproteomic analysis of ethylene-regulated protein phosphorylation in 
      etiolated seedlings of Arabidopsis mutant ein2 using two-dimensional separations 
      coupled with a hybrid quadrupole time-of-flight mass spectrometer.
PG  - 1646-61
LID - 10.1002/pmic.200800420 [doi]
AB  - Ethylene regulates a variety of stress responses and developmental adaptation in 
      plants. In the present study, the phosphoproteomics is adopted to investigate the 
      differential protein phosphorylation by ethylene in Arabidopsis 
      ethylene-insensitive 2 (ein2) mutant. A total of 224 phosphopeptides were 
      identified, of which 64 phosphopeptides were detected three or more times. 
      Ethylene induces a general reduction in phosphorylated proteins in ein2. Totally, 
      three ethylene-enhanced and three ethylene-repressible unique phosphopeptides 
      were identified, respectively. Classification of the cellular functions of these 
      phosphoproteins revealed that 55.5% of them are related to signaling and gene 
      expression. Peptide sequence alignment reveals two highly conserved 
      phosphorylation motifs, PRVD/GSx and SPDYxx. Alignment of these phosphopeptides 
      with Arabidopsis proteins reveals five phosphorylation motifs. Both 
      ethylene-enhanced and -repressible phosphopeptides present in these motifs. 
      EIL-1, ERF110 transcription factors and Hua enhancer 4 (HEN4) are predicted to 
      contain one of the phosphorylation motifs. The phosphorylation of the 
      motif-containing peptides has been validated by the in vitro kinase assays 
      coupled with MS analysis. The differential regulation of phosphorylation by 
      ethylene is substantiated by Western dot blot analysis. Taken together, these 
      results suggest that ethylene signals may be transduced by a phosphor-relay from 
      receptors to transcriptional events via both ein2-dependent and -independent 
      pathways.
FAU - Li, Hao
AU  - Li H
AD  - Department of Biology, The Hong Kong University of Science and Technology, Hong 
      Kong SAR, PR China.
FAU - Wong, Wai Shing
AU  - Wong WS
FAU - Zhu, Lin
AU  - Zhu L
FAU - Guo, Hong Wei
AU  - Guo HW
FAU - Ecker, Joseph
AU  - Ecker J
FAU - Li, Ning
AU  - Li N
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Germany
TA  - Proteomics
JT  - Proteomics
JID - 101092707
RN  - 0 (Arabidopsis Proteins)
RN  - 0 (EIN2 protein, Arabidopsis)
RN  - 0 (ERF110 protein, Arabidopsis)
RN  - 0 (Ethylenes)
RN  - 0 (Phosphopeptides)
RN  - 0 (Phosphoproteins)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (Transcription Factors)
RN  - 91GW059KN7 (ethylene)
SB  - IM
MH  - Amino Acid Motifs
MH  - Amino Acid Sequence
MH  - Arabidopsis/drug effects/*metabolism
MH  - Arabidopsis Proteins/analysis/chemistry/*metabolism
MH  - Computational Biology
MH  - Electrophoresis, Gel, Two-Dimensional/*methods
MH  - Ethylenes/biosynthesis/*pharmacology
MH  - Mass Spectrometry/instrumentation
MH  - Molecular Sequence Data
MH  - Mutation/genetics
MH  - Phosphopeptides/analysis/chemistry/classification
MH  - Phosphoproteins/*analysis/chemistry
MH  - Phosphorylation/drug effects
MH  - Proteomics/*methods
MH  - Receptors, Cell Surface/*metabolism
MH  - Reproducibility of Results
MH  - Seedlings/drug effects/*metabolism
MH  - Sequence Alignment
MH  - Transcription Factors/*analysis/chemistry
EDAT- 2009/03/03 09:00
MHDA- 2009/04/30 09:00
CRDT- 2009/03/03 09:00
PHST- 2009/03/03 09:00 [entrez]
PHST- 2009/03/03 09:00 [pubmed]
PHST- 2009/04/30 09:00 [medline]
AID - 10.1002/pmic.200800420 [doi]
PST - ppublish
SO  - Proteomics. 2009 Mar;9(6):1646-61. doi: 10.1002/pmic.200800420.