PMID- 25912465
OWN - NLM
STAT- MEDLINE
DCOM- 20160921
LR  - 20211203
IS  - 1365-313X (Electronic)
IS  - 0960-7412 (Linking)
VI  - 82
IP  - 6
DP  - 2015 Jun
TI  - An autophosphorylation site database for leucine-rich repeat receptor-like 
      kinases in Arabidopsis thaliana.
PG  - 1042-1060
LID - 10.1111/tpj.12863 [doi]
AB  - Leucine-rich repeat receptor-like kinases (LRR RLKs) form a large family of plant 
      signaling proteins consisting of an extracellular domain connected by a 
      single-pass transmembrane sequence to a cytoplasmic kinase domain. 
      Autophosphorylation on specific Ser and/or Thr residues in the cytoplasmic domain 
      is often critical for the activation of several LRR RLK family members with 
      proven functional roles in plant growth regulation, morphogenesis, disease 
      resistance, and stress responses. While identification and functional 
      characterization of in vivo phosphorylation sites is ultimately required for a 
      full understanding of LRR RLK biology and function, bacterial expression of 
      recombinant LRR RLK cytoplasmic catalytic domains for identification of in vitro 
      autophosphorylation sites provides a useful resource for further targeted 
      identification and functional analysis of in vivo sites. In this study we 
      employed high-throughput cloning and a variety of mass spectrometry approaches to 
      generate an autophosphorylation site database representative of more than 30% of 
      the approximately 223 LRR RLKs in Arabidopsis thaliana. We used His-tagged 
      constructs of complete cytoplasmic domains to identify a total of 592 
      phosphorylation events across 73 LRR RLKs, with 497 sites uniquely assigned to 
      specific Ser (268 sites) or Thr (229 sites) residues in 68 LRR RLKs. Multiple 
      autophosphorylation sites per LRR RLK were the norm, with an average of seven 
      sites per cytoplasmic domain, while some proteins showed more than 20 unique 
      autophosphorylation sites. The database was used to analyze trends in the 
      localization of phosphorylation sites across cytoplasmic kinase subdomains and to 
      derive a statistically significant sequence motif for phospho-Ser 
      autophosphorylation.
CI  - (c) 2015 The Authors The Plant Journal (c) 2015 John Wiley & Sons Ltd.
FAU - Mitra, Srijeet K
AU  - Mitra SK
AD  - Department of Horticultural Science, North Carolina State University, Raleigh, 
      NC, 27695, USA.
FAU - Chen, Ruiqiang
AU  - Chen R
AD  - Department of Horticultural Science, North Carolina State University, Raleigh, 
      NC, 27695, USA.
FAU - Dhandaydham, Murali
AU  - Dhandaydham M
AD  - Department of Horticultural Science, North Carolina State University, Raleigh, 
      NC, 27695, USA.
FAU - Wang, Xiaofeng
AU  - Wang X
AD  - Department of Horticultural Science, North Carolina State University, Raleigh, 
      NC, 27695, USA.
FAU - Blackburn, Robert Kevin
AU  - Blackburn RK
AD  - Department of Molecular and Structural Biochemistry, North Carolina State 
      University, Raleigh, NC, 27695, USA.
FAU - Kota, Uma
AU  - Kota U
AD  - Department of Molecular and Structural Biochemistry, North Carolina State 
      University, Raleigh, NC, 27695, USA.
FAU - Goshe, Michael B
AU  - Goshe MB
AD  - Department of Molecular and Structural Biochemistry, North Carolina State 
      University, Raleigh, NC, 27695, USA.
FAU - Schwartz, Daniel
AU  - Schwartz D
AD  - Department of Physiology and Neurobiology, University of Connecticut, Storrs, CT, 
      06269, USA.
FAU - Huber, Steven C
AU  - Huber SC
AD  - USDA/ARS, University of Illinois, Urbana, IL, 61801, USA.
FAU - Clouse, Steven D
AU  - Clouse SD
AD  - Department of Horticultural Science, North Carolina State University, Raleigh, 
      NC, 27695, USA.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
DEP - 20150522
PL  - England
TA  - Plant J
JT  - The Plant journal : for cell and molecular biology
JID - 9207397
RN  - 0 (Arabidopsis Proteins)
RN  - EC 2.7.- (Protein Kinases)
RN  - EC 2.7.1.- (BAK1 protein, Arabidopsis)
RN  - EC 2.7.1.- (SERK1 protein, Arabidopsis)
RN  - EC 2.7.11.1 (BRI1 protein, Arabidopsis)
RN  - EC 2.7.11.1 (Protein Serine-Threonine Kinases)
SB  - IM
MH  - Amino Acid Motifs
MH  - Amino Acid Sequence
MH  - Arabidopsis/genetics/metabolism
MH  - Arabidopsis Proteins/genetics/*metabolism
MH  - Cytoplasm/metabolism
MH  - *Databases, Factual
MH  - Escherichia coli/genetics
MH  - Molecular Sequence Data
MH  - Phosphorylation
MH  - Protein Kinases/genetics/*metabolism
MH  - Protein Serine-Threonine Kinases/genetics/metabolism
MH  - Protein Structure, Tertiary
OTO - NOTNLM
OT  - Arabidopsis thaliana
OT  - mass spectrometry
OT  - motif analysis
OT  - phosphorylation
OT  - receptor kinase
EDAT- 2015/04/29 06:00
MHDA- 2016/09/23 06:00
CRDT- 2015/04/28 06:00
PHST- 2015/03/18 00:00 [received]
PHST- 2015/04/21 00:00 [accepted]
PHST- 2015/04/28 06:00 [entrez]
PHST- 2015/04/29 06:00 [pubmed]
PHST- 2016/09/23 06:00 [medline]
AID - 10.1111/tpj.12863 [doi]
PST - ppublish
SO  - Plant J. 2015 Jun;82(6):1042-1060. doi: 10.1111/tpj.12863. Epub 2015 May 22.