PMID- 21423366
OWN - NLM
STAT- PubMed-not-MEDLINE
DCOM- 20110509
LR  - 20240320
IS  - 1664-042X (Electronic)
IS  - 1664-042X (Linking)
VI  - 1
DP  - 2010
TI  - A membrane protein/signaling protein interaction network for Arabidopsis version 
      AMPv2.
PG  - 24
LID - 10.3389/fphys.2010.00024 [doi]
LID - 24
AB  - Interactions between membrane proteins and the soluble fraction are essential for 
      signal transduction and for regulating nutrient transport. To gain insights into 
      the membrane-based interactome, 3,852 open reading frames (ORFs) out of a target 
      list of 8,383 representing membrane and signaling proteins from Arabidopsis 
      thaliana were cloned into a Gateway-compatible vector. The mating-based split 
      ubiquitin system was used to screen for potential protein-protein interactions 
      (pPPIs) among 490 Arabidopsis ORFs. A binary robotic screen between 142 
      receptor-like kinases (RLKs), 72 transporters, 57 soluble protein kinases and 
      phosphatases, 40 glycosyltransferases, 95 proteins of various functions, and 89 
      proteins with unknown function detected 387 out of 90,370 possible PPIs. A 
      secondary screen confirmed 343 (of 386) pPPIs between 179 proteins, yielding a 
      scale-free network (r(2) = 0.863). Eighty of 142 transmembrane RLKs tested 
      positive, identifying 3 homomers, 63 heteromers, and 80 pPPIs with other 
      proteins. Thirty-one out of 142 RLK interactors (including RLKs) had previously 
      been found to be phosphorylated; thus interactors may be substrates for 
      respective RLKs. None of the pPPIs described here had been reported in the major 
      interactome databases, including potential interactors of G-protein-coupled 
      receptors, phospholipase C, and AMT ammonium transporters. Two RLKs found as 
      putative interactors of AMT1;1 were independently confirmed using a split 
      luciferase assay in Arabidopsis protoplasts. These RLKs may be involved in 
      ammonium-dependent phosphorylation of the C-terminus and regulation of ammonium 
      uptake activity. The robotic screening method established here will enable a 
      systematic analysis of membrane protein interactions in fungi, plants and 
      metazoa.
FAU - Lalonde, Sylvie
AU  - Lalonde S
AD  - Department of Plant Biology, Carnegie Institution for Science Stanford, CA, USA. 
      slalonde@stanford.edu
FAU - Sero, Antoinette
AU  - Sero A
FAU - Pratelli, Rejane
AU  - Pratelli R
FAU - Pilot, Guillaume
AU  - Pilot G
FAU - Chen, Jin
AU  - Chen J
FAU - Sardi, Maria I
AU  - Sardi MI
FAU - Parsa, Saman A
AU  - Parsa SA
FAU - Kim, Do-Young
AU  - Kim DY
FAU - Acharya, Biswa R
AU  - Acharya BR
FAU - Stein, Erica V
AU  - Stein EV
FAU - Hu, Heng-Chen
AU  - Hu HC
FAU - Villiers, Florent
AU  - Villiers F
FAU - Takeda, Kouji
AU  - Takeda K
FAU - Yang, Yingzhen
AU  - Yang Y
FAU - Han, Yong S
AU  - Han YS
FAU - Schwacke, Rainer
AU  - Schwacke R
FAU - Chiang, William
AU  - Chiang W
FAU - Kato, Naohiro
AU  - Kato N
FAU - Loque, Dominique
AU  - Loque D
FAU - Assmann, Sarah M
AU  - Assmann SM
FAU - Kwak, June M
AU  - Kwak JM
FAU - Schroeder, Julian I
AU  - Schroeder JI
FAU - Rhee, Seung Y
AU  - Rhee SY
FAU - Frommer, Wolf B
AU  - Frommer WB
LA  - eng
PT  - Journal Article
DEP - 20100922
PL  - Switzerland
TA  - Front Physiol
JT  - Frontiers in physiology
JID - 101549006
PMC - PMC3059934
OTO - NOTNLM
OT  - kinase
OT  - phosphorylation
OT  - protein interaction
OT  - receptor
OT  - split ubiquitin system
OT  - transport
OT  - yeast two hybrid
EDAT- 2010/01/01 00:00
MHDA- 2010/01/01 00:01
PMCR- 2010/09/22
CRDT- 2011/03/23 06:00
PHST- 2010/06/11 00:00 [received]
PHST- 2010/07/20 00:00 [accepted]
PHST- 2011/03/23 06:00 [entrez]
PHST- 2010/01/01 00:00 [pubmed]
PHST- 2010/01/01 00:01 [medline]
PHST- 2010/09/22 00:00 [pmc-release]
AID - 10.3389/fphys.2010.00024 [doi]
PST - epublish
SO  - Front Physiol. 2010 Sep 22;1:24. doi: 10.3389/fphys.2010.00024. eCollection 2010.