PMID- 20347422
OWN - NLM
STAT- MEDLINE
DCOM- 20100420
LR  - 20220309
IS  - 1097-4164 (Electronic)
IS  - 1097-2765 (Print)
IS  - 1097-2765 (Linking)
VI  - 37
IP  - 6
DP  - 2010 Mar 26
TI  - Postnatal deamidation of 4E-BP2 in brain enhances its association with raptor and 
      alters kinetics of excitatory synaptic transmission.
PG  - 797-808
LID - 10.1016/j.molcel.2010.02.022 [doi]
AB  - The eIF4E-binding proteins (4E-BPs) repress translation initiation by preventing 
      eIF4F complex formation. Of the three mammalian 4E-BPs, only 4E-BP2 is enriched 
      in the mammalian brain and plays an important role in synaptic plasticity and 
      learning and memory formation. Here we describe asparagine deamidation as a 
      brain-specific posttranslational modification of 4E-BP2. Deamidation is the 
      spontaneous conversion of asparagines to aspartates. Two deamidation sites were 
      mapped to an asparagine-rich sequence unique to 4E-BP2. Deamidated 4E-BP2 
      exhibits increased binding to the mammalian target of rapamycin (mTOR)-binding 
      protein raptor, which effects its reduced association with eIF4E. 4E-BP2 
      deamidation occurs during postnatal development, concomitant with the attenuation 
      of the activity of the PI3K-Akt-mTOR signaling pathway. Expression of deamidated 
      4E-BP2 in 4E-BP2(-/-) neurons yielded mEPSCs exhibiting increased charge transfer 
      with slower rise and decay kinetics relative to the wild-type form. 4E-BP2 
      deamidation may represent a compensatory mechanism for the developmental 
      reduction of PI3K-Akt-mTOR signaling.
CI  - (c) 2010 Elsevier Inc. All rights reserved.
FAU - Bidinosti, Michael
AU  - Bidinosti M
AD  - Department of Biochemistry and Goodman Cancer Centre, McGill University, 
      Montreal, QC H3G 1Y6, Canada.
FAU - Ran, Israeli
AU  - Ran I
FAU - Sanchez-Carbente, Maria R
AU  - Sanchez-Carbente MR
FAU - Martineau, Yvan
AU  - Martineau Y
FAU - Gingras, Anne-Claude
AU  - Gingras AC
FAU - Gkogkas, Christos
AU  - Gkogkas C
FAU - Raught, Brian
AU  - Raught B
FAU - Bramham, Clive R
AU  - Bramham CR
FAU - Sossin, Wayne S
AU  - Sossin WS
FAU - Costa-Mattioli, Mauro
AU  - Costa-Mattioli M
FAU - DesGroseillers, Luc
AU  - DesGroseillers L
FAU - Lacaille, Jean-Claude
AU  - Lacaille JC
FAU - Sonenberg, Nahum
AU  - Sonenberg N
LA  - eng
GR  - P41 RR018522/RR/NCRR NIH HHS/United States
GR  - HHMI/Howard Hughes Medical Institute/United States
GR  - R01 GM066157/GM/NIGMS NIH HHS/United States
GR  - P41 RR018522-048661/RR/NCRR NIH HHS/United States
GR  - 15121/CAPMC/CIHR/Canada
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Mol Cell
JT  - Molecular cell
JID - 9802571
RN  - 0 (Eif4ebp2 protein, mouse)
RN  - 0 (Eukaryotic Initiation Factors)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Animals, Newborn
MH  - Brain/*metabolism
MH  - Cells, Cultured
MH  - Eukaryotic Initiation Factors/chemistry/deficiency/genetics/*metabolism
MH  - Humans
MH  - Kinetics
MH  - Mice
MH  - Mice, Knockout
MH  - Molecular Sequence Data
MH  - Organ Specificity
MH  - Phosphorylation
MH  - *Protein Processing, Post-Translational
MH  - Protein Transport
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - *Synaptic Transmission
PMC - PMC2861547
MID - NIHMS193241
EDAT- 2010/03/30 06:00
MHDA- 2010/04/21 06:00
PMCR- 2010/09/26
CRDT- 2010/03/30 06:00
PHST- 2009/07/14 00:00 [received]
PHST- 2009/12/06 00:00 [revised]
PHST- 2010/02/21 00:00 [accepted]
PHST- 2010/03/30 06:00 [entrez]
PHST- 2010/03/30 06:00 [pubmed]
PHST- 2010/04/21 06:00 [medline]
PHST- 2010/09/26 00:00 [pmc-release]
AID - S1097-2765(10)00204-2 [pii]
AID - 10.1016/j.molcel.2010.02.022 [doi]
PST - ppublish
SO  - Mol Cell. 2010 Mar 26;37(6):797-808. doi: 10.1016/j.molcel.2010.02.022.