PMID- 10381539
OWN - NLM
STAT- MEDLINE
DCOM- 19990921
LR  - 20190826
IS  - 0169-328X (Print)
IS  - 0169-328X (Linking)
VI  - 70
IP  - 1
DP  - 1999 Jun 18
TI  - Brain-derived neurotrophic factor enhances association of protein tyrosine 
      phosphatase PTP1D with the NMDA receptor subunit NR2B in the cortical 
      postsynaptic density.
PG  - 18-25
AB  - Our recent studies revealed that brain-derived neurotrophic factor (BDNF) rapidly 
      enhances tyrosine phosphorylation and dephosphorylation of the NMDA receptor 
      subunit, NR2B, in the postsynaptic density (PSD), potentially regulating synaptic 
      plasticity. To explore the molecular mechanisms underlying synaptic NR2B 
      signaling, we examined the protein tyrosine phosphatase, PTP1D; BDNF reportedly 
      increases association of PTP1D with tyrosine phosphorylated proteins in cortical 
      neurons and PC 12 cells. We now report that PTP1D is an intrinsic component of 
      the rat cerebrocortical PSD, based on Western blot analysis using specific 
      anti-PTP1D antibodies. In addition, NR2B was co-immunoprecipitated with PTP1D 
      using anti-NR2B antibodies or anti-PTP1D antibodies, indicating physical 
      association of the subunit with PTP1D. Moreover, treatment of the purified PSD 
      with BDNF for 5 min elicited a two-fold increase in the association of NR2B with 
      PTP1D. The BDNF action appeared to be specific, since nerve growth factor, 
      another member of the neurotrophin gene family, did not alter the association. 
      Finally, an overlay assay revealed that BDNF caused a two-fold increase in 
      binding of blotted PSD NR2B proteins to PTP1D-SH2 domains, revealing molecular 
      mechanisms mediating the PTP1D-NR2B binding. Taken together, our results raise 
      the possibility that PTP1D participates in BDNF-mediated NR2B signaling cascades 
      at the postsynaptic site, thereby regulating synaptic plasticity.
CI  - Copyright 1999 Elsevier Science B.V.
FAU - Lin, S Y
AU  - Lin SY
AD  - Department of Neuroscience and Cell Biology, UMDNJ-Robert Wood Johnson Medical 
      School, 679 Hoes Lane, Piscataway, NJ 08854, USA.
FAU - Wu, K
AU  - Wu K
FAU - Len, G W
AU  - Len GW
FAU - Xu, J L
AU  - Xu JL
FAU - Levine, E S
AU  - Levine ES
FAU - Suen, P C
AU  - Suen PC
FAU - Mount, H T
AU  - Mount HT
FAU - Black, I B
AU  - Black IB
LA  - eng
GR  - HD 23315/HD/NICHD NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - Netherlands
TA  - Brain Res Mol Brain Res
JT  - Brain research. Molecular brain research
JID - 8908640
RN  - 0 (Brain-Derived Neurotrophic Factor)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Peptide Fragments)
RN  - 0 (Receptors, N-Methyl-D-Aspartate)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 11)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 6)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatases)
RN  - EC 3.1.3.48 (Ptpn11 protein, rat)
RN  - EC 3.1.3.48 (Ptpn6 protein, rat)
RN  - EC 3.1.3.48 (SH2 Domain-Containing Protein Tyrosine Phosphatases)
SB  - IM
MH  - Animals
MH  - Brain-Derived Neurotrophic Factor/*pharmacology
MH  - Intracellular Signaling Peptides and Proteins
MH  - Nerve Tissue Proteins/metabolism
MH  - Neuronal Plasticity/*physiology
MH  - Peptide Fragments/metabolism
MH  - Phosphorylation
MH  - Protein Binding
MH  - *Protein Processing, Post-Translational
MH  - Protein Tyrosine Phosphatase, Non-Receptor Type 11
MH  - Protein Tyrosine Phosphatase, Non-Receptor Type 6
MH  - Protein Tyrosine Phosphatases/*metabolism
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Receptors, N-Methyl-D-Aspartate/chemistry/*metabolism
MH  - SH2 Domain-Containing Protein Tyrosine Phosphatases
MH  - Synaptic Membranes/*metabolism
MH  - src Homology Domains
EDAT- 1999/06/25 00:00
MHDA- 1999/06/25 00:01
CRDT- 1999/06/25 00:00
PHST- 1999/06/25 00:00 [pubmed]
PHST- 1999/06/25 00:01 [medline]
PHST- 1999/06/25 00:00 [entrez]
AID - S0169328X99001229 [pii]
AID - 10.1016/s0169-328x(99)00122-9 [doi]
PST - ppublish
SO  - Brain Res Mol Brain Res. 1999 Jun 18;70(1):18-25. doi: 
      10.1016/s0169-328x(99)00122-9.