PMID- 10460236
OWN - NLM
STAT- MEDLINE
DCOM- 19990923
LR  - 20191023
IS  - 1529-2401 (Electronic)
IS  - 0270-6474 (Linking)
VI  - 19
IP  - 17
DP  - 1999 Sep 1
TI  - The insulin receptor tyrosine kinase substrate p58/53 and the insulin receptor
      are components of CNS synapses.
PG  - 7300-8
AB  - The synapse is the primary locus of cell-cell communication in the nervous
      system. It is now clear that the synapse incorporates diverse cell signaling
      modalities in addition to classical neurotransmission. Here we show that two
      components of the insulin pathway are localized at CNS synapses, where they are
      components of the postsynaptic density (PSD). An immunochemical screen revealed
      that polypeptides of 58 and 53 kDa (p58/53) were highly enriched in PSD fractions
      from rat cerebral cortex, hippocampus, and cerebellum. These polypeptides were
      purified and microsequenced, revealing that p58/53 is identical to the insulin
      receptor tyrosine kinase substrate p58/53 (IRSp53). Our analysis of IRSp58/53
      mRNA suggests that within rat brain there is one coding region for IRSp58 and
      IRSp53; we find no evidence of alternative splicing. We demonstrate that
      IRSp58/53 is expressed in the synapse-rich molecular layer of the cerebellum and 
      is highly concentrated at the synapses of cultured hippocampal neurons, where it 
      co-localizes with the insulin receptor. Together, these data suggest that insulin
      signaling may play a role at CNS synapses.
FAU - Abbott, M A
AU  - Abbott MA
AD  - Department of Neuroscience, Brown University, Providence, Rhode Island 02912,
      USA.
FAU - Wells, D G
AU  - Wells DG
FAU - Fallon, J R
AU  - Fallon JR
LA  - eng
GR  - R01 HD023924/HD/NICHD NIH HHS/United States
GR  - HD23924/HD/NICHD NIH HHS/United States
GR  - MH53571/MH/NIMH NIH HHS/United States
GR  - NS10343/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Neurosci
JT  - The Journal of neuroscience : the official journal of the Society for
      Neuroscience
JID - 8102140
RN  - 0 (BAIAP2 protein, human)
RN  - 0 (Insulin Receptor Substrate Proteins)
RN  - 0 (Irs1 protein, rat)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Phosphoproteins)
RN  - EC 2.7.10.1 (Receptor, Insulin)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Brain/cytology/*physiology
MH  - Brain Chemistry
MH  - Cells, Cultured
MH  - Cerebellum/chemistry/cytology/physiology
MH  - Electrophoresis, Gel, Two-Dimensional
MH  - Hippocampus/chemistry/cytology/physiology
MH  - Insulin Receptor Substrate Proteins
MH  - Molecular Sequence Data
MH  - Nerve Tissue Proteins/*analysis/chemistry/genetics
MH  - Neurons/chemistry/*physiology
MH  - Phosphoproteins/*analysis/chemistry/genetics
MH  - Rats
MH  - Receptor, Insulin/*analysis/genetics/*metabolism
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
MH  - Synapses/chemistry/*physiology
MH  - Synaptosomes/chemistry
PMC - PMC6782521
EDAT- 1999/08/25 00:00
MHDA- 1999/08/25 00:01
CRDT- 1999/08/25 00:00
PHST- 1999/08/25 00:00 [pubmed]
PHST- 1999/08/25 00:01 [medline]
PHST- 1999/08/25 00:00 [entrez]
PST - ppublish
SO  - J Neurosci. 1999 Sep 1;19(17):7300-8.