PMID- 11912194
OWN - NLM
STAT- MEDLINE
DCOM- 20020702
LR  - 20210206
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 277
IP  - 22
DP  - 2002 May 31
TI  - Insulin receptor substrate 4 associates with the protein IRAS.
PG  - 19439-47
AB  - The insulin receptor substrates (IRSs) are key components in signaling from the 
      insulin receptor, and consequently any proteins that interact with them are 
      expected to participate in insulin signaling. In this study we have searched for 
      proteins that interact with IRS-4 by identifying the proteins that 
      coimmunoprecipitated with IRS-4 from human embryonic kidney 293 cells by 
      microsequencing through mass spectrometry. A group of proteins was found. These 
      included phosphatidylinositol 3-kinase, a protein previously identified as an 
      IRS-4 interactor, and several proteins for which there was no previous evidence 
      of IRS-4 association. One of these proteins, named IRAS, that had been found 
      earlier in another context was examined in detail. The results from the 
      overexpression of IRAS, where its amount was about the same as that of IRS-4, 
      indicated that IRAS associated directly with IRS-4 and showed that the increased 
      complexation of IRS-4 with IRAS did not alter the insulin-stimulated tyrosine 
      phosphorylation of IRS-4 or the association of IRS-4 with phosphatidylinositol 
      3-kinase or Grb2. On the other hand, overexpression of IRAS enhanced 
      IRS-4-dependent insulin stimulation of the extracellularly regulated kinase. The 
      domains of IRAS and IRS-4 responsible for the association of these two proteins 
      were identified, and it was shown that IRAS also associates with IRS-1, IRS-2, 
      and IRS-3.
FAU - Sano, Hiroyuki
AU  - Sano H
AD  - Department of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 
      03755, USA.
FAU - Liu, Simon C H
AU  - Liu SC
FAU - Lane, William S
AU  - Lane WS
FAU - Piletz, John E
AU  - Piletz JE
FAU - Lienhard, Gustav E
AU  - Lienhard GE
LA  - eng
GR  - R01 MH049248/MH/NIMH NIH HHS/United States
GR  - MH49248/MH/NIMH 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.
DEP - 20020323
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (Carrier Proteins)
RN  - 0 (DNA, Complementary)
RN  - 0 (GRB2 Adaptor Protein)
RN  - 0 (GRB2 protein, human)
RN  - 0 (IRS1 protein, human)
RN  - 0 (IRS2 protein, human)
RN  - 0 (IRS3P protein, human)
RN  - 0 (IRS4 protein, human)
RN  - 0 (Imidazoline Receptors)
RN  - 0 (Insulin Receptor Substrate Proteins)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (Irs1 protein, mouse)
RN  - 0 (Irs2 protein, mouse)
RN  - 0 (Irs4 protein, mouse)
RN  - 0 (NISCH protein, human)
RN  - 0 (Phosphoproteins)
RN  - 0 (Proteins)
RN  - 42HK56048U (Tyrosine)
RN  - EC 2.7.1.- (Phosphatidylinositol 3-Kinases)
SB  - IM
MH  - *Adaptor Proteins, Signal Transducing
MH  - Animals
MH  - Binding Sites
MH  - COS Cells
MH  - Carrier Proteins/*chemistry/*metabolism
MH  - Cell Line
MH  - DNA, Complementary/metabolism
MH  - GRB2 Adaptor Protein
MH  - Humans
MH  - Imidazoline Receptors
MH  - Immunoblotting
MH  - Insulin Receptor Substrate Proteins
MH  - *Intracellular Signaling Peptides and Proteins
MH  - Mass Spectrometry
MH  - Phosphatidylinositol 3-Kinases/metabolism
MH  - Phosphoproteins/*chemistry/*metabolism
MH  - Phosphorylation
MH  - Plasmids/metabolism
MH  - Precipitin Tests
MH  - Protein Binding
MH  - Protein Structure, Tertiary
MH  - Proteins/metabolism
MH  - Subcellular Fractions/metabolism
MH  - Time Factors
MH  - Transfection
MH  - Tyrosine/metabolism
EDAT- 2002/03/26 10:00
MHDA- 2002/07/03 10:01
CRDT- 2002/03/26 10:00
PHST- 2002/03/26 10:00 [pubmed]
PHST- 2002/07/03 10:01 [medline]
PHST- 2002/03/26 10:00 [entrez]
AID - S0021-9258(20)85001-7 [pii]
AID - 10.1074/jbc.M111838200 [doi]
PST - ppublish
SO  - J Biol Chem. 2002 May 31;277(22):19439-47. doi: 10.1074/jbc.M111838200. Epub 2002 
      Mar 23.