PMID- 10207032
OWN - NLM
STAT- MEDLINE
DCOM- 19990520
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 17
DP  - 1999 Apr 23
TI  - Mutation of tyrosine 960 within the insulin receptor juxtamembrane domain impairs
      glucose transport but does not inhibit ligand-mediated phosphorylation of insulin
      receptor substrate-2 in 3T3-L1 adipocytes.
PG  - 12075-80
AB  - CSF-1 is equipotent to insulin in its ability to stimulate 2-[3H]deoxyglucose
      uptake in 3T3-L1 adipocytes expressing the colony stimulating factor-1
      receptor/insulin receptor chimera (CSF1R/IR). However, CSF-1-stimulated glucose
      uptake and glycogen synthesis is reduced by 50% in comparison to insulin in
      3T3-L1 cells expressing a CSF1R/IR mutated at Tyr960 (CSF1R/IRA960).
      CSF-1-treated adipocytes expressing the CSF1R/IRA960 were impaired in their
      ability to phosphorylate insulin receptor substrate 1 (IRS-1) but not in their
      ability to phosphorylate IRS-2. Immunoprecipitation of IRS proteins followed by
      Western blotting revealed that the intact CSF1R/IR co-precipitates with IRS-2
      from CSF-1-treated cells. In contrast, the CSF1R/IRA960 co-precipitates poorly
      with IRS-2. These observations suggest that Tyr960 is important for interaction
      of the insulin receptor cytoplasmic domain with IRS-2, but it is not essential to
      the ability of the insulin receptor tyrosine kinase to use IRS-2 as a substrate. 
      These observations also suggest that in 3T3-L1 adipocytes, tyrosine
      phosphorylation of IRS-2 by the insulin receptor tyrosine kinase is not
      sufficient for maximal stimulation of receptor-regulated glucose transport or
      glycogen synthesis.
FAU - Chaika, O V
AU  - Chaika OV
AD  - Eppley Institute for Research in Cancer and Allied Diseases, University of
      Nebraska Medical Center, Omaha, Nebraska 68198-6805, USA.
FAU - Chaika, N
AU  - Chaika N
FAU - Volle, D J
AU  - Volle DJ
FAU - Hayashi, H
AU  - Hayashi H
FAU - Ebina, Y
AU  - Ebina Y
FAU - Wang, L M
AU  - Wang LM
FAU - Pierce, J H
AU  - Pierce JH
FAU - Lewis, R E
AU  - Lewis RE
LA  - eng
GR  - DK52809/DK/NIDDK NIH HHS/United States
GR  - P30 CA36727/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Insulin Receptor Substrate Proteins)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (Irs2 protein, mouse)
RN  - 0 (Ligands)
RN  - 0 (Phosphoproteins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 42HK56048U (Tyrosine)
RN  - 81627-83-0 (Macrophage Colony-Stimulating Factor)
RN  - EC 2.7.1.- (Phosphatidylinositol 3-Kinases)
RN  - EC 2.7.10.1 (Receptor, Insulin)
RN  - EC 2.7.10.1 (Receptor, Macrophage Colony-Stimulating Factor)
RN  - IY9XDZ35W2 (Glucose)
SB  - IM
MH  - 3T3 Cells
MH  - Adipocytes/*metabolism
MH  - Animals
MH  - Biological Transport
MH  - Cell Membrane/metabolism
MH  - Cytoplasm/metabolism
MH  - Enzyme Activation
MH  - Glucose/*metabolism
MH  - Insulin Receptor Substrate Proteins
MH  - Intracellular Signaling Peptides and Proteins
MH  - Ligands
MH  - Macrophage Colony-Stimulating Factor/pharmacology
MH  - Mice
MH  - Phosphatidylinositol 3-Kinases/metabolism
MH  - Phosphoproteins/*metabolism
MH  - Phosphorylation
MH  - Receptor, Insulin/genetics/*metabolism
MH  - Receptor, Macrophage Colony-Stimulating Factor/metabolism
MH  - Recombinant Fusion Proteins/metabolism
MH  - Tyrosine/genetics/*metabolism
EDAT- 1999/04/17 00:00
MHDA- 1999/04/17 00:01
CRDT- 1999/04/17 00:00
PHST- 1999/04/17 00:00 [pubmed]
PHST- 1999/04/17 00:01 [medline]
PHST- 1999/04/17 00:00 [entrez]
AID - 10.1074/jbc.274.17.12075 [doi]
AID - S0021-9258(19)73533-9 [pii]
PST - ppublish
SO  - J Biol Chem. 1999 Apr 23;274(17):12075-80. doi: 10.1074/jbc.274.17.12075.