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J Biol Chem, Vol. 273, Issue 17, 10726-10732, April 24, 1998
From the Department of Biochemistry, Dartmouth Medical School,
Hanover, New Hampshire 03755 and We recently cloned IRS-4, a new member of the
insulin receptor substrate (IRS) family. In this study we have
characterized IRS-4 in human embryonic kidney 293 cells, where it was
originally discovered. IRS-4 was the predominant insulin-elicited
phosphotyrosine protein in these cells. Subcellular fractionation
revealed that about 50% of IRS-4 was located in cellular membranes,
and immunofluorescence indicated that IRS-4 was concentrated at the
plasma membrane. Immunoelectron microscopy conclusively established
that a large portion of the IRS-4 was located at the cytoplasmic
surface of the plasma membrane in both the unstimulated and
insulin-treated states. IRS-4 was found to be associated with two src
homology 2 (SH2) domain-containing proteins, phosphatidylinositol
3-kinase and Grb2, the adaptor to the guanine nucleotide exchange
factor for Ras. On the other hand, no significant association was
detected with two other SH2 domain proteins, the SH2-containing protein tyrosine phosphatase 2 and phospholipase C
Characterization of Insulin Receptor Substrate 4 in Human
Embryonic Kidney 293 Cells
, Department of Cell
Biology, Medical School, Utrecht University,
3584 CX Utrecht, The Netherlands
. Insulin-like growth factor I acting through its receptor was as effective as insulin in
eliciting tyrosine phosphorylation of IRS-4, but interleukin 4 and
epidermal growth factor were ineffective.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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