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American Chemical Society, Biochemistry, 27(36), p. 8304-8310, 1997

DOI: 10.1021/bi9630974

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The 60 kDa Insulin Receptor Substrate Functions Like an IRS Protein (pp60<sup>IRS3</sup>) in Adipose Cells

Journal article published in 1997 by Jennifer Smith-Hall, Sebastian Pons, Mary Elizabeth Patti ORCID, Deborah J. Burks, Lynne Yenush, Xiao Jian Sun, C. Ronald Kahn, Morris F. White
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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Abstract

The 60 kDa insulin receptor substrate in rat adipocytes that binds to the PI-3 kinase displays several functional characteristics in common with the IRS proteins; so we propose the name pp60(IRS3) to distinguish it from other tyrosine phosphorylated proteins of similar size. During insulin stimulation, p85 associated with pp60(IRS3) more rapidly than with IRS-1 or IRS-2. In mice lacking IRS-1, p85 associated more strongly with pp60(IRS3) than with IRS-2, suggesting that pp60(IRS3) provides an alternate pathway in these cells. Synthetic peptides containing two phosphorylated YMPM motifs displace pp60(IRS3) and IRS-1 from alphap85 immune complexes, suggesting that pp60(IRS3), like IRS-1, engages both SH2 domains in p85. Moreover, pp60(IRS3) binds to immobilized peptides containing a phosphorylated NPXY motif, suggesting that it contains a PTB domain with similar specificity to that in IRS-1. The cloning of pp60(IRS3) will reveal a new member of the IRS protein family which mediates insulin receptor signals in a narrow range of tissues.