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. 2001 Jan 15;193(2):263–270. doi: 10.1084/jem.193.2.263

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© 2001 The Rockefeller University Press

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SSI family proteins modulate the phosphorylation state of IRS-1. (A) L929/neo (lanes 1–4) and L929/SSI-1 (lanes 5–8) cells were stimulated with insulin for 0 (lanes 1 and 5), 10 (lanes 2 and 6), 30 (lanes 3 and 7), and 60 min (lanes 4 and 8). Total cell lysates were subjected to Western blot analysis with antiphosphotyrosine antibody. Arrow indicates reduced phosphorylation band in L929/SSI-1 cells. (B) L929/neo (lanes 1–4), L929/SSI-1 (lanes 5–8), L929/SSI-3 (lanes 9–12), or L929/SOCS5 (lanes 13–16) cells were treated with insulin (top and second panels) or IGF-1 (third and bottom panels) for the indicated times. Tyrosine phosphorylation of IRS-1 was analyzed (top and third panels) by immunoprecipitation followed by Western blot analysis. The second and bottom panels show that equal amounts of IRS-1 were immunoprecipitated. (C) MEFs derived from SSI-1^+/+ (lanes 1–4) and SSI-1^−/− (lanes 5–8) were treated with insulin and the phosphorylation state of IRS-1 was detected as in B. IP, immunoprecipitation; WB, Western blot analysis; pY, phosphotyrosine.