Interleukin-3 Induces the Association of the Inositol 5-Phosphatase SHIP with SHP2
作者： Ling Liu , Jacqueline E. Damen , Mark D. Ware , Gerald Krystal
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摘要: We recently purified and cloned a 145-kDa protein that becomes tyrosine phosphorylated associated with Shc in response to multiple cytokines. Based on its predicated amino acid sequence enzymatic activity, we have called this SHIP, for rc omology 2-containing nositol hosphatase. To gain further insight into the intracellular pathways putative signal transduction intermediate might regulate investigated whether SHIP binds proteins other than Shc. The results presented herein demonstrate following interleukin-3 stimulation, phosphatase, SHP2 (also Syp, PTP1D, SHPTP2, PTP2C) is not present these SHIP-SHP2 complexes. Time course studies reveal SHIP's association transient maximal at 10 min of stimulation interleukin-3. show occurs through direct interaction SH2 domain pYXN(I/V) within SHP2.
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