SHIP2 associates with intersectin and recruits it to the plasma membrane in response to EGF.

@article{Xie2008SHIP2AW,
  title={SHIP2 associates with intersectin and recruits it to the plasma membrane in response to EGF.},
  author={Jingwei Xie and Isabelle Vandenbroere and Isabelle Pirson},
  journal={FEBS letters},
  year={2008},
  volume={582 20},
  pages={
          3011-7
        }
}
We identified intersectin1 (ITSN1) as a new binding partner of the SH2 domain containing inositol 5-phosphatase 2 (SHIP2). The interaction between SHIP2 and ITSN1 was confirmed in vivo. Src homology 3D, A, C, and E domains of ITSN1 were shown to be implicated in the interaction. In response to epidermal growth factor, SHIP2 expression could recruit the ITSN1 short form (ITSN1-S) to the cell membrane, while SHIP2 overexpression did not modulate the ITSN-mediated extracellular signal-regulated… CONTINUE READING

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References

Publications referenced by this paper.
SHOWING 1-10 OF 28 REFERENCES

The association between the SH2-containing inositol polyphosphate 5phosphatase 2 (SHIP2) and the adaptor protein APS has an impact on biochemical properties of both partners

S. Onnockx, S. J. De, +5 authors I. Pirson
  • J. Cell Physiol
  • 2008
VIEW 2 EXCERPTS