Epidermal Growth Factor Stimulates the Tyrosine Phosphorylation of SHPS-1 and Association of SHPS-1 with SHP-2, a SH2 Domain-Containing Protein Tyrosine Phosphatase |
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| Affiliation: | 2. Massachusetts General Hospital and Harvard Medical School, Charlestown, MA, United States;1. Department of Physics, School of Natural Sciences, Shiv Nadar University, Gautam Budh Nagar 201314, Uttar Pradesh, India.;2. Amity Institute of Nanotechnology, Amity University, Sector-125, Noida 201303, Uttar Pradesh, India.;3. Department of Electrical Engineering, School of Engineering, Shiv Nadar University, Gautam Budh Nagar 201314, Uttar Pradesh, India.;4. Nanotechnology and Integrated Bioengineering Centre, Jordanstown Campus, University of Ulster, Newtownabbey, BT37 OQB, Northern Ireland, United Kingdom. |
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| Abstract: | SHPS-1 is a 120 kDa glycosylated receptor-like protein that contains immunoglobulin-like domains in its extracellular region and four potential tyrosine phosphorylation for SH2 domain binding sites in its cytoplasmic region. Epidermal growth factor (EGF) stimulated the rapid tyrosine phosphorylation of SHPS-1 and subsequent association of SHPS-1 with SHP-2, a protein tyrosine phosphatase containing SH2 domains, in Chinese hamster ovary cells overexpressing human EGF receptors. In the cells overexpressing SHPS-1, the tyrosine phosphorylation of SHPS-1 was more evident than that observed in parent cells. However, overexpression of SHPS-1 alone did not affect the activation of MAP kinase in response to EGF. These results suggest that SHPS-1 may be involved in the recruitment of SHP-2 from the cytosol to the plasma membrane in response to EGF. |
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