| Autor: |
Mehta, Payal, Wavreille, Anne-Sophie, Justiniano, Steven E., Marsh, Rachel L., Yu, Jianhua, Burry, Richard W., Jarjoura, David, Eubank, Timothy, Caligiuri, Michael A., Butchar, Jonathan P., Tridandapani, Susheela |
| Předmět: |
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| Zdroj: |
PLoS ONE; 2011, Vol. 6 Issue 6, p1-10, 10p |
| Abstrakt: |
SHIP and SHIP-2 are inositol phosphatases that regulate Fc&ggr;R-mediated phagocytosis through catalytic as well as noncatalytic mechanisms. In this study we have used two-dimensional fluorescence difference gel electrophoresis (DIGE) analysis to identify downstream signaling proteins that uniquely associate with SHIP or SHIP-2 upon Fc&ggr;R clustering in human monocytes. We identified LyGDI as a binding partner of SHIP, associating inducibly with the SHIP/Grb2/Shc complex. Immunodepletion and competition experiments with recombinant SHIP domains revealed that Grb2 and the proline-rich domain of SHIP were necessary for SHIP-LyGDI association. Functional studies in primary human monocytes showed that LyGDI sequesters Rac in the cytosol, preventing it from localizing to the membrane. Consistent with this, suppression of LyGDI expression resulted in significantly enhanced Fc&ggr;R-mediated phagocytosis. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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