The effect of phosphatases SHP‐1 and SHIP‐1 on signaling by the ITIM‐ and ITAM‐containing Fcγ receptors FcγRIIB and FcγRIIA

@article{Huang2003TheEO,
  title={The effect of phosphatases SHP‐1 and SHIP‐1 on signaling by the ITIM‐ and ITAM‐containing Fc$\gamma$ receptors Fc$\gamma$RIIB and Fc$\gamma$RIIA},
  author={Zhen-yu Huang and Sharon Hunter and Moo-kyung Kim and Zena K. Indik and Alan D. Schreiber},
  journal={Journal of Leukocyte Biology},
  year={2003},
  volume={73}
}
Inositol and tyrosine phosphatases have been implicated in inhibitory signaling by an Fc receptor for immunoglobulin G, FcγRIIB, in B cells, mast cells, and monocytes. Here, we propose a role for the Src homology 2 (SH2)‐containing tyrosine phosphatase‐1 (SHP‐1) in FcγRIIB‐mediated inhibition of FcγR signaling. Coexpression of SHP‐1 enhances FcγRIIB‐mediated inhibition of FcγRIIA phagocytosis in COS‐1 cells. SHP‐1 also enhances the reduction in FcγRIIA tyrosine phosphorylation that accompanies… 
A pleckstrin homology‐related domain in SHIP1 mediates membrane localization during Fcγ receptor‐induced phagocytosis
  • A. Ming-Lum, S. Shojania, A. Mui
  • Biology
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 2012
TLDR
A pleckstrin homology‐related domain in SHIP1 mediates membrane localization during Fcγ receptor‐induced phagocytosis, and the PH‐R‐mediated membrane interaction appears to be a major mechanism by whichSHIP1 is recruited to the membrane.
The inositol phosphatase SHIP-2 down-regulates FcgammaR-mediated phagocytosis in murine macrophages independently of SHIP-1.
TLDR
SHIP-2 is a novel negative regulator of FcgammaR-mediated phagocytosis independent of SHIP-1, and down-regulates upstream activation of Rac.
A PKC-SHP1 signaling axis desensitizes Fcγ receptor signaling by reducing the tyrosine phosphorylation of CBL and regulates FcγR mediated phagocytosis
TLDR
The results suggest a functional model by which PKC interacts with SHP1 to affect the phosphorylation state of CBL, the activation state of Rac and the negative regulation of ITAM signaling i.e. Fcγ receptor mediated phagocytosis.
Phosphatidylinositol Phosphate Kinase Type Iγ Directly Associates with and Regulates Shp-1 Tyrosine Phosphatase*
TLDR
It is shown that Shp-1 phosphatase activity is inhibited by the product of PIPKIγ661, phosphatidylinositol 4,5-bisphosphate, in vitro, and this combined results suggest a model in which the reciprocal actions of Src tyrosine kinase and Sh p-1 tyrosines phosphatases dynamically regulate the association between PIPkiγ661 and talin.
Src homology 2-containing inositol 5'-phosphatase 1 negatively regulates IFN-gamma production by natural killer cells stimulated with antibody-coated tumor cells and interleukin-12.
TLDR
These results are the first to show a physiologic role for SHIP1 in the regulation of NK cell cytokine production and implicate PI3-K in the induction of MAPK signal transduction following costimulation of NK cells via the FcR and the IL-12R.
Differential Dephosphorylation of the FcRγ Immunoreceptor Tyrosine-based Activation Motif Tyrosines with Dissimilar Potential for Activating Syk*
TLDR
The findings argue for a novel regulatory mechanism, where dephosphorylation of phospho-Tyr58 is likely to promote the down-regulation of Syk activation and suppression of mast cell responses.
Regulation of hematopoietic cell function by inhibitory immunoglobulin G receptors and their inositol lipid phosphatase effectors
TLDR
This review provides an overview of current knowledge of membrane proximal events in signaling by inhibitory/regulatory receptors focusing on structural and functional characteristics of receptors and their effectors Src homology 2 (SH2) domain‐ containing tyrosine phosphatase 1 and SH2 domain‐containing inositol 5‐phosphatase‐1.
Sirt1 negatively regulates FcεRI-mediated mast cell activation through AMPK- and PTP1B-dependent processes
TLDR
It is shown that Sirt1 negatively regulates FcεRI-stimulated mast cell activation and anaphylaxis through two mutually regulated pathways involving AMP-activated protein kinase (AMPK) and protein tyrosine phosphatase 1B (PTP1B).
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TLDR
FcγRIIB phosphorylation may not be sufficient in vivo to enable the recruitment of SHP-1 but that (pathological?) conditions that would hyperphosphorylate FcγrIIB might enable SHp-1 recruitment.
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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