Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor FcγRIIB Journal Article
| Authors: | Ono, M.; Bolland, S.; Tempst, P.; Ravetch, J. V. |
| Article Title: | Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor FcγRIIB |
| Abstract: | IMMUNE complexes are potent activators of inflammatory cells, triggering effector responses through the crosslinking of Fc receptors (FcRs) such as FcεRI or FcγRIII (ref. 1). On B cells and mast cells, immune complexes are also negative regulators of activation triggered by antigen and Fc receptors, a consequence of coligation of the B-cell antigen receptor or FcεRI, respectively, and the inhibitory receptor FcγRIIB. Here we show that inhibitory signalling by FcγRIIB does not require the SH2-domain-containing protein tyrosine phosphatase, SHP-1, in mast cells and results in the recruitment of the SH2-domain-containing inositol polyphosphate 5- phosphatase, SHIP, to the tyrosine-phosphorylated 13-amino-acid inhibitory motif of FcγRIIB in both B cells and mast cells. SHIP, by hydrolysing the 5- phosphate of phosphatidylinositol(3,4,5)P3 and inositol(1,3,4,5)P4, suggests a mechanism by which FcγRIIB can inhibit calcium influx and downstream responses triggered by immune receptors. |
| Keywords: | signal transduction; nonhuman; animal cell; animals; mice; immune system; cell line; calcium; phosphorylation; mice, inbred c57bl; inflammatory cell; b lymphocyte; b-lymphocytes; amino acid sequence; molecular sequence data; intracellular signaling peptides and proteins; peptides; fc receptor; receptors, igg; negative feedback; phosphoric monoester hydrolases; mast cell; mast cells; antigen antibody complex; cross linking; protein-tyrosine-phosphatase; cell degranulation; inositol phosphate; priority journal; article; shp1 protein tyrosine phosphatase; src homology domains |
| Journal Title: | Nature |
| Volume: | 383 |
| Issue: | 6597 |
| ISSN: | 0028-0836 |
| Publisher: | Nature Publishing Group |
| Date Published: | 1996-09-19 |
| Start Page: | 263 |
| End Page: | 266 |
| Language: | English |
| DOI: | 10.1038/383263a0 |
| PUBMED: | 8805703 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Source: Scopus |
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