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© Matteo Bonazzi, Edith Gouin
Observation en immunofluorescence d'une cellule infectée par Listeria monocytogenes. En bleu: marquage des protéines de surface de Listeria qui permet de visualiser les bactéries. En rouge et vert: marquage de l'actine, une protéine qui forme le cytosquelette des cellules. Les Listeria utilisent l'actine cellulaire pour former des "comêtes" et se déplacer à l'intérieur des cellules qu'elles infectent. Cell infected by Listeria monocytogenes. The surface proteins (in blue) of Listeria enable us to view the bacteria. Actin, a constituent protein of cells, is shown in red and green.
Publication : Immunology letters

The SH2 domain-containing inositol 5-phosphatase SHIP1 is recruited to the intracytoplasmic domain of human FcgammaRIIB and is mandatory for negative regulation of B cell activation

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Immunology letters - 19 Dec 2005

Isnardi I, Bruhns P, Bismuth G, Fridman WH, Daëron M

Link to Pubmed [PMID] – 16406061

Immunol. Lett. 2006 Apr;104(1-2):156-65

Murine FcgammaRIIB were demonstrated to recruit SH2 domain-containing inositol 5-phosphatases (SHIP1/2), when their ITIM is tyrosyl-phosphorylated upon co-aggregation with BCR, and SHIP1 to account for FcgammaRIIB-dependent negative regulation of murine B cell activation. Although human FcgammaRIIB share the same ITIM as murine FcgammaRIIB and similarly inhibit human B cell activation, which among the four known SH2 domain-containing (tyrosine or inositol) phosphatases is/are recruited by human FcgammaRIIB is unclear. Our recent finding that, besides the ITIM, a second tyrosine-based motif is mandatory for murine FcgammaRIIB to recruit SHIP1 challenged the possibility that human FcgammaRIIB recruit this phosphatase. Human FcgammaRIIB indeed lack this motif. Using an experimental model which enabled us to compare human FcgammaRIIB and murine FcgammaRIIB under strictly controlled conditions, we show that SHIP1 is recruited to the intracytoplasmic domain of human FcgammaRIIB and inhibits the same biological responses and intracellular signals as when recruited by murine FcgammaRIIB. Identical results were observed in murine and in human B cells. We demonstrate that SHIP is necessary for human FcgammaRIIB to inhibit BCR signaling, and cannot be replaced by SHP-1 or SHP-2. Although it contains no tyrosine, the C-terminal segment of human FcgammaRIIB was as mandatory as the tyrosine-containing C-terminal segment of murine FcgammaRIIB for SHIP1 to be recruited to the ITIM. This segment, however, did not recruit the adapters Grb2/Grap which were demonstrated to stabilize the recruitment of SHIP1 to the ITIM in murine FcgammaRIIB.

http://www.ncbi.nlm.nih.gov/pubmed/16406061