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Science 26 June 1992:
Vol. 256. no. 5065, pp. 1808 - 1812
DOI: 10.1126/science.1535455

Articles

Science, Vol 256, Issue 5065, 1808-1812
Copyright © 1992 by American Association for the Advancement of Science


articles

Cytoplasmic domain heterogeneity and functions of IgG Fc receptors in B lymphocytes

S Amigorena, C Bonnerot, Drake JR, D Choquet, W Hunziker, JG Guillet, P Webster, C Sautes, I Mellman, and WH Fridman

Laboratoire d'Immunologie Cellulaire et Clinique, INSERM U 255, Institut Curie, Paris, France.

B lymphocytes and macrophages express closely related immunoglobulin G (IgG) Fc receptors (Fc gamma RII) that differ only in the structures of their cytoplasmic domains. Because of cell type-specific alternative messenger RNA splicing, B-cell Fc gamma RII contains an insertion of 47 amino acids that participates in determining receptor function in these cells. Transfection of an Fc gamma RII-negative B-cell line with complementary DNA's encoding the two splice products and various receptor mutants indicated that the insertion was responsible for preventing both Fc gamma RII-mediated endocytosis and Fc gamma RII-mediated antigen presentation. The insertion was not required for Fc gamma RII to modulate surface immunoglobulin-triggered B-cell activation. Instead, regulation of activation involved a region of the cytoplasmic domain common to both the lymphocyte and macrophage receptor isoforms. In contrast, the insertion did contribute to the formation of caps in response to receptor cross-linking, consistent with suggestions that the lymphocyte but not macrophage form of the receptor can associate with the detergent-insoluble cytoskeleton.


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R. Lesourne, P. Bruhns, W. H. Fridman, and M. Daeron (2001)
J. Biol. Chem. 276, 6327-6336
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Src Homology 2 Domain-containing Inositol 5-Phosphatase 1 Mediates Cell Cycle Arrest by Fcgamma RIIB.
O. Malbec, C. Schmitt, P. Bruhns, G. Krystal, W. H. Fridman, and M. Daeron (2001)
J. Biol. Chem. 276, 30381-30391
   Abstract »    Full Text »    PDF »
The AP2 binding site of synaptotagmin 1 is not an internalization signal but a regulator of endocytosis.
N. Jarousse and R. B. Kelly (2001)
J. Cell Biol. 154, 857-866
   Abstract »    Full Text »    PDF »



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