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

S Amigorena, C Bonnerot, Drake, D Choquet, W Hunziker, J. Guillet, P Webster, C Sautes, I Mellman, W. Fridman
Science. 1992-06-26; 256(5065): 1808-1812
DOI: 10.1126/science.1535455

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1. Science. 1992 Jun 26;256(5065):1808-12.

Cytoplasmic domain heterogeneity and functions of IgG Fc receptors in B

Amigorena S(1), Bonnerot C, Drake JR, Choquet D, Hunziker W, Guillet JG, Webster
P, Sautes C, Mellman I, Fridman WH.

Author information:
(1)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.

DOI: 10.1126/science.1535455
PMID: 1535455 [Indexed for MEDLINE]

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