Cytoplasmic Domain Heterogeneity and Functions of IgG Fc Receptors in B Lymphocytes

B lymphocytes and macrophages express closely related immunoglobulin G (IgG) Fc receptors (FcγRII) that differ only in the structures of their cytoplasmic domains. Because of cell type-specific alternative messenger RNA splicing, B-cell FcγRII contains an insertion of 47 amino acids that participate...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1992-06, Vol.256 (5065), p.1808-1812
Main Authors: Amigorena, Sebastian, Bonnerot, Christian, Drake, James R., Choquet, Daniel, Hunziker, Walter, Guillet, Jean-Gerard, Webster, Paul, Sautes, Catherine, Mellman, Ira, Fridman, Wolf Herman
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Antibodies
Antigen-Antibody Complex - metabolism
Antigen-Antibody Reactions - genetics
Antigen-Antibody Reactions - immunology
Antigens
Antigens, CD - genetics
Antigens, CD - immunology
Antigens, Differentiation - genetics
Antigens, Differentiation - immunology
B lymphocytes
B-Lymphocytes - immunology
Biological and medical sciences
Calcium - metabolism
Cell lines
Cell membranes
Cytoplasm
DNA-Binding Proteins
Dose-Response Relationship, Immunologic
Endocytosis
Endocytosis - genetics
Endocytosis - immunology
Fc receptors
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Humans
Immunobiology
Immunohistochemistry
Lymphocyte Activation - immunology
Lymphoid cells: ontogeny, maturation, markers, receptors, circulation and recirculation
Macrophages
Microscopy, Electron
Molecular Sequence Data
Protein isoforms
Receptors
Receptors, Fc - genetics
Receptors, Fc - immunology
Receptors, IgG
Repressor Proteins - pharmacology
T lymphocytes
Transcription Factors - pharmacology
Transfection
Viral Proteins
Viral Regulatory and Accessory Proteins
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Summary:B lymphocytes and macrophages express closely related immunoglobulin G (IgG) Fc receptors (FcγRII) that differ only in the structures of their cytoplasmic domains. Because of cell type-specific alternative messenger RNA splicing, B-cell FcγRII contains an insertion of 47 amino acids that participates in determining receptor function in these cells. Transfection of an FcγRII-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 FcγRII-mediated endocytosis and FcγRII-mediated antigen presentation. The insertion was not required for FcγRII 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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1535455