Structural Heterogeneity and Functional Domains of Murine Immunoglobulin G Fc Receptors

• Published in: Science (American Association for the Advancement of Science) Vol. 234; no. 4777; pp. 718 - 725
• Main Authors: Ravetch, Jeffrey V., Luster, Andrew D., Weinshank, Richard, Kochan, Jarema, Pavlovec, Amalia, Portnoy, Daniel A., Hulmes, Jeffrey, Pan, Yu-Ching E., Unkeless, Jay C.
• Format: Journal Article
• Language: English
• Published: Washington, DC The American Association for the Advancement of Science 07-11-1986; American Association for the Advancement of Science
• Subjects: Amino Acid Sequence; Amino acids; Analysis of the immune response. Humoral and cellular immunity; Animals; Base Sequence; Biochemistry; Biological and medical sciences; cDNA; Cell lines; Cell receptors; Complementary DNA; DNA - genetics; expression; Fundamental and applied biological sciences. Psychology; Fundamental immunology; Gene Expression Regulation; Genes; Genetics; Histocompatibility Antigens Class II - genetics; Immunobiology; Immunoglobulin G; Immunoglobulins; L cells; Lymphocytes; Lymphocytes - physiology; Macrophages; Macrophages - physiology; Medical research; Membrane Proteins; Mice; nucleotide sequence; Organs and cells involved in the immune response; Protein Conformation; Receptors; Receptors, Fc - genetics; Receptors, IgG; T lymphocytes; Transcription, Genetic; Transfection; Molecular structure; Nucleotide sequence; Rodentia; IgG; Gene expression; Signal transduction; Heterogeneity; Vertebrata; Membrane receptor; Mammalia; Transfection; Complementary DNA; Fc-Fragment; Mouse; Animal; T»-Lymphocyte; Macrophage
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.2946078

Binding of antibodies to effector cells by way of receptors to their constant regions (Fc receptors) is central to the pathway that leads to clearance of antigens by the immune system. The structure and function of this important class of receptors on immune cells is addressed through the molecular characterization of Fc receptors (FcR) specific for the murine immunoglobulin G isotype. Structural diversity is encoded by two genes that by alternative splicing result in expression of molecules with highly conserved extracellular domains and different transmembrane and intracytoplasmic domains. The proteins encoded by these genes are members of the immunoglobulin supergene family, most homologous to the major histocompatibility complex molecule E$_{\beta}$. Functional reconstitution of ligand binding by transfection of individual FcR genes demonstrates that the requirements for ligand binding are encoded in a single gene. These studies demonstrate the molecular basis for the functional heterogeneity of FcR's, accounting for the possible transduction of different signals in response to a single ligand.