What is Immunoglobulins Superfamily (IgSF)?
Immunoglobulin superfamily (IgSF) is a family of proteins widely present in various organisms, and its members have similar structural domains and functions. Proteins of this family typically consist of a series of repeating immunoglobulin domains joined by two beta sheets (beta sheets). The immunoglobulin superfamily plays a variety of important biological functions in the body.
In the immune system, members of the immunoglobulin superfamily include immunoglobulins (antibodies), T cell receptors, and many ligand receptor molecules. These proteins bind to antigens or ligands through their structural domains, thereby regulating the immune response of the body. Members of the immunoglobulin superfamily play key roles in antigen recognition, activation and regulation of immune cells, and the formation of immune memory.
In addition to the immune system, members of the immunoglobulin superfamily play important roles in processes such as the nervous system, cell adhesion, and cell migration. For example, the immunoglobulin superfamily proteins on the surface of nerve cells are responsible for mutual recognition and adhesion between neurons, and promote neuron migration and synapse formation. In addition, immunoglobulin superfamily proteins are also involved in processes such as cell-cell adhesion, cell-cell interaction, and cell-matrix interaction.
Fig.1 Schematic diagram showing examples of the structure of IGSF CAMS and their links to the cytoskeleton components. [1]
Research Field of the Immunoglobulin Superfamily
Immunoglobulin superfamily (IgSF) is a widely studied field, involving many different research directions and application fields. The following are some of the areas of study of the immunoglobulin superfamily:
- Immunology research: Members of the immunoglobulin superfamily play an important role in the body's immune response. Researchers study the structure, function, and regulation of members of the immunoglobulin superfamily to gain insight into the mechanisms of immune responses, immune cell interactions, and the development and treatment of immune-related diseases.
- Neuroscience research: Members of the immunoglobulin superfamily play an important role in the nervous system and participate in processes such as recognition between neurons, synapse formation, and synaptic transmission. By studying the functions and interactions of these proteins, researchers explore the mechanisms of nervous system development, synaptic plasticity, and neurodegenerative diseases.
- Research on cell adhesion and migration: Cell adhesion molecules in the immunoglobulin superfamily play an important role in the process of mutual recognition, adhesion and migration between cells. By studying the structure and function of these proteins, researchers reveal the mechanism of cell adhesion and understand processes such as cell migration, tissue formation and development.
- Tumor immunotherapy: members of the immunoglobulin superfamily are of great significance in tumor immunotherapy. Researchers use the specific binding ability of members of the immunoglobulin superfamily to develop CAR-T cell therapy and other immunotherapies to enhance the immune system's ability to attack tumor cells.
- Drug development and therapeutic targets: members of the immunoglobulin superfamily, as proteins on the cell surface, are widely used in drug development and therapeutic target research. By studying the structure and function of these proteins, researchers search for new drug targets and design and develop drugs against members of the immunoglobulin superfamily for the treatment of immune-related diseases and other diseases.
Antigen Receptor Accessory Molecules
MHC Class I
MHC Class II
Co-receptors
Other Immunoglobulins
IgSF CAMs
Co-stimulatory/inhibitory Molecules
Growth Factor Receptors
Receptor Tyrosine Kinases
References:
[1] Leshchyns'ka I, Sytnyk V. Reciprocal Interactions between Cell Adhesion Molecules of the Immunoglobulin Superfamily and the Cytoskeleton in Neurons. Front Cell Dev Biol. 2016;4:9. Published 2016 Feb 16. doi:10.3389/fcell.2016.00009 https://pubmed.ncbi.nlm.nih.gov/26909348/
