EffektorDomäne

EffektorDomäne is a protein domain found in various proteins involved in immune response and inflammation regulation. It is characterized by a conserved sequence motif, typically located at the carboxy-terminal end of the protein. The domain is named after its role in mediating the interaction between immune receptors and their effectors, such as kinases and phosphatases.

The EffektorDomäne is composed of several subdomains, including the ITIM (immunoreceptor tyrosine-based inhibitory motif) and ITAM (immunoreceptor tyrosine-based activation motif) motifs. These motifs play crucial roles in the activation and inhibition of downstream signaling pathways. The ITAM motif, for example, can recruit and activate kinases like Syk, leading to the phosphorylation of various substrates and the initiation of immune responses. Conversely, the ITIM motif can recruit phosphatases, such as SHP-1, to dephosphorylate and inhibit signaling.

The EffektorDomäne is found in a wide range of immune receptors, including those belonging to the B-cell receptor (BCR) and T-cell receptor (TCR) families. In B cells, the EffektorDomäne of the BCR can mediate the activation of signaling pathways that lead to antibody production and immune response. In T cells, the EffektorDomäne of the TCR can initiate signaling cascades that result in cell proliferation, differentiation, and the release of cytokines.

Mutations in genes encoding proteins with EffektorDomäne have been linked to various immune-related disorders, such as autoimmune diseases and immunodeficiency syndromes. Understanding the structure and function of the EffektorDomäne is therefore important for comprehending immune system regulation and for developing therapeutic strategies targeting immune-related diseases.