Final answer:
The cytoplasmic domains in immune receptors that are phosphorylated are called Immunoreceptor Tyrosine-based Activation Motifs (ITAMs). They play a critical role in immune cell signaling by being phosphorylated upon antigen binding, initiating cellular responses through the intracellular domain.
Step-by-step explanation:
The portions of the cytoplasmic domains of many immune receptors that are targets for phosphorylation are known as Immunoreceptor Tyrosine-based Activation Motifs (ITAMs). These domains are essential in the signal transduction processes of immune cells. When immune receptors connect with their specific antigens, ITAMs are phosphorylated on tyrosine residues within the intracellular domain, which then triggers a downstream cellular response, such as cell activation, differentiation, or proliferation.
Receptor Tyrosine Kinase-Mediated Signal Transduction is a process that involves the phosphorylation of tyrosine residues on the cytoplasmic domain of the receptor, catalyzed by the receptor's intrinsic kinase activity upon binding to its effector. This phosphorylation of specific tyrosine amino acids in target proteins leads to various cellular responses. Such signaling pathways are common in cells' response to various signals, potentially leading to similar outcomes under different conditions.