Tyrosine Kinase Linked Receptors Deraya University Presented By Abdelfatah mahmoud Abdelfatah 1190245
Tyrosine kinase-linked receptors, also known as receptor tyrosine kinases (RTKs), are an important class of cell surface receptors that play crucial roles in many cellular processes. Introduction
RTKs are transmembrane proteins with three main domains: An extracellular ligand-binding domain A single transmembrane helix An intracellular tyrosine kinase domain They function as both receptors and enzymes, receiving signals from the environment and catalyzing intracellular reactions. Structure and Function
Ligand binding : Growth factors, hormones, or other signaling molecules bind to the extracellular domain. Receptor dimerization : Ligand binding causes two receptor monomers to come together and form a dimer. Autophosphorylation : The intracellular kinase domains phosphorylate tyrosine residues on each other. Signaling complex assembly : The phosphorylated tyrosines serve as docking sites for intracellular signaling proteins. Activation Mechanism
RTKs activate several major signaling cascades, including: MAP kinase pathway Phosphoinositide 3-kinase pathway STAT pathway These pathways ultimately lead to changes in gene expression and cellular behavior. Signaling Pathways
RTKs regulate critical cellular processes such as: Cell growth and division Differentiation Survival Metabolism Migration Dysregulation of RTK signaling is implicated in many diseases, especially cancers. Understanding RTK mechanisms has led to the development of targeted cancer therapies Biological Roles
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