Final answer:
A tyrosine kinase receptor can simultaneously trigger several cellular responses by forming a dimer when signaling molecules bind. Phosphate groups are then attached to tyrosine residues, initiating cellular responses. These responses are later terminated by phosphatases removing the phosphate groups.
Step-by-step explanation:
A tyrosine kinase receptor is different from a G-protein linked receptor in that it can trigger multiple cellular responses at the same time. When both signaling molecules are in their receptor sites, the molecules form a dimer – two molecules joined together. ATP is converted to ADP and the phosphate groups get attached to the tyrosine molecules. The addition of the phosphate groups causes a cascade of cellular responses.
Understanding Tyrosine Kinase Receptors :
Receptor tyrosine kinases are enzyme-linked receptors that have a crucial role in cellular signaling. They possess a single helical transmembrane region, with extracellular and intracellular domains. Upon binding of a signaling molecule, such as growth factors like Epidermal Growth Factor (EGF), to the extracellular domain, the receptor undergoes dimerization. This activates the intracellular kinase domains, which then transfer phosphate groups from ATP to tyrosine residues on the receptor itself, a process known as autophosphorylation. These phosphorylated tyrosine residues then serve as docking sites for other signaling proteins within the cell, which in turn trigger downstream cellular responses such as cell division, differentiation, or apoptosis. When the signaling needs to be terminated, phosphatases remove the phosphate groups from the phosphotyrosine residues, thus ending the cellular response.