Question

What do both G protein-coupled receptors and tyrosine kinase receptors have in common?

The binding site for the signaling molecule is located on the outside of the cell.
		They both interact with G proteins.
		Binding of the signaling molecule forms a dimer.
		They both result in a phosphorylation cascade.

Answer 1

Both G-protein coupled receptor and Tyrosine kinase receptors are the transmembrane proteins, with each protein composed of three distinct domains:

1. Extracellular domain (N-terminal)

2. Transmembrane hydrophobic domain (which spans through the membrane)

3. Intracellular or cytoplasmic domain (C-terminal).

For both the receptors, there are ligand binding sites in the extracellular domain (which bind to different ligands to elicite a specific cellular response) and the binding of these ligands induce the conformational changes in the transmembrane domain (in case or GPCR) or dimerization of two Tyrosine kinase receptors leading to autophsphorylation of Tyrosine residues within the receptor (in case of Tyrosine kinase receptor) which then activates the C-terminal or cytoplasmic domain to initiate as signalling cascade inside the cell. Although the mechanism of signal transduction is different in both th receptors, both these receptors communicate externally with the ligand and transmit the signal to intracellular components.

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