Insulin is released by the beta islets of the pancreas after a meal when glucose

Question

Insulin is released by the beta islets of the pancreas after a meal when glucose levels are high. Released as a peptide, insulin binds to a unique class of receptors that lead to the reduction of blood sugar levels. The insulin receptor has a tyrosine kinase intracellular domain. However, unlike many other similar single transmembrane receptors with a tyrosine kinase activity (such as growth factor receptors), the insulin receptor is a crosslinked dimer in the resting state made of two alpha and two beta strands (heterotetramer) Which of the following statements describe how the insulin receptor is activated? Choose one or more: A. Following insulin binding, the receptor will bind with another receptor as long as only one insulin peptide is B. The intracellular domain of the insulin receptor, specifically the tyrosines, must be phosphorylated to recruit C. An insulin receptor has two binding sites for insulin, and each ligand is required to begin bound. This is an example of a negative feedback cooperative regulation. the intracellular signaling partners. autophosphorylation. autophosphorylation of the beta subunits. D. Insulin binding to the insulin receptor induces a conformational change that stimulates tyrosine

Explanation / Answer

Insulin recepetor is activated: ans- (B) the intracellular domain of the insulin receptor, specifically the tyrosines, must be phosphorylated to recruit the intracellular signalling partners.

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