Join thousands of students who trust us to help them ace their exams!Watch the first video
Multiple Choice
Which of the following is TRUE concerning the interaction between the insulin receptor and IRS-1:
A
The IRS protein phosphorylates the insulin receptor.
B
The β-subunits of the receptor bind to insulin, where each subunit has a separate insulin binding site.
C
Each β-subunit acts as a serine kinase and auto-phosphorylates the other subunit.
D
IRS is phosphorylated by the tyrosine kinase domains in the β-subunits of the insulin receptor.
E
IRS contains phosphorylated threonine residues that directly bind to insulin.
Verified step by step guidance
1
Understand the role of the insulin receptor: The insulin receptor is a transmembrane receptor that is activated by insulin. It is composed of two α-subunits and two β-subunits.
Identify the function of the β-subunits: The β-subunits of the insulin receptor have intrinsic tyrosine kinase activity, which means they can phosphorylate tyrosine residues on target proteins.
Clarify the role of IRS-1: IRS-1 (Insulin Receptor Substrate 1) is a key signaling molecule that becomes phosphorylated on tyrosine residues by the activated insulin receptor.
Examine the interaction between the insulin receptor and IRS-1: Upon insulin binding, the β-subunits of the receptor undergo autophosphorylation, which activates their kinase activity. This leads to the phosphorylation of IRS-1 on specific tyrosine residues.
Conclude the correct statement: The correct interaction is that IRS-1 is phosphorylated by the tyrosine kinase domains in the β-subunits of the insulin receptor, facilitating downstream signaling pathways.