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Insulin Receptor: Structure and Function

Wellcome Research Laboratories Research Triangle Park, North Carolina 27514

Correspondence: Address requests for reprints to: Dr. Steven Jacobs, Wellcome Research Laboratories, 3030 Cornwallis Road, Research Triangle Park, North Carolina 27514.

Abstract

INSULIN receptor has been purified by affinity chromatography and studied by affinity labeling techniques. It is composed of two types of subunits, (molecular weight 135,000) and β (molecular weight 90,000), which form a disulfide-linked heterotetramer (β)₂. Both - and β-subunits are glycoproteins. Both are exposed on the outer surface of the membrane, a is the subunit that is predominantly affinity labeled by insulin and is probably the insulin-binding subunit; however, β may also comprise a portion of the insulin-binding site.

Receptors for insulin-like growth factors have also been affinity labeled. A photoaffinity labeling derivative of basic somatomedin affinity labels a protein with a subunit structure very similar to the insulin receptor. In contrast, multiplication-stimulating activity is affinity cross-linked to a protein with an entirely different subunit structure. After binding to cell surface receptors, insulin, along with its receptor, is internalized by an endocytic process, which in some cells involves coated pits.

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