Abstract
Methods and reagents developed during the late 1970s have led to significant new insights into the protein structure of the insulin receptor over the past five years. The importance of this information resides in the presumption that the insulin receptor initiates all the biological responses mediated by the hormone and therefore that its structure must contain key information related to cellular signaling mechanisms. Because the mechanism of insulin action is still not understood, this assumption has not yet been proved. However, the data available are fully consistent with this view. Furthermore, it is probable that the insulin receptor, like many other receptor systems, contains structural information that catalyzes other functions such as desensitization of the insulin response and transport of insulin to or among various cellular compartments, as well as its own recycling from intracellular compartments to the cell-surface membrane. It seems reasonable to assume that various receptor domains participate both specifically and directly in these various biological functions. It follows that an important future objective in this field is to obtain the primary sequence and general protein structure of this receptor in order to better define the biochemical mechanisms by which the insulin receptor fulfills its various functions.
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Pessin, J.E., Mottola, C., Yu, KT., Czech, M.P. (1985). Subunit Structure and Regulation of the Insulin-Receptor Complex. In: Czech, M.P. (eds) Molecular Basis of Insulin Action. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-4874-0_1
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