Biochemistry
Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Chapter 14, Problem 15P
Interpretation Introduction

Interpretation:

Action of insulin binding and EGF binding on the chimeric receptor should be determined.

Concept introduction:

The cell-surface receptors for EGF and insulin are thought to have the same origin because of the similarity in cysteine-rich residues in their EC domains. Moreover, they both have tyrosine kinase domains. The only difference is found in their catalytic site, which is specific for ligands and biological functions.

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In expressing therapeutic proteins (check all that apply): O Bacteria could be used if you want the protein's disulfide bonds formed before secretion from the bacterial cell. The N-terminal signal sequence and the C chain of insulin must be cleaved off in the rough ER before it's active. O Proteolytic protein maturation can be performed by mammalian cells. □ One of the required modifications to preproinsulin, before it's mature, is glycosylation. Both preproinsulin and proinsulin are inactive proteins.
Suppose that, through genetic manipulations, a chimeric receptor is produced that consists of the extracellular domain of the insulin receptor and the transmembrane and intracellular domains of the EGF receptor. Cells expressing this receptor are exposed to insulin, and the level of phosphorylation of the chimeric receptor is examined. What would you expect to observe and why? What would you expect to observe if these cells were exposed to EGF?
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