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bunton33 bunton33
wrote...
13 years ago
A molecular biologist fiddled with the gene for a plasma membrane integral membrane protein (IMP) that acts as receptor for a ligand. This ligand-receptor pair participates in receptor-mediated endocytosis. When the normal gene of a mouse was replaced (ie, there was no normal activity) by the experimentally altered gene it was found that the consequences of ligand binding to the receptor were different from normal. In normal cells, the receptors disappeared from the PM following ligand binding and no more receptors could be found on the cells’ PMs for at least 6 hours. In the engineered cells, however, the receptor reappears on the PM within 5 minutes of endocytosis. When the researcher examined the receptor carefully, it was found that only a single amino acid was changed and that this amino acid was located in the cytosolic domain of the integral membrane protein.

Hypothesize how this single amino acid change could have such a profound effect on the cells. Be sure to defend your hypothesis.
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Valued Member
13 years ago
Well, what have you gotten thus far? We should build on each other's knowledge.

The structural elements involved in regulation or receptor activity are generally located in the cytosolic domain. There are, above all, protein sequences that permit phosphorylation of the receptor by protein kinases. Phosphorylation at Ser/Thr or Tyr residues of the cytosolic domain may lead to inactivation or activation of the receptor and thus weaken or strength signal transmission. In this way, Ser/Thr-phosphorylation is used in the process of internalization of receptors in order to remove the receptor from circulation after it has been activated. The protein kinases involved are often part of other signaling pathways and can link the activity of the transmembrane receptors to other signal networks.

Targeted degradation of receptors is another means of regulating receptor activity. Signals for ubiquitination and subsequent degradation in the proteosome has been identify in the cytosolic domain of transmembrane receptors. A major mechanism of targeting transmembrane receptors fro proteolysis uses signal-directed phosphorylation of the cytosolic domain.
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