How would you design an experiment to test whether M-CSF growth factor receptor signaling is dependent on dimerization of the receptor?

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Patrina SchowalterLv2

4 Nov 2018

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EGFR (epidermal growth factor receptor) has been intensivelystudied in cancer and treatments have been developed to inhibitEGFR signaling. Sialylation of EGFR is known to block dimerizationand down regulate signaling. I just read this paper:

Liu et al. 2011. Sialylation and fucosylation of epidermalgrowth factor receptor suppress its dimerization and activation inlung cancer cells. PNAS 108: 11332

A certain mutation in the receptor for epidermal growth factor (EGF) causes the mutated receptor protein to send a positive signal along the associated intracellular signaling pathway even when the EGF ligand is not bound to it. This signal leads to abnormal cell proliferation in the absence of growth factor. On the basis of this information, would you class the gene for the EGF receptor as a tumor suppressor gene or a potential oncogene? Explain your answer.

salmonox645

The EGF-receptor is a receptor tyrosine kinase that binds toepidermal growth factor (EGF). In response to EGF binding, theEGF-receptor stimulates a signaling pathway that involves Ras.Ultimately, this signaling pathway leads to the upregulation offactors that promote cell division. As a result, in response toEGF, cells that express the EGF-receptor undergo cell division toproduce more cells. If an inhibitor that inhibited all G proteinswas added to cells, how would this affect the ability of thesecells to respond to EGF?

1)The inhibitor would have no effect, because the EGF-receptoris not a G protein-coupled receptor.

2)While the receptor would dimerize and autophosphorylate in thepresence of the inhibitor, downstream signaling would be preventedbecause the inhibitor would affect Ras activity.

3)In the presence of the inhibitor, the receptor could bind toEGF and dimerize, but it would not be able to autophosphorylatebecause this requires the activity of a G protein.