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Explain protein phosphorylation as molecular switches.A.
In one major class of switch protein, the phosphate is added covalently by a protein kinase, which transfers the terminal phosphate group from ATP to the signaling protein; the phosphate is then removed by a protein phosphatase.
B.
The activity of any protein that is regulated by phosphorylation depends—moment by moment—on the balance between the activities of the protein kinases that phosphorylate it and the protein phosphatases that dephosphorylate it.
C.
Many of the switch proteins controlled by phosphorylation are themselves protein kinases, and these are often organized into phosphorylation cascades: one protein kinase, activated by phosphorylation, phosphorylates the next protein kinase in the sequence, and so on, transmitting the signal onward and, in the process, amplifying, distributing, and regulating it.
D.
Two main types of protein kinases operate in intracellular signaling pathways: the most common are serine/threonine kinases, which—as the name implies—phosphorylate proteins on serines or threonines; others are tyrosine kinases, which phosphorylate proteins on tyrosine.
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