What are Serine/Theonine phosphatases?
Definition: Serine/Theonine phosphatases are metal-requiring enzymes that regulate many pathways involved in cell proliferation, programmed cell death (apoptosis), embryonic development, and cell differentiation.
Reversible protein phosphorylation is widely used by cells to either propagate or terminate intracellular signal transduction pathways. The addition or removal of a negatively charged phosphate can influence the size, charge and conformation of a protein and/or its interactions with other proteins.
Whereas kinases use ATP to phosphorylate amino acid side chains in target proteins, phosphatases hydrolyse phosphates off these residues. Kinases and phosphatases work in concert to switch the function of a protein on or off and so are essential for homeostatic balance of cell signalling. Phosphatases have been characterized as having activity toward serine and threonine residues, or toward tyrosine residues.
Serine/Theonine phosphatases are grouped into two gene families, the PPP and the PPM gene families, based on sequence analysis.
PPP Gene family
The PP1 subfamily is comprised of a catalytic subunit that interacts with several proteins including targeting subunits and inhibitor proteins. The PP2A subfamily are heterotrimers comprised of a catalytic subunit and two regulatory subunits.
PPM Gene Family
This group corresponds to the PP2C enzymes, which are activated by high concentrations of Mg. This subfamily is less well studied that the PPP group, and little is known about their regulation.
Many phosphatases are key in the development of pathological pathways where inhibition can reverse or delay the onset of human diseases. Abnormal serine/threonine phosphatase activity has been linked with several diseases, including diabetes, cardiovascular disorders, cancer, and Alzheimer's disease. Therefore, the pharmacological manipulation of phosphatase activity is an attractive strategy for the treatment of such conditions.
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