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Mol Cell. 2009 Mar 13;33(5):537-45. doi: 10.1016/j.molcel.2009.02.015.

From promiscuity to precision: protein phosphatases get a makeover.

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Program in Cancer and Stem Cell Biology, Duke-NUS Graduate Medical School Singapore, Singapore, Republic of Singapore.


The control of biological events requires strict regulation using complex protein phosphorylation and dephosphorylation strategies. The bulk of serine-threonine dephosphorylations are catalyzed by a handful of phosphatase catalytic subunits, giving rise to the misconception that these phosphatases are promiscuous and unregulated enzymes in vivo. The reality is much more nuanced: PP1 and PP2A, the most abundant serine-threonine phosphatases, are, in fact, families of hundreds of protein serine/threonine phosphatases, assembled from a few catalytic subunits in combination with a highly diverse array of regulators. As recent publications illustrate, these regulatory subunits confer specificity, selectivity, localization, and regulation on these important enzymes.

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