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|Title:||From Promiscuity to Precision: Protein Phosphatases Get a Makeover||Authors:||Virshup, D.M.
|Issue Date:||13-Mar-2009||Citation:||Virshup, D.M., Shenolikar, S. (2009-03-13). From Promiscuity to Precision: Protein Phosphatases Get a Makeover. Molecular Cell 33 (5) : 537-545. ScholarBank@NUS Repository. https://doi.org/10.1016/j.molcel.2009.02.015||Abstract:||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. © 2009 Elsevier Inc. All rights reserved.||Source Title:||Molecular Cell||URI:||http://scholarbank.nus.edu.sg/handle/10635/133023||ISSN:||10972765||DOI:||10.1016/j.molcel.2009.02.015|
|Appears in Collections:||Staff Publications|
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