From Promiscuity to Precision: Protein Phosphatases Get a Makeover Export

@article{citeulike:4278089, 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.}, author = {Virshup, David M. and Shenolikar, Shirish}, citeulike-article-id = {4278089}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.molcel.2009.02.015}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S1097276509001312}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/19285938}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=19285938}, doi = {10.1016/j.molcel.2009.02.015}, issn = {10972765}, journal = {Molecular Cell}, keywords = {phosphatase, review, specificity, substrate}, month = {March}, number = {5}, pages = {537--545}, posted-at = {2009-07-02 03:31:36}, priority = {2}, title = {From Promiscuity to Precision: Protein Phosphatases Get a Makeover}, url = {http://dx.doi.org/10.1016/j.molcel.2009.02.015}, volume = {33}, year = {2009} }

TY - JOUR ID - citeulike:4278089 L3 - citeulike-article-id:4278089 N2 - 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. IS - 5 JF - Molecular Cell SN - 10972765 EP - 545 TI - From Promiscuity to Precision: Protein Phosphatases Get a Makeover VL - 33 SP - 537 KW - phosphatase KW - review KW - specificity KW - substrate AU - Virshup, David AU - Shenolikar, Shirish PY - 2009/03/13/ UR - http://dx.doi.org/10.1016/j.molcel.2009.02.015 ER -