Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.molcel.2009.02.015
Title: From Promiscuity to Precision: Protein Phosphatases Get a Makeover
Authors: Virshup, D.M. 
Shenolikar, S.
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

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

383
checked on Nov 14, 2018

WEB OF SCIENCETM
Citations

367
checked on Nov 14, 2018

Page view(s)

27
checked on Nov 1, 2018

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.