From promiscuity to precision: protein phosphatases get a makeover.

Journal Article (Journal Article;Review)

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.

Full Text

Duke Authors

Cited Authors

  • Virshup, DM; Shenolikar, S

Published Date

  • March 13, 2009

Published In

Volume / Issue

  • 33 / 5

Start / End Page

  • 537 - 545

PubMed ID

  • 19285938

Electronic International Standard Serial Number (EISSN)

  • 1097-4164

Digital Object Identifier (DOI)

  • 10.1016/j.molcel.2009.02.015


  • eng

Conference Location

  • United States