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
Language
- eng
Conference Location
- United States