From promiscuity to precision: protein phosphatases get a makeover.
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.
Virshup
David M
DM
Program in Cancer and Stem Cell Biology, Duke-NUS Graduate Medical School Singapore, Singapore, Republic of Singapore. david.virshup@duke-nus.edu.sg
Shenolikar
Shirish
S
D000818:Animals; D020134:Catalytic Domain; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000378:metabolism*; D007527:Isoenzymes; D008958:Models, Molecular; D010749:Phosphoprotein Phosphatases / Q000737:chemistry / Q000378:metabolism*; D010766:Phosphorylation; D011487:Protein Conformation; D054645:Protein Phosphatase 1 / Q000378:metabolism; D054648:Protein Phosphatase 2 / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D015398:Signal Transduction; D013379:Substrate Specificity; D016212:Transforming Growth Factor beta / Q000378:metabolism; D016875:tau Proteins / Q000378:metabolism
D047908:Intracellular Signaling Peptides and Proteins; D007527:Isoenzymes; D016212:Transforming Growth Factor beta; D016875:tau Proteins; D010749:Phosphoprotein Phosphatases; D054645:Protein Phosphatase 1; D054648:Protein Phosphatase 2; C080406:protein phosphatase 4