title: The 3D structure of protein phosphatase 2A: new insights into a ubiquitous regulator of cell signaling.
abstract: Protein phosphatase 2A (PP2A) is a serine/threonine phosphatase implicated in cancer. Three new crystal structures of PP2A show how it interacts with inhibitory toxins and with one of its regulatory subunits. The structures also explain how specific site mutations may lead to cancer and suggest a novel role for PP2A methylation in the formation of PP2A holoenzymes.
authors.affiliation: Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA. marc.mumby@utsouthwestern.edu
authors.forename: Marc
authors.initials: M
authors.lastname: Mumby
mesh_terms: D019943:Amino Acid Substitution; D018360:Crystallography, X-Ray; D020035:Holoenzymes; D006801:Humans; D008745:Methylation; D009369:Neoplasms / Q000209:etiology / Q000235:genetics; D009676:Noxae / Q000494:pharmacology; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D054648:Protein Phosphatase 2; D021122:Protein Subunits; D015398:Signal Transduction
chemical_list: D020035:Holoenzymes; D009676:Noxae; D021122:Protein Subunits; D010749:Phosphoprotein Phosphatases; D054648:Protein Phosphatase 2