title: Structural basis for protein phosphatase 1 regulation and specificity.
abstract: The ubiquitous serine/threonine protein phosphatase 1 (PP1) regulates diverse, essential cellular processes such as cell cycle progression, protein synthesis, muscle contraction, carbohydrate metabolism, transcription and neuronal signaling. However, the free catalytic subunit of PP1, while an effective enzyme, lacks substrate specificity. Instead, it depends on a diverse set of regulatory proteins (≥ 200) to confer specificity towards distinct substrates. Here, we discuss recent advances in structural studies of PP1 holoenzyme complexes and summarize the new insights these studies have provided into the molecular basis of PP1 regulation and specificity.
authors.affiliation: Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, RI 02912, USA. wolfgang_peti@brown.edu
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Peti
authors.forename: Angus C
authors.initials: AC
authors.lastname: Nairn
authors.forename: Rebecca
authors.initials: R
authors.lastname: Page
mesh_terms: D020134:Catalytic Domain; D020035:Holoenzymes / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008840:Microfilament Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D054645:Protein Phosphatase 1 / Q000737:chemistry* / Q000378:metabolism; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity; D000099273:Neurabins
chemical_list: D020035:Holoenzymes; D008840:Microfilament Proteins; D009419:Nerve Tissue Proteins; D054645:Protein Phosphatase 1; D021122:Protein Subunits; D000099273:Neurabins