title: S-Nitrosylation of p47(phox) enhances phosphorylation by casein kinase 2.
abstract: OBJECTIVE
  Leukocyte NADPH oxidase, which is active in neutrophils, is a membrane-bound enzyme that catalyzes the reduction of oxygen to O2(-) by using NADPH as an electron donor. Previously, we reported that casein kinase 2 (CK2), a ubiquitous and highly conserved Ser/Thr kinase, is responsible for p47(phox) phosphorylation and that phosphorylation of p47(phox) by CK2 regulates the deactivation of NADPH oxidase.
  
  
  METHODS
  Here, we report that the residue Cys(196) of p47(phox) is a target of S-nitrosylation by S-nitrosothiol and peroxynitrite and that this modification enhanced phosphorylation of p47(phox) by CK2.
  
  
  RESULTS
  S-Nitrosylated p47(phox) enhanced CK2 b subunit binding, presumably due to alterations in protein conformation.
  
  
  CONCLUSIONS
  Taken together, we propose that S-nitrosylation of p47(phox) regulates the deactivation of NADPH oxidase via enhancement of p47(phox) phosphorylation by CK2.
authors.forename: In Sup
authors.initials: IS
authors.lastname: Kil
authors.forename: Jin Hyup
authors.initials: JH
authors.lastname: Lee
authors.forename: Soo Hyun
authors.initials: SH
authors.lastname: Yoon
authors.forename: Young Seuk
authors.initials: YS
authors.lastname: Bae
authors.forename: Seontae
authors.initials: S
authors.lastname: Kim
authors.forename: Seoung Woo
authors.initials: SW
authors.lastname: Shin
authors.forename: Jeen-Woo
authors.initials: JW
authors.lastname: Park
mesh_terms: D047390:Casein Kinase II / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D019255:NADPH Oxidases / Q000737:chemistry / Q000378:metabolism; D010766:Phosphorylation; D011487:Protein Conformation; D026403:S-Nitrosothiols / Q000378:metabolism
chemical_list: D026403:S-Nitrosothiols; D019255:NADPH Oxidases; D047390:Casein Kinase II
keywords: Conformational change; Deactivation; NADPH oxidase; Nitrosylation; SH3 domains