The Ku70 autoantigen interacts with p40phox in B lymphocytes
| Autor: | Grandvaux N, Grizot S, Pv, Vignais, Marie-Claire DAGHER |
|---|---|
| Přispěvatelé: | Dagher, Marie-Claire, Biochimie et biophysique des systèmes intégrés (BBSI), Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 1999 |
| Předmět: |
Cytoplasm
Fluorescent Antibody Technique MESH: DNA Helicases DNA-Activated Protein Kinase Autoantigens [SDV.IMM.II]Life Sciences [q-bio]/Immunology/Innate immunity MESH: Saccharomyces cerevisiae Proteins 0302 clinical medicine MESH: Animals Phosphorylation MESH: NADPH Oxidase MESH: Fluorescent Antibody Technique B-Lymphocytes 0303 health sciences Nuclear Proteins Antigens Nuclear MESH: Saccharomyces cerevisiae DNA-Binding Proteins MESH: COS Cells MESH: Autoantigens COS Cells Subcellular Fractions MESH: Cell Nucleus DNA Complementary Saccharomyces cerevisiae Proteins Recombinant Fusion Proteins Saccharomyces cerevisiae Protein Serine-Threonine Kinases Transfection MESH: Phosphoproteins MESH: Protein-Serine-Threonine Kinases 03 medical and health sciences MESH: B-Lymphocytes MESH: Recombinant Fusion Proteins Animals Humans Ku Autoantigen MESH: Antigens Nuclear [SDV.IMM.II] Life Sciences [q-bio]/Immunology/Innate immunity 030304 developmental biology Cell Nucleus Binding Sites MESH: Humans MESH: Phosphorylation MESH: Transfection MESH: Cytoplasm DNA Helicases NADPH Oxidases MESH: DNA Complementary Cell Biology Phosphoproteins MESH: Binding Sites MESH: Subcellular Fractions MESH: DNA-Activated Protein Kinase MESH: Nuclear Proteins MESH: DNA-Binding Proteins 030217 neurology & neurosurgery |
| Zdroj: | Journal of Cell Science Journal of Cell Science, Company of Biologists, 1999, 112 ( Pt 4), pp.503-13 Journal of Cell Science, 1999, 112 ( Pt 4), pp.503-13 Europe PubMed Central |
| ISSN: | 0021-9533 1477-9137 |
| Popis: | International audience; Ku70, a regulatory component of the DNA-dependent protein kinase, was identified by a yeast two-hybrid screen of a B lymphocyte cDNA library as a partner of p40phox, a regulatory component of the O2--producing NADPH oxidase. Truncated constructs of p40phox and Ku70 were used to map the interacting sites. The 186 C-terminal amino acids (aa) of Ku70 were found to interact with two distinct regions of p40phox, the central core region (aa 50-260) and the C-terminal extremity (aa 260-339). In complementary experiments, it was observed that Ku70 binds to immobilized recombinant p40phox fusion protein and that p40phox and Ku70 from a B lymphocyte cell extract comigrate in successive chromatographies on Q Separose, Superose 12 and hydroxylapatite columns. Moreover, we report that Ku70 and p40phox colocalize in B lymphocytes and in transfected Cos-7 cells. We also show that the two NADPH oxidase activating factors, p47phox and p67phox are substrates for DNA-PK in vitro and that they are present together with p40phox in the nucleus of B cells. These results may help solve the paradox that the phox protein triad, p40phox, p47phox and p67phox, is expressed equally in B lymphocytes and neutrophils, whereas the redox component of the NADPH oxidase, a flavocytochrome b, which is well expressed in neutrophils, is barely detectable in B lymphocytes. |
| Databáze: | OpenAIRE |
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