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Cell cycle-dependent gene networks for cell proliferation activated by nuclear CK2α complexes.
Homma, Miwako Kato; Nakato, Ryuichiro; Niida, Atsushi; Bando, Masashige; Fujiki, Katsunori; Yokota, Naoko; Yamamoto, So; Shibata, Takeshi; Takagi, Motoki; Yamaki, Junko; Kozuka-Hata, Hiroko; Oyama, Masaaki; Shirahige, Katsuhiko; Homma, Yoshimi.
Afiliación
  • Homma MK; Department of Biomolecular Sciences, Fukushima Medical University School of Medicine, Fukushima, Japan mkhomma@fmu.ac.jp.
  • Nakato R; Laboratory of Computational Genomics, Institute for Quantitative Biosciences, University of Tokyo, Bunkyo, Japan.
  • Niida A; Human Genome Center, The Institute of Medical Science, The University of Tokyo, Minato, Japan.
  • Bando M; Institute for Quantitative Biosciences, The University of Tokyo, Bunkyo, Japan.
  • Fujiki K; Institute for Quantitative Biosciences, The University of Tokyo, Bunkyo, Japan.
  • Yokota N; Laboratory of Computational Genomics, Institute for Quantitative Biosciences, University of Tokyo, Bunkyo, Japan.
  • Yamamoto S; Department of Biomolecular Sciences, Fukushima Medical University School of Medicine, Fukushima, Japan.
  • Shibata T; K.K. ABSciex, Shinagawa, Japan.
  • Takagi M; Translational Research Center, Fukushima Medical University School of Medicine, Fukushima, Japan.
  • Yamaki J; Department of Biomolecular Sciences, Fukushima Medical University School of Medicine, Fukushima, Japan.
  • Kozuka-Hata H; Medical Proteomics Laboratory, The Institute of Medical Science, The University of Tokyo, Minato, Japan.
  • Oyama M; Medical Proteomics Laboratory, The Institute of Medical Science, The University of Tokyo, Minato, Japan.
  • Shirahige K; Institute for Quantitative Biosciences, The University of Tokyo, Bunkyo, Japan.
  • Homma Y; Department of Biosciences and Nutrition, Karolinska Institutet, Biomedicum, Stockholm, Sweden.
Life Sci Alliance ; 7(1)2024 01.
Article en En | MEDLINE | ID: mdl-37907238
ABSTRACT
Nuclear expression of protein kinase CK2α is reportedly elevated in human carcinomas, but mechanisms underlying its variable localization in cells are poorly understood. This study demonstrates a functional connection between nuclear CK2 and gene expression in relation to cell proliferation. Growth stimulation of quiescent human normal fibroblasts and phospho-proteomic analysis identified a pool of CK2α that is highly phosphorylated at serine 7. Phosphorylated CK2α translocates into the nucleus, and this phosphorylation appears essential for nuclear localization and catalytic activity. Protein signatures associated with nuclear CK2 complexes reveal enrichment of apparently unique transcription factors and chromatin remodelers during progression through the G1 phase of the cell cycle. Chromatin immunoprecipitation-sequencing profiling demonstrated recruitment of CK2α to active gene loci, more abundantly in late G1 phase than in early G1, notably at transcriptional start sites of core histone genes, growth stimulus-associated genes, and ribosomal RNAs. Our findings reveal that nuclear CK2α complexes may be essential to facilitate progression of the cell cycle, by activating histone genes and triggering ribosomal biogenesis, specified in association with nuclear and nucleolar transcriptional regulators.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Histonas / Redes Reguladoras de Genes Límite: Humans Idioma: En Revista: Life Sci Alliance Año: 2024 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Histonas / Redes Reguladoras de Genes Límite: Humans Idioma: En Revista: Life Sci Alliance Año: 2024 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos