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Pask integrates hormonal signaling with histone modification via Wdr5 phosphorylation to drive myogenesis.
Kikani, Chintan K; Wu, Xiaoying; Paul, Litty; Sabic, Hana; Shen, Zuolian; Shakya, Arvind; Keefe, Alexandra; Villanueva, Claudio; Kardon, Gabrielle; Graves, Barbara; Tantin, Dean; Rutter, Jared.
Afiliación
  • Kikani CK; Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.
  • Wu X; Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.
  • Paul L; Department of Oncological Sciences, University of Utah School of Medicine, Salt Lake City, United States.
  • Sabic H; Huntsman Cancer Institute, University of Utah School of Medicine, Salt Lake City, United States.
  • Shen Z; Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.
  • Shakya A; Department of Pathology, University of Utah School of Medicine, Salt Lake City, United States.
  • Keefe A; Department of Pathology, University of Utah School of Medicine, Salt Lake City, United States.
  • Villanueva C; Department of Human Genetics, University of Utah School of Medicine, Salt Lake City, United States.
  • Kardon G; Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.
  • Graves B; Department of Human Genetics, University of Utah School of Medicine, Salt Lake City, United States.
  • Tantin D; Department of Oncological Sciences, University of Utah School of Medicine, Salt Lake City, United States.
  • Rutter J; Huntsman Cancer Institute, University of Utah School of Medicine, Salt Lake City, United States.
Elife ; 52016 09 23.
Article en En | MEDLINE | ID: mdl-27661449
PAS domain containing protein kinase (Pask) is an evolutionarily conserved protein kinase implicated in energy homeostasis and metabolic regulation across eukaryotic species. We now describe an unexpected role of Pask in promoting the differentiation of myogenic progenitor cells, embryonic stem cells and adipogenic progenitor cells. This function of Pask is dependent upon its ability to phosphorylate Wdr5, a member of several protein complexes including those that catalyze histone H3 Lysine 4 trimethylation (H3K4me3) during transcriptional activation. Our findings suggest that, during myoblast differentiation, Pask stimulates the conversion of repressive H3K4me1 to activating H3K4me3 marks on the promoter of the differentiation gene myogenin (Myog) via Wdr5 phosphorylation. This enhances accessibility of the MyoD transcription factor and enables transcriptional activation of the Myog promoter to initiate muscle differentiation. Thus, as an upstream kinase of Wdr5, Pask integrates signaling cues with the transcriptional network to regulate the differentiation of progenitor cells.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Transducción de Señal / N-Metiltransferasa de Histona-Lisina / Proteínas Serina-Treonina Quinasas / Desarrollo de Músculos / Código de Histonas / Músculos Límite: Animals / Humans Idioma: En Revista: Elife Año: 2016 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Transducción de Señal / N-Metiltransferasa de Histona-Lisina / Proteínas Serina-Treonina Quinasas / Desarrollo de Músculos / Código de Histonas / Músculos Límite: Animals / Humans Idioma: En Revista: Elife Año: 2016 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido