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The Impact of p70S6 Kinase-Dependent Phosphorylation of Gemin2 in UsnRNP Biogenesis.
Esser, Lea Marie; Li, Qiaoping; Jüdt, Maximilian; Kähne, Thilo; Stork, Björn; Grimmler, Matthias; Wesselborg, Sebastian; Peter, Christoph.
Afiliação
  • Esser LM; Institute of Molecular Medicine I, Medical Faculty, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.
  • Li Q; Institute of Molecular Medicine I, Medical Faculty, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.
  • Jüdt M; Institute of Molecular Medicine I, Medical Faculty, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.
  • Kähne T; Institute of Experimental Internal Medicine, Otto von Guericke University, 39120 Magdeburg, Germany.
  • Stork B; Institute of Molecular Medicine I, Medical Faculty, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.
  • Grimmler M; Institute for Biomolecular Research, Hochschule Fresenius gGmbH, University of Applied Sciences, 65510 Idstein, Germany.
  • Wesselborg S; DiaServe Laboratories GmbH, 82393 Iffeldorf, Germany.
  • Peter C; Institute of Molecular Medicine I, Medical Faculty, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.
Int J Mol Sci ; 24(21)2023 Oct 25.
Article em En | MEDLINE | ID: mdl-37958537
ABSTRACT
The survival motor neuron (SMN) complex is a multi-megadalton complex involved in post-transcriptional gene expression in eukaryotes via promotion of the biogenesis of uridine-rich small nuclear ribonucleoproteins (UsnRNPs). The functional center of the complex is formed from the SMN/Gemin2 subunit. By binding the pentameric ring made up of the Sm proteins SmD1/D2/E/F/G and allowing for their transfer to a uridine-rich short nuclear RNA (UsnRNA), the Gemin2 protein in particular is crucial for the selectivity of the Sm core assembly. It is well established that post-translational modifications control UsnRNP biogenesis. In our work presented here, we emphasize the crucial role of Gemin2, showing that the phospho-status of Gemin2 influences the capacity of the SMN complex to condense in Cajal bodies (CBs) in vivo. Additionally, we define Gemin2 as a novel and particular binding partner and phosphorylation substrate of the mTOR pathway kinase ribosomal protein S6 kinase beta-1 (p70S6K). Experiments using size exclusion chromatography further demonstrated that the Gemin2 protein functions as a connecting element between the 6S complex and the SMN complex. As a result, p70S6K knockdown lowered the number of CBs, which in turn inhibited in vivo UsnRNP synthesis. In summary, these findings reveal a unique regulatory mechanism of UsnRNP biogenesis.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Ligação a RNA / Proteínas Quinases S6 Ribossômicas 70-kDa Idioma: En Revista: Int J Mol Sci Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Alemanha

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Ligação a RNA / Proteínas Quinases S6 Ribossômicas 70-kDa Idioma: En Revista: Int J Mol Sci Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Alemanha