Dokument: Phosphorylation of pICln by the autophagy activating kinase ULK1 regulates snRNP biogenesis and splice activity of the cell

Titel:Phosphorylation of pICln by the autophagy activating kinase ULK1 regulates snRNP biogenesis and splice activity of the cell
URL für Lesezeichen:https://docserv.uni-duesseldorf.de/servlets/DocumentServlet?id=67011
URN (NBN):urn:nbn:de:hbz:061-20241010-131617-3
Kollektion:Publikationen
Sprache:Englisch
Dokumententyp:Wissenschaftliche Texte » Artikel, Aufsatz
Medientyp:Text
Autoren: Esser, Lea Marie [Autor]
Schmitz, Katharina [Autor]
Hillebrand, Frank [Autor]
Erkelenz, Steffen [Autor]
Schaal, Heiner [Autor]
Stork, Björn [Autor]
Grimmler, Matthias [Autor]
Wesselborg, Sebastian [Autor]
Peter, Christoph [Autor]
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Dateien vom 16.10.2024 / geändert 16.10.2024
Stichwörter:pICln, ULK1, Autophagy, PRMT5, UsnRNP, spliceosomal activity
Beschreibung:The spliceosome, responsible for all mature protein-coding transcripts of eukaryotic intron-containing genes, consists of small uridine-rich nuclear ribonucleoproteins (UsnRNPs). The assembly of UsnRNPs depends, on one hand, on the arginine methylation of Sm proteins catalyzed by the PRMT5 complex. On the other hand, it depends on the phosphorylation of the PRMT5 subunit pICln by the Uncoordinated Like Kinase 1 (ULK1). In consequence, phosphorylation of pICln affects the stability of the UsnRNP assembly intermediate, the so-called 6 S complex. The detailed mechanisms of phosphorylation-dependent integrity and subsequent UsnRNP assembly of the 6 S complex in vivo have not yet been analyzed.
By using a phospho-specific antibody against ULK1-dependent phosphorylation sites of pICln, we visualize the intracellular distribution of phosphorylated pICln. Furthermore, we detect the colocaliphosphor-pICln1 with phospho-pICln by size-exclusion chromatography and immunofluorescence techniques. We also show that phosphorylated pICln is predominantly present in the 6 S complex. The addition of ULK1 to in vitro produced 6 S complex, as well as the reconstitution of ULK1 in ULK1-deficient cells, increases the efficiency of snRNP biogenesis. Accordingly, inhibition of ULK1 and the associated decreased pICln phosphorylation lead to accumulation of the 6 S complex and reduction in the spliceosomal activity of the cell.
Rechtliche Vermerke:Originalveröffentlichung:
Esser, L. M., Schmitz, K., Hillebrand, F., Erkelenz, S., Schaal, H., Stork, B., Grimmler, M., Wesselborg, S., & Peter, C. (2023). Phosphorylation of pICln by the autophagy activating kinase ULK1 regulates snRNP biogenesis and splice activity of the cell [OnlineRessource]. Computational and Structural Biotechnology Journal , 21, 2100–2109. https://doi.org/10.1016/j.csbj.2023.03.015
Lizenz:Creative Commons Lizenzvertrag
Dieses Werk ist lizenziert unter einer Creative Commons Namensnennung 4.0 International Lizenz
Fachbereich / Einrichtung:Medizinische Fakultät
Dokument erstellt am:10.10.2024
Dateien geändert am:16.10.2024
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