TY  - JOUR
AU  - Schmitz, Katharina
AU  - Cox, Jan
AU  - Esser, Lea Marie
AU  - Voss, Martin
AU  - Sander, Katja
AU  - Löffler, Antje
AU  - Hillebrand, Frank
AU  - Erkelenz, Steffen
AU  - Schaal, Heiner
AU  - Kähne, Thilo
AU  - Klinker, Stefan
AU  - Zhang, Tao
AU  - Nagel-Steger, Luitgard
AU  - Willbold, Dieter
AU  - Seggewiß, Sabine
AU  - Schlütermann, David
AU  - Stork, Björn
AU  - Grimmler, Matthias
AU  - Wesselborg, Sebastian
AU  - Peter, Christoph
TI  - An essential role of the autophagy activating kinase ULK1 in snRNP biogenesis
JO  - Nucleic acids research
VL  - 49
IS  - 11
SN  - 0301-5610
CY  - Oxford
PB  - Oxford Univ. Press
M1  - FZJ-2021-05894
SP  - 6437 - 6455
PY  - 2021
AB  - The biogenesis of small uridine-rich nuclear ribonucleoproteins (UsnRNPs) depends on the methylation of Sm proteins catalyzed by the methylosome and the subsequent action of the SMN complex, which assembles the heptameric Sm protein ring onto small nuclear RNAs (snRNAs). In this sophisticated process, the methylosome subunit pICln (chloride conductance regulatory protein) is attributed to an exceptional key position as an ‘assembly chaperone’ by building up a stable precursor Sm protein ring structure. Here, we show that—apart from its autophagic role—the Ser/Thr kinase ULK1 (Uncoordinated [unc-51] Like Kinase 1) functions as a novel key regulator in UsnRNP biogenesis by phosphorylation of the C-terminus of pICln. As a consequence, phosphorylated pICln is no longer capable to hold up the precursor Sm ring structure. Consequently, inhibition of ULK1 results in a reduction of efficient UsnRNP core assembly. Thus ULK1, depending on its complex formation, exerts different functions in autophagy or snRNP biosynthesis.
LB  - PUB:(DE-HGF)16
C6  - pmid:34096600
UR  - <Go to ISI:>//WOS:000671550100035
DO  - DOI:10.1093/nar/gkab452
UR  - https://juser.fz-juelich.de/record/904324
ER  -