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@ARTICLE{Schmitz:904324,
      author       = {Schmitz, Katharina and Cox, Jan and Esser, Lea Marie and
                      Voss, Martin and Sander, Katja and Löffler, Antje and
                      Hillebrand, Frank and Erkelenz, Steffen and Schaal, Heiner
                      and Kähne, Thilo and Klinker, Stefan and Zhang, Tao and
                      Nagel-Steger, Luitgard and Willbold, Dieter and Seggewiß,
                      Sabine and Schlütermann, David and Stork, Björn and
                      Grimmler, Matthias and Wesselborg, Sebastian and Peter,
                      Christoph},
      title        = {{A}n essential role of the autophagy activating kinase
                      {ULK}1 in sn{RNP} biogenesis},
      journal      = {Nucleic acids research},
      volume       = {49},
      number       = {11},
      issn         = {0301-5610},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press},
      reportid     = {FZJ-2021-05894},
      pages        = {6437 - 6455},
      year         = {2021},
      abstract     = {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.},
      cin          = {IBI-7},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5244 - Information Processing in Neuronal Networks
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5244},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34096600},
      UT           = {WOS:000671550100035},
      doi          = {10.1093/nar/gkab452},
      url          = {https://juser.fz-juelich.de/record/904324},
}