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@ARTICLE{Tutas:277313,
      author       = {Tutas, Janine and Tolve, Marianna and Özer-Yildiz, Ebru
                      and Ickert, Lotte and Klein, Ines and Silverman, Quinn and
                      Liebsch, Filip and Dethloff, Frederik and Giavalisco,
                      Patrick and Endepols, Heike and Georgomanolis, Theodoros and
                      Neumaier, Bernd and Drzezga, Alexander and Schwarz, Guenter
                      and Thorens, Bernard and Gatto, Graziana and Frezza,
                      Christian and Kononenko, Natalia L},
      title        = {{A}utophagy regulator {ATG}5 preserves cerebellar function
                      by safeguarding its glycolytic activity.},
      journal      = {Nature metabolism},
      volume       = {7},
      number       = {2},
      issn         = {2522-5812},
      address      = {[London]},
      publisher    = {Springer Nature},
      reportid     = {DZNE-2025-00376},
      pages        = {297 - 320},
      year         = {2025},
      abstract     = {Dysfunctions in autophagy, a cellular mechanism for
                      breaking down components within lysosomes, often lead to
                      neurodegeneration. The specific mechanisms underlying
                      neuronal vulnerability due to autophagy dysfunction remain
                      elusive. Here we show that autophagy contributes to
                      cerebellar Purkinje cell (PC) survival by safeguarding their
                      glycolytic activity. Outside the conventional housekeeping
                      role, autophagy is also involved in the ATG5-mediated
                      regulation of glucose transporter 2 (GLUT2) levels during
                      cerebellar maturation. Autophagy-deficient PCs exhibit GLUT2
                      accumulation on the plasma membrane, along with increased
                      glucose uptake and alterations in glycolysis. We identify
                      lysophosphatidic acid and serine as glycolytic intermediates
                      that trigger PC death and demonstrate that the deletion of
                      GLUT2 in ATG5-deficient mice mitigates PC neurodegeneration
                      and rescues their ataxic gait. Taken together, this work
                      reveals a mechanism for regulating GLUT2 levels in neurons
                      and provides insights into the neuroprotective role of
                      autophagy by controlling glucose homeostasis in the brain.},
      keywords     = {Animals / Autophagy-Related Protein 5: metabolism /
                      Autophagy-Related Protein 5: genetics / Mice / Glycolysis /
                      Autophagy / Cerebellum: metabolism / Purkinje Cells:
                      metabolism / Glucose: metabolism / Glucose Transporter Type
                      2: metabolism / Mice, Knockout / Autophagy-Related Protein 5
                      (NLM Chemicals) / Atg5 protein, mouse (NLM Chemicals) /
                      Glucose (NLM Chemicals) / Glucose Transporter Type 2 (NLM
                      Chemicals) / Slc2a2 protein, mouse (NLM Chemicals)},
      cin          = {AG Boecker},
      ddc          = {610},
      cid          = {I:(DE-2719)1011202},
      pnm          = {353 - Clinical and Health Care Research (POF4-353)},
      pid          = {G:(DE-HGF)POF4-353},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39815080},
      doi          = {10.1038/s42255-024-01196-4},
      url          = {https://pub.dzne.de/record/277313},
}