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@MISC{Tutas:280736,
      author       = {Tutas, Janine and Kononenko, Natalia L. and Tutas, Janine
                      and Tolve, Marianna},
      othercontributors = {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, Günter and Thorens, Bernard and
                          Gatto, Graziana and Frezza, Christian and Kononenko, Natalia
                          L.},
      title        = {{D}ataset: {A}utophagy regulator {ATG}5 maintains
                      cerebellar function by preventing its excessive glycolytic
                      activity.},
      publisher    = {Zenodo},
      reportid     = {DZNE-2025-00957},
      year         = {2024},
      abstract     = {The uploaded metabolomic dataset contains
                      liquid-chromatography-mass spectrometry (LC-MS) data
                      associated to the publication of Janine Tutas et al. from
                      the Natalia Kononenko laboratory. The title of the
                      publication is: Autophagy regulator ATG5 preserves
                      cerebellar function by safeguarding its glycolytic activity.
                      This article is to be published in Nature Metabolism Article
                      Abstract Dysfunctions in autophagy, a cellular mechanism for
                      breaking down components within lysosomes, often lead to
                      neurodegeneration. The specific mechanisms underlying
                      neuronal vulnerability to autophagy dysfunction remain
                      elusive. Here, we show that autophagy contributes to the
                      survival of cerebellar Purkinje cells (PCs) by safeguarding
                      their glycolytic activity. This function of autophagy is
                      independent of its conventional housekeeping role and
                      involves 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 deletion of GLUT2 in ATG5-deficient
                      mice mitigates PC neurodegeneration and restores their
                      ataxic gait. Taken together, this work reveals a novel
                      mechanism for regulating GLUT2 levels in neurons and
                      provides new insights into the neuroprotective role of
                      autophagy by controlling glucose homeostasis in the brain.},
      keywords     = {ATG5 (Other) / autophagy (Other) / glycolysis (Other) /
                      Purkinje cells (Other) / neurodegeneration (Other)},
      cin          = {AG Boecker},
      cid          = {I:(DE-2719)1011202},
      pnm          = {353 - Clinical and Health Care Research (POF4-353)},
      pid          = {G:(DE-HGF)POF4-353},
      typ          = {PUB:(DE-HGF)32},
      doi          = {10.5281/zenodo.10635079},
      url          = {https://pub.dzne.de/record/280736},
}