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000277313 1001_ $$0P:(DE-2719)9002478$$aTutas, Janine$$b0$$udzne
000277313 245__ $$aAutophagy regulator ATG5 preserves cerebellar function by safeguarding its glycolytic activity.
000277313 260__ $$a[London]$$bSpringer Nature$$c2025
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000277313 520__ $$aDysfunctions in autophagy, a cellular mechanism for breaking down components within lysosomes, often lead to neurodegeneration. The specific mechanisms underlying neuronal vulnerability due to autophagy dysfunction remain elusive. Here we show that autophagy contributes to cerebellar Purkinje cell (PC) survival by safeguarding their glycolytic activity. Outside the conventional housekeeping role, autophagy is also involved in the ATG5-mediated regulation of glucose transporter 2 (GLUT2) levels during cerebellar maturation. Autophagy-deficient PCs exhibit GLUT2 accumulation on the plasma membrane, along with increased glucose uptake and alterations in glycolysis. We identify lysophosphatidic acid and serine as glycolytic intermediates that trigger PC death and demonstrate that the deletion of GLUT2 in ATG5-deficient mice mitigates PC neurodegeneration and rescues their ataxic gait. Taken together, this work reveals a mechanism for regulating GLUT2 levels in neurons and provides insights into the neuroprotective role of autophagy by controlling glucose homeostasis in the brain.
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000277313 650_7 $$2NLM Chemicals$$aAutophagy-Related Protein 5
000277313 650_7 $$2NLM Chemicals$$aAtg5 protein, mouse
000277313 650_7 $$0IY9XDZ35W2$$2NLM Chemicals$$aGlucose
000277313 650_7 $$2NLM Chemicals$$aGlucose Transporter Type 2
000277313 650_7 $$2NLM Chemicals$$aSlc2a2 protein, mouse
000277313 650_2 $$2MeSH$$aAnimals
000277313 650_2 $$2MeSH$$aAutophagy-Related Protein 5: metabolism
000277313 650_2 $$2MeSH$$aAutophagy-Related Protein 5: genetics
000277313 650_2 $$2MeSH$$aMice
000277313 650_2 $$2MeSH$$aGlycolysis
000277313 650_2 $$2MeSH$$aAutophagy
000277313 650_2 $$2MeSH$$aCerebellum: metabolism
000277313 650_2 $$2MeSH$$aPurkinje Cells: metabolism
000277313 650_2 $$2MeSH$$aGlucose: metabolism
000277313 650_2 $$2MeSH$$aGlucose Transporter Type 2: metabolism
000277313 650_2 $$2MeSH$$aMice, Knockout
000277313 7001_ $$0P:(DE-2719)9002317$$aTolve, Marianna$$b1$$udzne
000277313 7001_ $$aÖzer-Yildiz, Ebru$$b2
000277313 7001_ $$00000-0003-2729-0928$$aIckert, Lotte$$b3
000277313 7001_ $$aKlein, Ines$$b4
000277313 7001_ $$00000-0003-3660-3199$$aSilverman, Quinn$$b5
000277313 7001_ $$00000-0002-0955-8065$$aLiebsch, Filip$$b6
000277313 7001_ $$00009-0002-1114-2621$$aDethloff, Frederik$$b7
000277313 7001_ $$00000-0002-4636-1827$$aGiavalisco, Patrick$$b8
000277313 7001_ $$00000-0002-6166-4818$$aEndepols, Heike$$b9
000277313 7001_ $$aGeorgomanolis, Theodoros$$b10
000277313 7001_ $$00000-0001-5425-3116$$aNeumaier, Bernd$$b11
000277313 7001_ $$0P:(DE-2719)2811239$$aDrzezga, Alexander$$b12
000277313 7001_ $$00000-0002-2118-9338$$aSchwarz, Guenter$$b13
000277313 7001_ $$00000-0002-3738-0129$$aThorens, Bernard$$b14
000277313 7001_ $$00000-0002-4244-8925$$aGatto, Graziana$$b15
000277313 7001_ $$00000-0002-3293-7397$$aFrezza, Christian$$b16
000277313 7001_ $$00000-0002-3425-6659$$aKononenko, Natalia L$$b17
000277313 773__ $$0PERI:(DE-600)2933873-6$$a10.1038/s42255-024-01196-4$$gVol. 7, no. 2, p. 297 - 320$$n2$$p297 - 320$$tNature metabolism$$v7$$x2522-5812$$y2025
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