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@ARTICLE{Overhoff:165350,
      author       = {Overhoff, Melina and Tellkamp, Frederik and Hess, Simon and
                      Tolve, Marianna and Tutas, Janine and Faerfers, Marcel and
                      Ickert, Lotte and Mohammadi, Milad and De Bruyckere, Elodie
                      and Kallergi, Emmanouela and Delle Vedove, Andrea and
                      Nikoletopoulou, Vassiliki and Wirth, Brunhilde and Isensee,
                      Joerg and Hucho, Tim and Puchkov, Dmytro and Isbrandt, Dirk
                      and Krueger, Marcus and Kloppenburg, Peter and Kononenko,
                      Natalia L},
      title        = {{A}utophagy regulates neuronal excitability by controlling
                      c{AMP}/protein kinase {A} signaling at the synapse.},
      journal      = {The EMBO journal},
      volume       = {41},
      number       = {22},
      issn         = {0261-4189},
      address      = {Hoboken, NJ [u.a.]},
      publisher    = {Wiley},
      reportid     = {DZNE-2022-01627},
      pages        = {e110963},
      year         = {2022},
      abstract     = {Autophagy provides nutrients during starvation and
                      eliminates detrimental cellular components. However,
                      accumulating evidence indicates that autophagy is not merely
                      a housekeeping process. Here, by combining mouse models of
                      neuron-specific ATG5 deficiency in either excitatory or
                      inhibitory neurons with quantitative proteomics,
                      high-content microscopy, and live-imaging approaches, we
                      show that autophagy protein ATG5 functions in neurons to
                      regulate cAMP-dependent protein kinase A (PKA)-mediated
                      phosphorylation of a synapse-confined proteome. This
                      function of ATG5 is independent of bulk turnover of synaptic
                      proteins and requires the targeting of PKA inhibitory R1
                      subunits to autophagosomes. Neuronal loss of ATG5 causes
                      synaptic accumulation of PKA-R1, which sequesters the PKA
                      catalytic subunit and diminishes cAMP/PKA-dependent
                      phosphorylation of postsynaptic cytoskeletal proteins that
                      mediate AMPAR trafficking. Furthermore, ATG5 deletion in
                      glutamatergic neurons augments AMPAR-dependent excitatory
                      neurotransmission and causes the appearance of spontaneous
                      recurrent seizures in mice. Our findings identify a novel
                      role of autophagy in regulating PKA signaling at
                      glutamatergic synapses and suggest the PKA as a target for
                      restoration of synaptic function in neurodegenerative
                      conditions with autophagy dysfunction.},
      keywords     = {Mice / Animals / Synapses: metabolism / Neurons: metabolism
                      / Cyclic AMP-Dependent Protein Kinases: metabolism / Signal
                      Transduction / Autophagy / PKA (Other) / autophagy (Other) /
                      brain (Other) / phosphorylation (Other) / synapse (Other)},
      cin          = {AG Isbrandt},
      ddc          = {570},
      cid          = {I:(DE-2719)1011003},
      pnm          = {351 - Brain Function (POF4-351)},
      pid          = {G:(DE-HGF)POF4-351},
      typ          = {PUB:(DE-HGF)16},
      pmc          = {pmc:PMC9670194},
      pubmed       = {pmid:36217825},
      doi          = {10.15252/embj.2022110963},
      url          = {https://pub.dzne.de/record/165350},
}