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Mechanisms regulating the turnover of synaptic vesicle (SV) proteins are not well understood. They are thought to require poly-ubiquitination and degradation through proteasome, endo-lysosomal or autophagy-related pathways. Bassoon was shown to negatively regulate presynaptic autophagy in part by scaffolding Atg5. Here, we show that increased autophagy in Bassoon knockout neurons depends on poly-ubiquitination and that the loss of Bassoon leads to elevated levels of ubiquitinated synaptic proteins per se. Our data show that Bassoon knockout neurons have a smaller SV pool size and a higher turnover rate as indicated by a younger pool of SV2. The E3 ligase Parkin is required for increased autophagy in Bassoon-deficient neurons as the knockdown of Parkin normalized autophagy and SV protein levels and rescued impaired SV recycling. These data indicate that Bassoon is a key regulator of SV proteostasis and that Parkin is a key E3 ligase in the autophagy-mediated clearance of SV proteins. © 2020, Hoffmann-Conaway et al.


Sheila Hoffmann-Conaway, Marisa M Brockmann, Katharina Schneider, Anil Annamneedi, Kazi Atikur Rahman, Christine Bruns, Kathrin Textoris-Taube, Thorsten Trimbuch, Karl-Heinz Smalla, Christian Rosenmund, Eckart D Gundelfinger, Craig Curtis Garner, Carolina Montenegro-Venegas. Parkin contributes to synaptic vesicle autophagy in Bassoon-deficient mice. eLife. 2020 May 04;9

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PMID: 32364493

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