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10.7554/eLife.56590 http://scihub22266oqcxt.onion/10.7554/eLife.56590 C7224700!7224700!32364493     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       eLife 2020 ; 9 (ä): ä Nephropedia Template TP {{tp|p=32364493|t=2020. Parkin contributes to synaptic vesicle autophagy in Bassoon-deficient mice |pdf=|usr=}}{{32364493}} gab.com Text Parkin contributes to synaptic vesicle autophagy in Bassoon-deficient mice JO: eLife http://www.kidney.de/pget.php?&tw=1&pmid=32364493 #FOAvip 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. Twit Text FOAVip Parkin contributes to synaptic vesicle autophagy in Bassoon-deficient mice ????eLife http://www.kidney.de/pget.php?&tw=1&pmid=32364493 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32364493 #FOAvip English Wikipedia <ref>{{Cite pmid|32364493}}</ref> Parkin contributes to synaptic vesicle autophagy in Bassoon-deficient mice #MMPMID32364493 Hoffmann-Conaway S; Brockmann MM; Schneider K; Annamneedi A; Rahman KA; Bruns C; Textoris-Taube K; Trimbuch T; Smalla KH; Rosenmund C; Gundelfinger ED; Garner CC; Montenegro-Venegas C eLife 2020[]; 9 (ä): ä PMID32364493show ga 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. äParkin contributes to synaptic vesicle autophagy in Bassoon-deficient (epmc).pdf DeepDyve Pubget Overpricing