About: Parkin contributes to synaptic vesicle autophagy in Bassoon-deficient mice

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About: Parkin contributes to synaptic vesicle autophagy in Bassoon-deficient mice Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Parkin contributes to synaptic vesicle autophagy in Bassoon-deficient mice
Creator	Rahman, Kazi Smalla, Karl-Heinz Annamneedi, Anil Brockmann, Marisa Bruns, Christine Garner, Craig Gundelfinger, Eckart Hoffmann-Conaway, Sheila Montenegro-Venegas, Carolina Rosenmund, Christian Schneider, Katharina Textoris-Taube, Kathrin Trimbuch, Thorsten
Source	PMC
abstract	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.
has issue date	2020-05-04(xsd:dateTime)
bibo:doi	10.7554/elife.56590
bibo:pmid	32364493
has license	cc-by
sha1sum (hex)	a8bfdfb6e55354a0fc77f264c1a0e7b42dd68f2b
schema:url	https://doi.org/10.7554/elife.56590
resource representing a document's title	Parkin contributes to synaptic vesicle autophagy in Bassoon-deficient mice
has PubMed Central identifier	PMC7224700
has PubMed identifier	32364493
resource representing a document's body	covid:a8bfdfb6e55354a0fc77f264c1a0e7b42dd68f2b#body_text
is schema:about of	named entity 'Bassoon' named entity 'proteasome' named entity 'neurons' named entity 'Parkin' named entity 'ARTICLE' named entity 'LIGASE' named entity 'recycling' named entity 'Bassoon' named entity 'turnover' named entity 'ubiquitinated' named entity 'proteins' named entity 'Bassoon' named entity 'ubiquitination' named entity 'synaptic vesicle' named entity 'RESEARCH ARTICLE' named entity 'Parkin' named entity 'presynaptic' named entity 'Bassoon' named entity 'E3 ligase' named entity 'eLife' named entity 'proteasome' named entity 'proteostasis' named entity 'Parkin' named entity 'lysosomal' named entity 'synaptic vesicle' named entity 'autophagy' named entity 'Bassoon' named entity 'sucrose' named entity 'autophagy' named entity 'synapses' named entity 'autophagy' named entity 'Bsn' named entity 'follow-up' named entity 'KO mice' named entity 'wildtype' named entity 'presynaptic' named entity 'SDS-PAGE' named entity 'presynaptic' named entity 'EDTA' named entity 'presynaptic' named entity 'autophagosomes' named entity 'Syt1' named entity 'Parkin' named entity 'Bassoon' named entity 'neurons' named entity 'secondary antibody' named entity 'autophagosome' named entity 'neurons' named entity 'protein' named entity 'lysine' named entity 'multi-domain' named entity 'presynaptic' named entity 'Bassoon' named entity 'neurons' named entity 'autophagy' named entity 'ubiquitin' named entity 'scatterplot' named entity 'mobile phase' named entity 'NBA' named entity 'proteasome' named entity 'hippocampal neurons' named entity 'Bassoon' named entity 'PINK1' named entity 'SV2' named entity 'peptides' named entity 'ubiquitination' named entity 'Syt1' named entity 'NaCl' named entity 'axons' named entity 'viral infections'

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