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Parkin contributes to synaptic vesicle autophagy in Bassoon-deficient mice

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

in: ELIFE, Jahrgang 9, e56590, 04.05.2020.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Hoffmann-Conaway, S, Brockmann, MM, Schneider, K, Annamneedi, A, Rahman, KA, Bruns, C, Textoris-Taube, K, Trimbuch, T, Smalla, K-H, Rosenmund, C, Gundelfinger, ED, Garner, CC & Montenegro-Venegas, C 2020, 'Parkin contributes to synaptic vesicle autophagy in Bassoon-deficient mice', ELIFE, Jg. 9, e56590. https://doi.org/10.7554/eLife.56590

APA

Hoffmann-Conaway, S., Brockmann, M. M., Schneider, K., Annamneedi, A., Rahman, K. A., Bruns, C., Textoris-Taube, K., Trimbuch, T., Smalla, K-H., Rosenmund, C., Gundelfinger, E. D., Garner, C. C., & Montenegro-Venegas, C. (2020). Parkin contributes to synaptic vesicle autophagy in Bassoon-deficient mice. ELIFE, 9, [e56590]. https://doi.org/10.7554/eLife.56590

Vancouver

Hoffmann-Conaway S, Brockmann MM, Schneider K, Annamneedi A, Rahman KA, Bruns C et al. Parkin contributes to synaptic vesicle autophagy in Bassoon-deficient mice. ELIFE. 2020 Mai 4;9. e56590. https://doi.org/10.7554/eLife.56590

Bibtex

@article{cbee9563522d428fa5390a90afc3e3d6,
title = "Parkin contributes to synaptic vesicle autophagy in Bassoon-deficient mice",
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.",
author = "Sheila Hoffmann-Conaway and Brockmann, {Marisa M} and Katharina Schneider and Anil Annamneedi and Rahman, {Kazi Atikur} and Christine Bruns and Kathrin Textoris-Taube and Thorsten Trimbuch and Karl-Heinz Smalla and Christian Rosenmund and Gundelfinger, {Eckart D} and Garner, {Craig Curtis} and Carolina Montenegro-Venegas",
year = "2020",
month = may,
day = "4",
doi = "10.7554/eLife.56590",
language = "English",
volume = "9",
journal = "ELIFE",
issn = "2050-084X",
publisher = "eLife Sciences Publications",

}

RIS

TY - JOUR

T1 - Parkin contributes to synaptic vesicle autophagy in Bassoon-deficient mice

AU - Hoffmann-Conaway, Sheila

AU - Brockmann, Marisa M

AU - Schneider, Katharina

AU - Annamneedi, Anil

AU - Rahman, Kazi Atikur

AU - Bruns, Christine

AU - Textoris-Taube, Kathrin

AU - Trimbuch, Thorsten

AU - Smalla, Karl-Heinz

AU - Rosenmund, Christian

AU - Gundelfinger, Eckart D

AU - Garner, Craig Curtis

AU - Montenegro-Venegas, Carolina

PY - 2020/5/4

Y1 - 2020/5/4

N2 - 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.

AB - 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.

U2 - 10.7554/eLife.56590

DO - 10.7554/eLife.56590

M3 - SCORING: Journal article

VL - 9

JO - ELIFE

JF - ELIFE

SN - 2050-084X

M1 - e56590

ER -