SKP2 attenuates autophagy through Beclin1-ubiquitination and its inhibition reduces MERS-Coronavirus infection
Here, Gassen et al. show that S-phase kinase-associated protein 2 (SKP2) is responsible for lysine-48-linked poly-ubiquitination of beclin 1, resulting in its proteasomal degradation, and that inhibition of SKP2 enhances autophagy and reduces replication of MERS coronavirus.
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Nature Portfolio
2019
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oai:doaj.org-article:173953915c6a47688637a8c938baf5152021-12-02T15:35:39ZSKP2 attenuates autophagy through Beclin1-ubiquitination and its inhibition reduces MERS-Coronavirus infection10.1038/s41467-019-13659-42041-1723https://doaj.org/article/173953915c6a47688637a8c938baf5152019-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-13659-4https://doaj.org/toc/2041-1723Here, Gassen et al. show that S-phase kinase-associated protein 2 (SKP2) is responsible for lysine-48-linked poly-ubiquitination of beclin 1, resulting in its proteasomal degradation, and that inhibition of SKP2 enhances autophagy and reduces replication of MERS coronavirus.Nils C. GassenDaniela NiemeyerDoreen MuthVictor M. CormanSilvia MartinelliAlwine GassenKathrin HafnerJan PapiesKirstin MösbauerAndreas ZellnerAnthony S. ZannasAlexander HerrmannFlorian HolsboerRuth Brack-WernerMichael BoshartBertram Müller-MyhsokChristian DrostenMarcel A. MüllerTheo ReinNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-16 (2019) |
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Science Q Nils C. Gassen Daniela Niemeyer Doreen Muth Victor M. Corman Silvia Martinelli Alwine Gassen Kathrin Hafner Jan Papies Kirstin Mösbauer Andreas Zellner Anthony S. Zannas Alexander Herrmann Florian Holsboer Ruth Brack-Werner Michael Boshart Bertram Müller-Myhsok Christian Drosten Marcel A. Müller Theo Rein SKP2 attenuates autophagy through Beclin1-ubiquitination and its inhibition reduces MERS-Coronavirus infection |
description |
Here, Gassen et al. show that S-phase kinase-associated protein 2 (SKP2) is responsible for lysine-48-linked poly-ubiquitination of beclin 1, resulting in its proteasomal degradation, and that inhibition of SKP2 enhances autophagy and reduces replication of MERS coronavirus. |
format |
article |
author |
Nils C. Gassen Daniela Niemeyer Doreen Muth Victor M. Corman Silvia Martinelli Alwine Gassen Kathrin Hafner Jan Papies Kirstin Mösbauer Andreas Zellner Anthony S. Zannas Alexander Herrmann Florian Holsboer Ruth Brack-Werner Michael Boshart Bertram Müller-Myhsok Christian Drosten Marcel A. Müller Theo Rein |
author_facet |
Nils C. Gassen Daniela Niemeyer Doreen Muth Victor M. Corman Silvia Martinelli Alwine Gassen Kathrin Hafner Jan Papies Kirstin Mösbauer Andreas Zellner Anthony S. Zannas Alexander Herrmann Florian Holsboer Ruth Brack-Werner Michael Boshart Bertram Müller-Myhsok Christian Drosten Marcel A. Müller Theo Rein |
author_sort |
Nils C. Gassen |
title |
SKP2 attenuates autophagy through Beclin1-ubiquitination and its inhibition reduces MERS-Coronavirus infection |
title_short |
SKP2 attenuates autophagy through Beclin1-ubiquitination and its inhibition reduces MERS-Coronavirus infection |
title_full |
SKP2 attenuates autophagy through Beclin1-ubiquitination and its inhibition reduces MERS-Coronavirus infection |
title_fullStr |
SKP2 attenuates autophagy through Beclin1-ubiquitination and its inhibition reduces MERS-Coronavirus infection |
title_full_unstemmed |
SKP2 attenuates autophagy through Beclin1-ubiquitination and its inhibition reduces MERS-Coronavirus infection |
title_sort |
skp2 attenuates autophagy through beclin1-ubiquitination and its inhibition reduces mers-coronavirus infection |
publisher |
Nature Portfolio |
publishDate |
2019 |
url |
https://doaj.org/article/173953915c6a47688637a8c938baf515 |
work_keys_str_mv |
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