Molecular basis of ubiquitin-specific protease 8 autoinhibition by the WW-like domain

In order to advance our understanding of the regulation of Ubiquitin-specific protease 8 (USP8), which is known to play a role in Cushing’s Disease, Kakihara et al identify and characterise amino acids 645–684 of USP8, which serve as an autoinhibitory region. Their pull-down and single-molecule FRET...

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Autores principales: Keijun Kakihara, Kengo Asamizu, Kei Moritsugu, Masahide Kubo, Tetsuya Kitaguchi, Akinori Endo, Akinori Kidera, Mitsunori Ikeguchi, Akira Kato, Masayuki Komada, Toshiaki Fukushima
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Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/553ea530ebaf4496bc79a1fb2f40c32c
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spelling oai:doaj.org-article:553ea530ebaf4496bc79a1fb2f40c32c2021-11-14T12:12:05ZMolecular basis of ubiquitin-specific protease 8 autoinhibition by the WW-like domain10.1038/s42003-021-02802-x2399-3642https://doaj.org/article/553ea530ebaf4496bc79a1fb2f40c32c2021-11-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-02802-xhttps://doaj.org/toc/2399-3642In order to advance our understanding of the regulation of Ubiquitin-specific protease 8 (USP8), which is known to play a role in Cushing’s Disease, Kakihara et al identify and characterise amino acids 645–684 of USP8, which serve as an autoinhibitory region. Their pull-down and single-molecule FRET analysis, as well as in silico modelling, suggest that the release of USP8 autoinhibition may underlie Cushing’s disease.Keijun KakiharaKengo AsamizuKei MoritsuguMasahide KuboTetsuya KitaguchiAkinori EndoAkinori KideraMitsunori IkeguchiAkira KatoMasayuki KomadaToshiaki FukushimaNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-12 (2021)
institution DOAJ
collection DOAJ
language EN
topic Biology (General)
QH301-705.5
spellingShingle Biology (General)
QH301-705.5
Keijun Kakihara
Kengo Asamizu
Kei Moritsugu
Masahide Kubo
Tetsuya Kitaguchi
Akinori Endo
Akinori Kidera
Mitsunori Ikeguchi
Akira Kato
Masayuki Komada
Toshiaki Fukushima
Molecular basis of ubiquitin-specific protease 8 autoinhibition by the WW-like domain
description In order to advance our understanding of the regulation of Ubiquitin-specific protease 8 (USP8), which is known to play a role in Cushing’s Disease, Kakihara et al identify and characterise amino acids 645–684 of USP8, which serve as an autoinhibitory region. Their pull-down and single-molecule FRET analysis, as well as in silico modelling, suggest that the release of USP8 autoinhibition may underlie Cushing’s disease.
format article
author Keijun Kakihara
Kengo Asamizu
Kei Moritsugu
Masahide Kubo
Tetsuya Kitaguchi
Akinori Endo
Akinori Kidera
Mitsunori Ikeguchi
Akira Kato
Masayuki Komada
Toshiaki Fukushima
author_facet Keijun Kakihara
Kengo Asamizu
Kei Moritsugu
Masahide Kubo
Tetsuya Kitaguchi
Akinori Endo
Akinori Kidera
Mitsunori Ikeguchi
Akira Kato
Masayuki Komada
Toshiaki Fukushima
author_sort Keijun Kakihara
title Molecular basis of ubiquitin-specific protease 8 autoinhibition by the WW-like domain
title_short Molecular basis of ubiquitin-specific protease 8 autoinhibition by the WW-like domain
title_full Molecular basis of ubiquitin-specific protease 8 autoinhibition by the WW-like domain
title_fullStr Molecular basis of ubiquitin-specific protease 8 autoinhibition by the WW-like domain
title_full_unstemmed Molecular basis of ubiquitin-specific protease 8 autoinhibition by the WW-like domain
title_sort molecular basis of ubiquitin-specific protease 8 autoinhibition by the ww-like domain
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/553ea530ebaf4496bc79a1fb2f40c32c
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