Y
Yuko Hirano
Researcher at University of Tokyo
Publications - 12
Citations - 1267
Yuko Hirano is an academic researcher from University of Tokyo. The author has contributed to research in topics: Proteasome & Proteasome assembly. The author has an hindex of 11, co-authored 12 publications receiving 1177 citations. Previous affiliations of Yuko Hirano include Institute of Medical Science.
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Journal ArticleDOI
A heterodimeric complex that promotes the assembly of mammalian 20S proteasomes
Yuko Hirano,Klavs B. Hendil,Hideki Yashiroda,Shun-ichiro Iemura,Ryoichi Nagane,Yusaku Hioki,Tohru Natsume,Keiji Tanaka,Shigeo Murata,Shigeo Murata +9 more
TL;DR: Two chaperones, designated proteasome assembling chaperone-1 (PAC1) and PAC2, that are involved in the maturation of mammalian 20S proteasomes are reported that identify a mechanism for the correct assembly of 20S proteasomes.
Journal ArticleDOI
A serine protease inhibitor prevents endoplasmic reticulum stress-induced cleavage but not transport of the membrane-bound transcription factor ATF6.
Tetsuya Okada,Kyosuke Haze,Satomi Nadanaka,Hiderou Yoshida,Hiderou Yoshida,Nabil G. Seidah,Yuko Hirano,Ryuichiro Sato,Manabu Negishi,Kazutoshi Mori +9 more
TL;DR: This study found that 4-(2-aminoethyl)benzenesulfonyl fluoride (AEBSF), a serine protease inhibitor, prevented ER stress-induced cleavage of ATF6α and ATF6β, resulting in inhibition of transcriptional induction of ATF 6-target genes.
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Direct demonstration of rapid degradation of nuclear sterol regulatory element-binding proteins by the ubiquitin-proteasome pathway.
TL;DR: Results demonstrate that the ubiquitin-proteasome system degrades SREBPs and that this system controls the expression of SREBP-responsive genes.
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Dissecting β-ring assembly pathway of the mammalian 20S proteasome
Yuko Hirano,Takeumi Kaneko,Kenta Okamoto,Minghui Bai,Hideki Yashiroda,Kaori Furuyama,Koichi Kato,Koichi Kato,Keiji Tanaka,Shigeo Murata +9 more
TL;DR: This work clarifies the mechanism of β‐ring formation on α‐rings by characterizing assembly intermediates accumulated in cells depleted of each β‐subunit and proposes a model in which β‐rings formation is assisted by both intramolecular and extrinsic chaperones, whose roles are partially different between yeast and mammals.
Journal ArticleDOI
Cooperation of Multiple Chaperones Required for the Assembly of Mammalian 20S Proteasomes
Yuko Hirano,Hidemi Hayashi,Shun-ichiro Iemura,Klavs B. Hendil,Shin-ichiro Niwa,Toshihiko Kishimoto,Masanori Kasahara,Tohru Natsume,Keiji Tanaka,Shigeo Murata,Shigeo Murata +10 more
TL;DR: A cooperative system of multiple chaperones involved in the correct assembly of mammalian 20S proteasomes is described, including a chaperone, designated PAC3, as a component of alpha rings.