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Thiolutin is a zinc chelator that inhibits the Rpn11 and other JAMM metalloproteases

Thiolutin is a disulfide-containing antibiotic and anti-angiogenic compound produced by Streptomyces. Its biological targets are not known. We show that reduced thiolutin is a zinc chelator that inhibits the JAB1/MPN/Mov34 (JAMM) domain-containing metalloprotease Rpn11, a deubiquitinating enzyme of...

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Hauptverfasser: Lauinger, Linda (VerfasserIn) , Shostak, Anton (VerfasserIn) , Cemel, Ibrahim (VerfasserIn) , Ha, Nati (VerfasserIn) , Stankovic-Valentin, Nicolas (VerfasserIn) , Melchior, Frauke (VerfasserIn) , Brunner, Michael (VerfasserIn) , Diernfellner, Axel (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 01 May 2017
In: Nature chemical biology
Year: 2017, Jahrgang: 13, Heft: 7, Pages: 709-714
ISSN:1552-4469
DOI:10.1038/nchembio.2370
Online-Zugang:Verlag, Volltext: http://dx.doi.org/10.1038/nchembio.2370
Verlag, Volltext: https://www.nature.com/articles/nchembio.2370
Volltext
Verfasserangaben:Linda Lauinger, Jing Li, Anton Shostak, Ibrahim Avi Cemel, Nati Ha, Yaru Zhang, Philipp E. Merkl, Simon Obermeyer, Nicolas Stankovic-Valentin, Tobias Schafmeier, Walter J. Wever, Albert A. Bowers, Kyle P. Carter, Amy E. Palmer, Herbert Tschochner, Frauke Melchior, Raymond J. Deshaies, Michael Brunner & Axel Diernfellner
Beschreibung
Zusammenfassung:Thiolutin is a disulfide-containing antibiotic and anti-angiogenic compound produced by Streptomyces. Its biological targets are not known. We show that reduced thiolutin is a zinc chelator that inhibits the JAB1/MPN/Mov34 (JAMM) domain-containing metalloprotease Rpn11, a deubiquitinating enzyme of the 19S proteasome. Thiolutin also inhibits the JAMM metalloproteases Csn5, the deneddylase of the COP9 signalosome; AMSH, which regulates ubiquitin-dependent sorting of cell-surface receptors; and BRCC36, a K63-specific deubiquitinase of the BRCC36-containing isopeptidase complex and the BRCA1-BRCA2-containing complex. We provide evidence that other dithiolopyrrolones also function as inhibitors of JAMM metalloproteases.
Beschreibung:Gesehen am 25.09.2018
Beschreibung:Online Resource
ISSN:1552-4469
DOI:10.1038/nchembio.2370

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