Lauinger, Linda and Li, Jing and Shostak, Anton and Cemel, Ibrahim Avi and Ha, Nati and Zhang, Yaru and Merkl, Philipp E. and Obermeyer, Simon and Stankovic-Valentin, Nicolas and Schafmeier, Tobias and Wever, Walter J. and Bowers, Albert A. and Carter, Kyle P. and Palmer, Amy E. and Tschochner, Herbert and Melchior, Frauke and Deshaies, Raymond J. and Brunner, Michael and Diernfellner, Axel (2017) Thiolutin is a zinc chelator that inhibits the Rpn11 and other JAMM metalloproteases. NATURE CHEMICAL BIOLOGY, 13 (7). 709-+. ISSN 1552-4450, 1552-4469
Full text not available from this repository. (Request a copy)Abstract
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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | HISTONE H2A DEUBIQUITINASE; MESSENGER-RNA; TRANSCRIPTIONAL REGULATION; NEUROSPORA-CRASSA; RESISTANT MUTANTS; ESCHERICHIA-COLI; MULTIPLE-MYELOMA; CIRCADIAN CLOCK; HUMAN-CELLS; PROTEASOME; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie III > Prof. Dr. Herbert Tschochner |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 14 Dec 2018 13:16 |
| Last Modified: | 25 Feb 2019 14:30 |
| URI: | https://pred.uni-regensburg.de/id/eprint/1648 |
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