Allosteric control of Ubp6 and the proteasome via a bidirectional switch

The proteasome recognizes ubiquitinated proteins and can also edit ubiquitin marks, allowing substrates to be rejected based on ubiquitin chain topology. In yeast, editing is mediated by deubiquitinating enzyme Ubp6. The proteasome activates Ubp6, whereas Ubp6 inhibits the proteasome through deubiqu...

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Detalles Bibliográficos
Autores principales: Hung, Ka Ying Sharon, Klumpe, Sven, Eisele, Markus R., Elsasser, Suzanne, Tian, Geng, Sun, Shuangwu, Moroco, Jamie A., Cheng, Tat Cheung, Joshi, Tapan, Seibel, Timo, Van Dalen, Duco, Feng, Xin-Hua, Lu, Ying, Ovaa, Huib, Engen, John R., Lee, Byung-Hoon, Rudack, Till, Sakata, Eri, Finley, Daniel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2022
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8837689/
https://www.ncbi.nlm.nih.gov/pubmed/35149681
http://dx.doi.org/10.1038/s41467-022-28186-y

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8837689/
https://www.ncbi.nlm.nih.gov/pubmed/35149681
http://dx.doi.org/10.1038/s41467-022-28186-y

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