Cargando…
Ubiquitin modulates 26S proteasome conformational dynamics and promotes substrate degradation
The 26S proteasome recognizes thousands of appropriate protein substrates in eukaryotic cells through attached ubiquitin chains and uses its adenosine triphosphatase (ATPase) motor for mechanical unfolding and translocation into a proteolytic chamber. Here, we used single-molecule Förster resonance...
Autores principales: | Jonsson, Erik, Htet, Zaw Min, Bard, Jared A. M., Dong, Ken C., Martin, Andreas |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Association for the Advancement of Science
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9788759/ https://www.ncbi.nlm.nih.gov/pubmed/36563145 http://dx.doi.org/10.1126/sciadv.add9520 |
Ejemplares similares
-
Conformational switching of the 26S proteasome enables substrate degradation
por: Matyskiela, Mary E., et al.
Publicado: (2013) -
Proteasome-associated ubiquitin ligase relays target plant hormone-specific transcriptional activators
por: Wang, Zhishuo, et al.
Publicado: (2022) -
ATP-competitive inhibitors modulate the substrate binding cooperativity of a kinase by altering its conformational entropy
por: Olivieri, Cristina, et al.
Publicado: (2022) -
Ubp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome
por: Bashore, Charlene, et al.
Publicado: (2015) -
PRP4KA phosphorylates SERRATE for degradation via 20S proteasome to fine-tune miRNA production in Arabidopsis
por: Wang, Lin, et al.
Publicado: (2022)