Cargando…
Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone
Cytosolic HSP90 requires multiple cochaperones in folding client proteins. However, the function of gp96 (HSP90b1, grp94), an HSP90 paralogue in the endoplasmic reticulum (ER), is believed to be independent of cochaperones. Here, we demonstrate that gp96 chaperones multiple Toll-like receptors (TLRs...
Autores principales: | Liu, Bei, Yang, Yi, Qiu, Zhijuan, Staron, Matthew, Hong, Feng, Li, Yi, Wu, Shuang, Li, Yunfeng, Hao, Bing, Bona, Robert, Han, David, Li, Zihai |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2982182/ https://www.ncbi.nlm.nih.gov/pubmed/20865800 http://dx.doi.org/10.1038/ncomms1070 |
Ejemplares similares
-
Erratum: Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone
por: Liu, Bei, et al.
Publicado: (2012) -
Hsp90 mutants with distinct defects provide novel insights into cochaperone regulation of the folding cycle
por: Mercier, Rebecca, et al.
Publicado: (2023) -
GP96: safeguarding Treg
por: Zhang, Yongliang, et al.
Publicado: (2015) -
The cochaperone CHIP marks Hsp70- and Hsp90-bound substrates for degradation through a very flexible mechanism
por: Quintana-Gallardo, Lucía, et al.
Publicado: (2019) -
Induction of Foxp3 and activation of Tregs by HSP gp96 for treatment of autoimmune diseases
por: Xu, Yuxiu, et al.
Publicado: (2021)