Cargando…
Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules
The cochaperone Sti1/Hop physically links Hsp70 and Hsp90. The protein exhibits one binding site for Hsp90 (TPR2A) and two binding sites for Hsp70 (TPR1 and TPR2B). How these sites are used remained enigmatic. Here we show that Sti1 is a dynamic, elongated protein that consists of a flexible N-termi...
Autores principales: | Röhl, Alina, Wengler, Daniela, Madl, Tobias, Lagleder, Stephan, Tippel, Franziska, Herrmann, Monika, Hendrix, Jelle, Richter, Klaus, Hack, Gordon, Schmid, Andreas B., Kessler, Horst, Lamb, Don C., Buchner, Johannes |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Pub. Group
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4403447/ https://www.ncbi.nlm.nih.gov/pubmed/25851214 http://dx.doi.org/10.1038/ncomms7655 |
Ejemplares similares
-
The Hsp70/90 cochaperone, Sti1, suppresses proteotoxicity by regulating spatial quality control of amyloid-like proteins
por: Wolfe, Katie J., et al.
Publicado: (2013) -
Hop/Sti1 phosphorylation inhibits its co-chaperone function
por: Röhl, Alina, 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) -
The Complex Phosphorylation Patterns That Regulate the Activity of Hsp70 and Its Cochaperones
por: Velasco, Lorea, et al.
Publicado: (2019) -
Mutations in Hsp90 Cochaperones Result in a Wide Variety of Human Disorders
por: Johnson, Jill L.
Publicado: (2021)