The self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70
Abstract J-domain proteins tune the specificity of Hsp70s, engaging them in precise functions. Despite their essential role, the structure and function of many J-domain proteins remain largely unknown. We explore human DNAJA2, finding that it reversibly forms highly-ordered, tubular structures that...
Main Authors: | Lorea Velasco-Carneros, Jorge Cuéllar, Leire Dublang, César Santiago, Jean-Didier Maréchal, Jaime Martín-Benito, Moisés Maestro, José Ángel Fernández-Higuero, Natalia Orozco, Fernando Moro, José María Valpuesta, Arturo Muga |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Portfolio
2023-09-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-023-41150-8 |
Similar Items
-
Author Correction: The self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70
by: Lorea Velasco-Carneros, et al.
Published: (2024-01-01) -
Inhibition of the Human Hsc70 System by Small Ligands as a Potential Anticancer Approach
by: Leire Dublang, et al.
Published: (2021-06-01) -
Truncation-Driven Lateral Association of α-Synuclein Hinders Amyloid Clearance by the Hsp70-Based Disaggregase
by: Aitor Franco, et al.
Published: (2021-11-01) -
Unzipping the Secrets of Amyloid Disassembly by the Human Disaggregase
by: Aitor Franco, et al.
Published: (2021-10-01) -
Comparative analysis of the anticoagulant activities and immunogenicity of HSC70 and HSC70TKD of Haemaphysalis flava
by: Yu-Ke Liu, et al.
Published: (2022-11-01)