Identification of a HTT-specific binding motif in DNAJB1 essential for suppression and disaggregation of HTT

Ayala Mariscal et al have identified and characterized the interface of pathogenic Huntingtin and the molecular chaperone DNAJB1. Histidine-244 of the C-terminal domain of DNAJB1 is a key residues for binding to the poly-proline region of HTT. This binding site is specific for the interaction with H...

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Bibliographic Details
Main Authors: S. M. Ayala Mariscal, M. L. Pigazzini, Y. Richter, M. Özel, I. L. Grothaus, J. Protze, K. Ziege, M. Kulke, M. ElBediwi, J. V. Vermaas, L. Colombi Ciacchi, S. Köppen, F. Liu, J. Kirstein
Format: Article
Language:English
Published: Nature Portfolio 2022-08-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-022-32370-5
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Summary:Ayala Mariscal et al have identified and characterized the interface of pathogenic Huntingtin and the molecular chaperone DNAJB1. Histidine-244 of the C-terminal domain of DNAJB1 is a key residues for binding to the poly-proline region of HTT. This binding site is specific for the interaction with Huntingtin.
ISSN:2041-1723