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

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

doi:10.1038/s41467-022-32370-5

Nature Communications (Aug 2022)

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

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

Affiliations

S. M. Ayala Mariscal: Leibniz Research Institute for Molecular Pharmacology (FMP) im Forschungsverbund Berlin e.V. (FMP)
M. L. Pigazzini: Leibniz Research Institute for Molecular Pharmacology (FMP) im Forschungsverbund Berlin e.V. (FMP)
Y. Richter: Department of Cell Biology, University of Bremen
M. Özel: Department of Cell Biology, University of Bremen
I. L. Grothaus: Hybrid Materials Interfaces Group, Faculty of Production Engineering and Bremen Center for Computational Materials Science, University of Bremen
J. Protze: Leibniz Research Institute for Molecular Pharmacology (FMP) im Forschungsverbund Berlin e.V. (FMP)
K. Ziege: Leibniz Research Institute for Molecular Pharmacology (FMP) im Forschungsverbund Berlin e.V. (FMP)
M. Kulke: MSU-DOE-Plant Research Laboratory, Michigan State University
M. ElBediwi: Department of Cell Biology, University of Bremen
J. V. Vermaas: MSU-DOE-Plant Research Laboratory, Michigan State University
L. Colombi Ciacchi: Hybrid Materials Interfaces Group, Faculty of Production Engineering and Bremen Center for Computational Materials Science, University of Bremen
S. Köppen: Hybrid Materials Interfaces Group, Faculty of Production Engineering and Bremen Center for Computational Materials Science, University of Bremen
F. Liu: Leibniz Research Institute for Molecular Pharmacology (FMP) im Forschungsverbund Berlin e.V. (FMP)
J. Kirstein: Leibniz Research Institute for Molecular Pharmacology (FMP) im Forschungsverbund Berlin e.V. (FMP)

DOI: https://doi.org/10.1038/s41467-022-32370-5
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 25

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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