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Article

TBK1 phosphorylates mutant Huntingtin and suppresses its aggregation and toxicity in Huntington's disease models.

The EMBO journal - 1 Sept 2020

Hegde Ramanath Narayana, Chiki Anass, Petricca Lara, Martufi Paola, Arbez Nicolas, Mouchiroud Laurent, Auwerx Johan, Landles Christian, Bates Gillian P, Singh-Bains Malvindar K, Dragunow Mike, Curtis Maurice A, Faull Richard Lm, Ross Christopher A, Caricasole Andrea, Lashuel Hilal A

Abstract excerpt

Phosphorylation of the N-terminal domain of the huntingtin (HTT) protein has emerged as an important regulator of its localization, structure, aggregation, clearance and toxicity. However, validation of the effect of bona fide phosphorylation in vivo and assessing the therapeutic potential of targeting phosphorylation for the treatment of Huntington's disease (HD) require the identification of the enzymes that...

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Source

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Identifiers

PMID: 32757223
DOI: 10.15252/embj.2020104671
PMCID: PMC7459410

Genes

HTT
TBK1
TANK

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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