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Article

ALS mutations disrupt self-association between the ubiquilin STI1 hydrophobic groove and internal placeholder sequences.

The EMBO journal - 1 Apr 2026

Onwunma Joan, Binsabaan Saeed, Allen Shawn P, Thanthirige Sachini R, Gaur Deepika, Sankaran Banumathi, Wohlever Matthew L

Abstract excerpt

Ubiquilins are molecular chaperones that play multifaceted roles in proteostasis, with point mutations in UBQLN2 leading to altered phase-separation properties and amyotrophic lateral sclerosis (ALS). Our mechanistic understanding of this essential process has been hindered by a lack of structural information on the STI1 domain, which is essential for ubiquilin chaperone activity and phase separation. Here, we...

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Share to Adaptor Proteins, Signal Transducing
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 41862640
DOI: 10.1038/s44318-026-00745-9
PMCID: PMC13083928

Genes

UBQLN2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

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