Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Truncation mutation of CHMP2B disrupts late endosome function but reduces TDP-43 aggregation through HSP70 upregulation.

Neurochemistry international - 1 Jul 2025

Iguchi Yohei, Takahashi Yuhei, Li Jiayi, Amakusa Yoshinobu, Kawakami Yu, Yoshimura Takashi, Chikuchi Ryo, Iida Madoka, Yokoi Satoshi, Katsuno Masahisa

Abstract excerpt

TAR DNA-binding protein 43 (TDP-43)-positive cytoplasmic aggregation is a pathological hallmark of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). This aggregation contributes substantially to the neurodegeneration of ALS and FTLD. The endosome, a key component of membrane trafficking in eukaryotic cells and is involved in the autophagy-lysosome pathway. Endosome-related genes...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to DNA-Binding Proteins
Share to Endosomal Sorting Complexes Required for Transport

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endosomes

Share to Frontotemporal Dementia

Share to HEK293 Cells

Share to HSP70 Heat-Shock Proteins

Share to Protein Aggregation, Pathological

Share to Up-Regulation

Source

Identifiers

PMID: 40316175
DOI: 10.1016/j.neuint.2025.105982

Genes

CHMP2B
TMEM106B

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Truncation mutation of CHMP2B disrupts late endosome function but reduces TDP-43 aggregation through HSP70 upregulation.PMID 40316175Read ↗

The role of CHMP2BIntron5 in autophagy and frontotemporal dementia.Semantic proximity Read ↗

Disruption of endocytic trafficking in frontotemporal dementia with CHMP2B mutations.Semantic proximity Read ↗

Frontotemporal dementia caused by CHMP2B mutations.Semantic proximity Read ↗

CHMP2B regulates TDP-43 phosphorylation and proteotoxicity via modulating CK1 turnover independent of the autophagy-lysosomal pathwaySemantic proximity Read ↗

Lessons learned from CHMP2B, implications for frontotemporal dementia and amyotrophic lateral sclerosis.Semantic proximity Read ↗

The role of CHMP2B in frontotemporal dementiaSemantic proximity Read ↗

Lysosome dysfunction as a cause of neurodegenerative diseases: Lessons from frontotemporal dementia and amyotrophic lateral sclerosisSemantic proximity Read ↗

C9orf72 deficiency impairs the autophagic response to aggregated TDP-25 and exacerbates TDP-25-mediated neurodegeneration in vivoSemantic proximity Read ↗

TDP-43 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis: From pathomechanisms to therapeutic strategiesSemantic proximity Read ↗

Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease.Semantic proximity Read ↗

Mislocalization of FTD3-associated mutant CHMP2B to the nucleus of human neurons due to loss of a nuclear export signal.Semantic proximity Read ↗

ESCRT, autophagy, and frontotemporal dementia.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.