Discover Community Create You

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

Molecular consequences of SCA5 mutations in the spectrin-repeat domains of β-III-spectrin.

The Journal of biological chemistry - 1 Jul 2025

Denha Sarah A, DeLaet Naomi R, Abukamil Abeer W, Alexopoulos Angelica N, Keller Amanda R, Thiel Matthew T, Atang Alexandra E, Avery Adam W

Abstract excerpt

Spinocerebellar ataxia type 5 (SCA5) mutations in the protein β-III-spectrin cluster to the N-terminal actin-binding domain (ABD) and the central spectrin-repeat domains (SRDs). We previously reported that a common molecular consequence of ABD-localized SCA5 mutations is increased actin binding. However, little is known about the molecular consequences of the SRD-localized mutations. It is known that the SRDs of...

Read the complete abstract on PubMed

Topics

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

Share to Actins
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Binding

Share to Protein Domains

Share to Spectrin

Share to Spinocerebellar Ataxias

Source

Open in PubMed Open full text

Identifiers

PMID: 40484375
DOI: 10.1016/j.jbc.2025.110350
PMCID: PMC12269838

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Molecular consequences of SCA5 mutations in the spectrin-repeat domains of β-III-spectrin.PMID 40484375Read ↗

Increased Actin Binding Is a Shared Molecular Consequence of Numerous SCA5 Mutations in β-III-Spectrin.Semantic proximity Read ↗

Increased actin binding is a shared molecular consequence of numerous spinocerebellar ataxia mutations in β-III-spectrinSemantic proximity Read ↗

A human β-III-spectrin spinocerebellar ataxia type 5 mutation causes high-affinity F-actin binding.Semantic proximity Read ↗

β-III-spectrin spinocerebellar ataxia type 5 mutation reveals a dominant cytoskeletal mechanism that underlies dendritic arborization.Semantic proximity Read ↗

-III spectrin mutation L253P associated with spinocerebellar ataxia type 5 interferes with binding to Arp1 and protein trafficking from the GolgiSemantic proximity Read ↗

Spinocerebellar ataxia type 5.Semantic proximity Read ↗

β-III-spectrin N-terminus is required for high-affinity actin binding and SCA5 neurotoxicity.Semantic proximity Read ↗

Spectrin: structure, function and disease.Semantic proximity Read ↗

β-III spectrin underpins ankyrin R function in Purkinje cell dendritic trees: protein complex critical for sodium channel activity is impaired by SCA5-associated mutations.Semantic proximity Read ↗

Spectrin mutations that cause spinocerebellar ataxia type 5 impair axonal transport and induce neurodegeneration in Drosophila.Semantic proximity Read ↗

Cerebellar ataxias: β-III spectrin's interactions suggest common pathogenic pathways.Semantic proximity Read ↗

βII spectrin (SPTBN1): biological function and clinical potential in cancer and other diseasesSemantic proximity Read ↗

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