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

The ARSACS disease protein sacsin controls lysosomal positioning and reformation by regulating microtubule dynamics.

The Journal of biological chemistry - 1 Sept 2022

Francis Vincent, Alshafie Walaa, Kumar Rahul, Girard Martine, Brais Bernard, McPherson Peter S

Abstract excerpt

Autosomal recessive spastic ataxia of Charlevoix-Saguenay is a fatal brain disorder featuring cerebellar neurodegeneration leading to spasticity and ataxia. This disease is caused by mutations in the SACS gene that encodes sacsin, a massive 4579-amino acid protein with multiple modular domains. However, molecular details of the function of sacsin are not clear. Here, using live cell imaging and biochemistry, we...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Heat-Shock Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lysosomes

Share to Microtubules

Share to Muscle Spasticity

Share to Mutation

Share to Spinocerebellar Ataxias

Source

Open in PubMed Open full text

Identifiers

PMID: 35933016
DOI: 10.1016/j.jbc.2022.102320
PMCID: PMC9437860

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The ARSACS disease protein sacsin controls lysosomal positioning and reformation by regulating microtubule dynamics.PMID 35933016Read ↗

Multi-omic profiling reveals the ataxia protein sacsin is required for integrin trafficking and synaptic organization.Semantic proximity Read ↗

Insights into SACS pathological attributes in autosomal recessive spastic ataxia of Charlevoix-Saguenay (ARSACS)☆.Semantic proximity Read ↗

Mitochondrial dysfunction and Purkinje cell loss in autosomal recessive spastic ataxia of Charlevoix-Saguenay (ARSACS)Semantic proximity Read ↗

Subcellular, biochemical and biophysical alterations in two glial cell models of ARSACSSemantic proximity Read ↗

Altered organization of the intermediate filament cytoskeleton and relocalization of proteostasis modulators in cells lacking the ataxia protein sacsinSemantic proximity Read ↗

HDAC inhibitor SAHA resolved intermediate filament bundling and defective autophagy caused by the lack of sacsin in ARSACS.Semantic proximity Read ↗

Cytosolic sequestration of spatacsin by Protein Kinase A and 14-3-3 proteins.Semantic proximity Read ↗

Genetics of Autosomal Recessive Spastic Ataxia of Charlevoix-Saguenay (ARSACS) and Role of Sacsin in Neurodegeneration.Semantic proximity Read ↗

Linking axonal degeneration to microtubule remodeling by Spastin-mediated microtubule severing.Semantic proximity Read ↗

CK1α, FAM83H, and FAM83B contribute to bundling of neurofilaments and are sequestered in cellular and mice models of ARSACSSemantic proximity Read ↗

Integrative Organelle-Based Functional Proteomics: In Silico Prediction of Impaired Functional Annotations in SACS KO Cell Model.Semantic proximity Read ↗

A reduction in Drp1-mediated fission compromises mitochondrial health in autosomal recessive spastic ataxia of Charlevoix SaguenaySemantic proximity Read ↗

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