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

Mutant huntingtin alters Tau phosphorylation and subcellular distribution.

Human molecular genetics - 1 Jan 2015

Blum David, Herrera Federico, Francelle Laetitia, Mendes Tiago, Basquin Marie, Obriot Hélène, Demeyer Dominique, Sergeant Nicolas, Gerhardt Ellen, Brouillet Emmanuel, Buée Luc, Outeiro Tiago F

Abstract excerpt

Tau abnormalities play a central role in several neurodegenerative diseases, collectively known as tauopathies. In the present study, we examined whether mutant huntingtin (mHtt), which causes Huntington's disease (HD), modifies Tau phosphorylation and subcellular localization using cell and mouse HD models. Initially, we used novel bimolecular fluorescence complementation assays in live cells to evaluate Tau...

Read the complete abstract on PubMed

Topics

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

Share to HEK293 Cells
Share to Huntingtin Protein

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Huntington Disease

Share to Nerve Tissue Proteins

Share to Phosphorylation

Share to Protein Transport

Share to Serotonin Plasma Membrane Transport Proteins

Share to tau Proteins

Source

Identifiers

PMID: 25143394
DOI: 10.1093/hmg/ddu421

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutant huntingtin alters Tau phosphorylation and subcellular distribution.PMID 25143394Read ↗

Implications of Tau Dysregulation in Huntington’s Disease and Potential for New TherapeuticsSemantic proximity Read ↗

Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neuronsSemantic proximity Read ↗

The Pathogenic R5L Mutation Disrupts Formation of Tau Complexes on the Microtubule by Altering Local N-Terminal StructureSemantic proximity Read ↗

The pathogenic R5L mutation disrupts formation of Tau complexes on the microtubule by altering local N-terminal structure.Semantic proximity Read ↗

Altered Levels and Isoforms of Tau and Nuclear Membrane Invaginations in Huntington’s DiseaseSemantic proximity Read ↗

Multiple pathways contribute to the pathogenesis of Huntington disease.Semantic proximity Read ↗

Protein phosphatase 1 regulates huntingtin exon 1 aggregation and toxicitySemantic proximity Read ↗

Huntingtin inclusion bodies have distinct immunophenotypes and ubiquitination profiles in the Huntington’s disease human cerebral cortexSemantic proximity Read ↗

Mutated tau binds less avidly to microtubules than wildtype tau in living cells.Semantic proximity Read ↗

Mutant Huntingtin Protein Interaction Map Implicates Dysregulation of Multiple Cellular Pathways in Neurodegeneration of Huntington’s DiseaseSemantic proximity Read ↗

Microtubule-dependent oligomerization of tau. Implications for physiological tau function and tauopathies.Semantic proximity Read ↗

The role of tau in the pathological process and clinical expression of Huntington's disease.Semantic proximity Read ↗

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