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

Tyrosine phosphorylation regulates hnRNPA2 granule protein partitioning and reduces neurodegeneration.

The EMBO journal - 1 Feb 2021

Ryan Veronica H, Perdikari Theodora M, Naik Mandar T, Saueressig Camillo F, Lins Jeremy, Dignon Gregory L, Mittal Jeetain, Hart Anne C, Fawzi Nicolas L

Abstract excerpt

mRNA transport in neurons requires formation of transport granules containing many protein components, and subsequent alterations in phosphorylation status can release transcripts for translation. Further, mutations in a structurally disordered domain of the transport granule protein hnRNPA2 increase its aggregation and cause hereditary proteinopathy of neurons, myocytes, and bone. We examine in vitro hnRNPA2...

Read the complete abstract on PubMed

Topics

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

Share to Animals, Genetically Modified
Share to Cytoplasmic Granules

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Heterogeneous-Nuclear Ribonucleoprotein Group A-B

Share to Microtubule-Associated Proteins

Share to Nerve Degeneration

Share to Neurodegenerative Diseases

Share to Protein Domains

Share to Tyrosine

Source

Open in PubMed Open full text

Identifiers

PMID: 33349959
DOI: 10.15252/embj.2020105001
PMCID: PMC7849316

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

Tyrosine phosphorylation regulates hnRNPA2 granule protein partitioning and reduces neurodegeneration.PMID 33349959Read ↗

Tyrosine phosphorylation regulates hnRNPA2 granule protein partitioning & reduces neurodegenerationSemantic proximity Read ↗

Characterization of HNRNPA1 mutations defines diversity in pathogenic mechanisms and clinical presentation.Semantic proximity Read ↗

The pathophysiology of neurodegenerative disease: Disturbing the balance between phase separation and irreversible aggregation.Semantic proximity Read ↗

DEFINING THE DIVERSITY OF HNRNPA1 MUTATIONS IN CLINICAL PHENOTYPE AND PATHOMECHANISMSemantic proximity Read ↗

Stress granule mediated protein aggregation and underlying gene defects in the FTD-ALS spectrumSemantic proximity Read ↗

Mechanistic View of hnRNPA2 Low-Complexity Domain Structure, Interactions, and Phase Separation Altered by Mutation and Arginine Methylation.Semantic proximity Read ↗

Toxic PR poly-dipeptides encoded by the <i>C9orf72</i> repeat expansion target Kapβ2 and dysregulate phase separation of low-complexity domainsSemantic proximity Read ↗

Disease-associated mutations affect TIA1 phase separation and aggregation in a proline-dependent manner.Semantic proximity Read ↗

Seeded aggregation of ANXA11 induces prion-like propagation, TDP-43 co-pathology and nucleocytoplasmic transport defectsSemantic proximity Read ↗

Cellular modifiers of TDP-43 phase transition and cytoplasmic aggregationSemantic proximity Read ↗

hnRNPDL Phase Separation Is Regulated by Alternative Splicing and Disease-Causing Mutations Accelerate Its Aggregation.Semantic proximity Read ↗

Pathological phase transitions in ALS-FTD impair dynamic RNA-protein granules.Semantic proximity Read ↗

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