Article

OPTN translocates to an ATG9A-positive compartment to regulate innate immune signalling and cytokine secretion

2019-08-22

Abstract excerpt

Optineurin (OPTN) is a multifunctional protein involved in autophagy, secretion as well as NF-κB and IRF3 signalling and mutations are associated with several human diseases including primary open-angle glaucoma (POAG), amyotrophic lateral sclerosis (ALS), Paget’s disease of bone (PDB) and Crohn’s disease (CD). Here we show that, in response to viral RNA, OPTN translocates to foci in the perinuclear region, where...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: a6b61224-4766-5da7-bc32-2d55f8b16d0d
DOI: 10.1101/744672

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

OPTN translocates to an ATG9A-positive compartment to regulate innate immune signalling and cytokine secretionDOI 10.1101/744672Read

Cellular Functions of Optineurin in Health and Disease.Semantic proximity Read

Emerging views of OPTN (optineurin) function in the autophagic process associated with diseaseSemantic proximity Read

Toward an integrative view of Optineurin functionsSemantic proximity Read

Role of Optineurin in the Mitochondrial Dysfunction: Potential Implications in Neurodegenerative Diseases and CancerSemantic proximity Read

Optineurin: A Coordinator of Membrane-Associated Cargo Trafficking and Autophagy.Semantic proximity Read

Dysfunction of Optineurin in Amyotrophic Lateral Sclerosis and Glaucoma.Semantic proximity Read

Fundamental roles of the Optineurin gene in the molecular pathology of Amyotrophic Lateral SclerosisSemantic proximity Read

Altered Functions and Interactions of Glaucoma-Associated Mutants of Optineurin.Semantic proximity Read

Optineurin deficiency impairs autophagy to cause interferon beta overproduction and increased survival of mice following viral infectionSemantic proximity Read

Linear ubiquitination is involved in the pathogenesis of optineurin-associated amyotrophic lateral sclerosis.Semantic proximity Read

Structural insights into the interaction and disease mechanism of neurodegenerative disease-associated optineurin and TBK1 proteins.Semantic proximity Read

Mutations in the ubiquitin-binding domain of OPTN/optineurin interfere with autophagy-mediated degradation of misfolded proteins by a dominant-negative mechanism.Semantic proximity Read