ArticleRNA (New York, N.Y.)2015
A conserved charged single α-helix with a putative steric role in paraspeckle formation.
Article in RNA (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- The gene-regulating proteins NONO and SFPQ assemble into ordered filaments.Communications biology · 2025Article
- Structural plasticity of the coiled-coil interactions in human SFPQ.Nucleic acids research · 2025Article
- Distribution of disease-causing germline mutations in coiled-coils implies an important role of their N-terminal region.Scientific reports · 2020Article
- PlaToLoCo: the first web meta-server for visualization and annotation of low complexity regions in proteins.Nucleic acids research · 2020Article
- Structural basis of the zinc-induced cytoplasmic aggregation of the RNA-binding protein SFPQ.Nucleic acids research · 2020Article
- Disentangling the complexity of low complexity proteins.Briefings in bioinformatics · 2020Review
- The Role of RNA in Biological Phase Separations.Journal of molecular biology · 2018Review
- Inhaled Pollutants: The Molecular Scene behind Respiratory and Systemic Diseases Associated with Ultrafine Particulate Matter.International journal of molecular sciences · 2017Review
- The DBHS proteins SFPQ, NONO and PSPC1: a multipurpose molecular scaffold.Nucleic acids research · 2016Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Paraspeckles are subnuclear particles involved in the regulation of mRNA expression. They are formed by the association of DBHS family proteins and the NEAT1 long noncoding RNA. Here, we show that a recently identified structural motif, the charged single α-helix, is largely conserved in the DBHS family. Based on the available structural data and a previously suggested multimerization scheme of DBHS proteins, we built a structural model of a (PSPC1/NONO)(n) multimer that might have relevance in paraspeckle formation. Our model contains an extended coiled-coil region that is followed by and partially overlaps with the predicted charged single α-helix. We suggest that the charged single α-helix can act as an elastic ruler governing the exact positioning of the dimeric core structures relative to each other during paraspeckle assembly along the NEAT1 noncoding RNA.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.