ArticleScientific reports2015
RBM45 homo-oligomerization mediates association with ALS-linked proteins and stress granules.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 51 citations in OpenAlex.
- RBM45 Preferential Binding to mThe journal of physical chemistry. B · 2026Article
- Molecular interactome of HNRNPU reveals regulatory networks in neuronal differentiation and DNA methylation.Nucleic acids research · 2026Article
- Structured protein domains enter the spotlight: modulators of biomolecular condensate form and function.Trends in biochemical sciences · 2025Review
- Article
- RBM45 is an mCell reports · 2022Article
- SRSF protein kinase 1 modulates RAN translation and suppresses CGG repeat toxicity.EMBO molecular medicine · 2021Article
- Autophagy of the mNature communications · 2021Article
- Structural basis for RNA recognition by the N-terminal tandem RRM domains of human RBM45.Nucleic acids research · 2021Article
- The Molecular Assembly State of Drp1 Controls its Association With the Mitochondrial Recruitment Receptors Mff and MIEF1/2.Frontiers in cell and developmental biology · 2021Article
- RBM45 associates with nuclear stress bodies and forms nuclear inclusions during chronic cellular stress and in neurodegenerative diseases.Acta neuropathologica communications · 2020Article
- Article
- RNA recognition motifs of disease-linked RNA-binding proteins contribute to amyloid formation.Scientific reports · 2019Article
- Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis.Frontiers in molecular neuroscience · 2019Review
- The genomics of desmoplastic small round cell tumor reveals the deregulation of genes related to DNA damage response, epithelial-mesenchymal transition, and immune response.Cancer communications (London, England) · 2018Article
- RBM45 competes with HDAC1 for binding to FUS in response to DNA damage.Nucleic acids research · 2017Article
- Review
- ALS-FTLD associated mutations of SQSTM1 impact on Keap1-Nrf2 signalling.Molecular and cellular neurosciences · 2016Article
- Immunoprecipitation and mass spectrometry defines an extensive RBM45 protein-protein interaction network.Brain research · 2016Review
- Developmentally Regulated RNA-binding Protein 1 (Drb1)/RNA-binding Motif Protein 45 (RBM45), a Nuclear-Cytoplasmic Trafficking Protein, Forms TAR DNA-binding Protein 43 (TDP-43)-mediated Cytoplasmic Aggregates.The Journal of biological chemistry · 2016Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The aggregation of RNA-binding proteins is a pathological hallmark of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). RBM45 is an RNA-binding protein that forms cytoplasmic inclusions in neurons and glia in ALS and FTLD. To explore the role of RBM45 in ALS and FTLD, we examined the contribution of the protein's domains to its function, subcellular localization, and interaction with itself and ALS-linked proteins. We find that RBM45 forms homo-oligomers and physically associates with the ALS-linked proteins TDP-43 and FUS in the nucleus. Nuclear localization of RBM45 is mediated by a bipartite nuclear-localization sequence (NLS) located at the C-terminus. RBM45 mutants that lack a functional NLS accumulate in the cytoplasm and form TDP-43 positive stress granules. Moreover, we identify a novel structural element, termed the homo-oligomer assembly (HOA) domain, that is highly conserved across species and promote homo-oligomerization of RBM45. RBM45 mutants that fail to form homo-oligomers exhibit significantly reduced association with ALS-linked proteins and inclusion into stress granules. These results show that RMB45 may function as a homo-oligomer and that its oligomerization contributes to ALS/FTLD RNA-binding protein aggregation.
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