ArticleMolecular biology reports2014
Selective interactions of hnRNP M isoforms with the TET proteins TAF15 and TLS/FUS.
Article in Molecular biology reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Evolutionary Analysis of the hnRNP Interactomes and Their Functions in Eukaryotes.Biochemical genetics · 2025Article
- The role of hnRNPs in frontotemporal dementia and amyotrophic lateral sclerosis.Acta neuropathologica · 2020Review
- Identification and Characterization of Sindbis Virus RNA-Host Protein Interactions.Journal of virology · 2018Article
- Genetic mutations in RNA-binding proteins and their roles in ALS.Human genetics · 2017Review
- Minor intron splicing is regulated by FUS and affected by ALS-associated FUS mutants.The EMBO journal · 2016Article
- The Genome-Wide Analysis of Carcinoembryonic Antigen Signaling by Colorectal Cancer Cells Using RNA Sequencing.PloS one · 2016Article
- Heterogeneous Nuclear Ribonucleoprotein M Facilitates Enterovirus Infection.Journal of virology · 2015Article
- Aberrant RNA homeostasis in amyotrophic lateral sclerosis: potential for new therapeutic targets?Neurodegenerative disease management · 2014Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The molecular composition of macromolecular assemblies engaged in transcription and splicing influences biogenesis of mRNA transcripts. Preference for one over the other interactive protein partner within those complexes is expected to change the gene expression pattern and to affect subsequent cellular events. We report here the novel and selective associations between RNA-binding proteins, namely the hnRNP M1-4 isoforms-involved in early spliceosome assembly and alternative splicing-and the transcription factors TAF15 and TLS/FUS. In immunoprecipitation studies on HeLa nuclear extracts, TAF15 co-immunoprecipitates preferably with the higher molecular weight hnRNP M3/4 isoforms, opposite to TLS/FUS that associates with the lower molecular weight hnRNP M1/2 species. We demonstrate that these associations can be mediated through direct protein-protein interactions via the amino-termini of the TET proteins, independently of RNA. Finally, we show partial co-localization of TAF15 and TLS/FUS with hnRNP M proteins in HeLa nuclei, supporting the biochemically obtained data. The participation of hnRNP M in an expanding network of protein-protein interactions suggests its important functioning in the coordination of transcriptional and post-transcriptional events.
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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.