ArticleThe Biochemical journal2002
Association of the 72/74-kDa proteins, members of the heterogeneous nuclear ribonucleoprotein M group, with the pre-mRNA at early stages of spliceosome assembly.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- The scaffold protein IQGAP1 links heat-induced stress signals to alternative splicing regulation in gastric cancer cells.Oncogene · 2021Article
- hnRNPM induces translation switch under hypoxia to promote colon cancer development.EBioMedicine · 2019Article
- hnRNPM guides an alternative splicing program in response to inhibition of the PI3K/AKT/mTOR pathway in Ewing sarcoma cells.Nucleic acids research · 2017Article
- Roles of Sumoylation in mRNA Processing and Metabolism.Advances in experimental medicine and biology · 2017Review
- An unbiased proteomics approach to identify human cytomegalovirus RNA-associated proteins.Virology · 2015Article
- Heterogeneous Nuclear Ribonucleoprotein M Facilitates Enterovirus Infection.Journal of virology · 2015Article
- Selective interactions of hnRNP M isoforms with the TET proteins TAF15 and TLS/FUS.Molecular biology reports · 2014Article
- Antagonistic effects of cellular poly(C) binding proteins on vesicular stomatitis virus gene expression.Journal of virology · 2011Article
- Comparative 3'UTR analysis allows identification of regulatory clusters that drive Eph/ephrin expression in cancer cell lines.PloS one · 2008Article
- NFX1-123 and poly(A) binding proteins synergistically augment activation of telomerase in human papillomavirus type 16 E6-expressing cells.Journal of virology · 2007Article
- DNA topoisomerase I is a cofactor for c-Jun in the regulation of epidermal growth factor receptor expression and cancer cell proliferation.Molecular and cellular biology · 2005Article
- Hrp59, an hnRNP M protein in Chironomus and Drosophila, binds to exonic splicing enhancers and is required for expression of a subset of mRNAs.The Journal of cell biology · 2005Article
- The WW domain-containing proteins interact with the early spliceosome and participate in pre-mRNA splicing in vivo.Molecular and cellular biology · 2004Article
- SUMO modification of heterogeneous nuclear ribonucleoproteins.Molecular and cellular biology · 2004Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have investigated the role played in precursor mRNA (pre-mRNA) splicing by the protein pair of molecular size 72/74 kDa, which are integral components of a discrete subset of heterogeneous nuclear (hn) ribonucleoproteins (RNPs) named large heterogeneous nuclear RNP (LH-nRNP). This 72/74 kDa pair of proteins has been shown to belong to the hnRNP M group, and are referred to as 72/74(M). By applying specific immunoprecipitation assays in a consecutive series of splicing reactions in vitro, the antigenic 72/74(M) protein species were found to associate with the pre-mRNA and not the intermediate or final products of splicing. Kinetic studies, combined with isolation of pre-spliceosomal and spliceosomal complexes from the splicing reaction, indicated a loose association of 72/74(M) with both the initially formed H assembly and the first splicing-committed E complex. Stable binding was seen at a later stage of the reaction, well in advance of the appearance of the first intermediate products of RNA splicing. Evidence is provided that supports the almost exclusive association of 72/74(M) with pre-mRNA within the pre-spliceosomal A complex. This dynamic binding appeared to involve pre-mRNA sites similar to those of spliceosomal U1 and U2 small nuclear RNP complexes. Moreover, a preferential binding to a truncated RNA containing the 5' exon-intron part, rather than the intron-3' exon part, of pre-mRNA was observed.
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