ArticleThe Journal of cell biology1994
Nuclear transport of U1 snRNP in somatic cells: differences in signal requirement compared with Xenopus laevis oocytes.
Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 45 citations in OpenAlex.
- The SMN complex drives structural changes in human snRNAs to enable snRNP assembly.Nature communications · 2023Article
- TGS1 impacts snRNA 3'-end processing, ameliorates survival motor neuron-dependent neurological phenotypes in vivo and prevents neurodegeneration.Nucleic acids research · 2022Article
- Loss of the RNA trimethylguanosine cap is compatible with nuclear accumulation of spliceosomal snRNAs but not pre-mRNA splicing or snRNA processing during animal development.PLoS genetics · 2020Article
- Cajal bodies and snRNPs - friends with benefits.RNA biology · 2017Review
- Identification and characterization of Drosophila Snurportin reveals a role for the import receptor Moleskin/importin-7 in snRNP biogenesis.Molecular biology of the cell · 2013Article
- Enhancement of U4/U6 small nuclear ribonucleoprotein particle association in Cajal bodies predicted by mathematical modeling.Molecular biology of the cell · 2006Article
- Ongoing U snRNP biogenesis is required for the integrity of Cajal bodies.Molecular biology of the cell · 2006Article
- The Herpesvirus saimiri small nuclear RNAs recruit AU-rich element-binding proteins but do not alter host AU-rich element-containing mRNA levels in virally transformed T cells.Molecular and cellular biology · 2004Article
- U4 snRNA nucleolar localization requires the NHPX/15.5-kD protein binding site but not Sm protein or U6 snRNA association.The Journal of cell biology · 2003Article
- SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex with snurportin1 and importin beta.Human molecular genetics · 2002Article
- The importin-beta binding domain of snurportin1 is responsible for the Ran- and energy-independent nuclear import of spliceosomal U snRNPs in vitro.The Journal of cell biology · 2002Article
- The box C/D motif directs snoRNA 5'-cap hypermethylation.Nucleic acids research · 2000Article
- Functional characterization of nuclear localization signals in yeast Sm proteins.Molecular and cellular biology · 2000Article
- Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin.The EMBO journal · 1999Article
- Snurportin1, an m3G-cap-specific nuclear import receptor with a novel domain structure.The EMBO journal · 1998Article
- Nucleolar localization elements in U8 snoRNA differ from sequences required for rRNA processing.RNA (New York, N.Y.) · 1998Article
- Interactions within the yeast Sm core complex: from proteins to amino acids.Molecular and cellular biology · 1998Article
- A 7-methylguanosine cap commits U3 and U8 small nuclear RNAs to the nucleolar localization pathway.Nucleic acids research · 1998Article
- AU-rich elements target small nuclear RNAs as well as mRNAs for rapid degradation.Genes & development · 1997Article
- Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The signal requirement for the nuclear import of U1 RNA in somatic cells from different species was investigated by microinjection of both digoxygenin-labeled wild type and mutant U1 RNA molecules and in vitro reconstituted U1 snRNPs. U1 RNA was shown to be targeted to the nucleus by a temperature-dependent process that requires the prior assembly of RNPs from the common proteins and the microinjected RNA. Competition in the cell between immunoaffinity-purified U1 snRNPs and digoxygenin-labeled U1 snRNPs reconstituted in vitro showed that the transport is saturable and should therefore be a mediated process. The transport of a karyophilic protein under the same conditions was not affected, indicating the existence of a U snRNP-specific transport pathway in somatic cells, as already seen in the Xenopus laevis oocyte system. Surprisingly, the signal requirement for nuclear transport of U1 snRNP was found to differ between oocytes and somatic cells from mouse, monkey and Xenopus, in that the m3GGpppG-cap is no longer an essential signaling component in somatic cells. However, as shown by investigation of the transport kinetics of m3GpppG- and ApppG-capped U1 snRNPs, the m3GpppG-cap accelerates the rate of U1 snRNP import significantly indicating that it has retained a signaling role for nuclear targeting of U1 snRNP in somatic cells. Moreover, our data strongly suggest that cell specific rather than species specific differences account for the differential m3G-cap requirement in nuclear import of U1 snRNPs.
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