ReviewNucleus (Austin, Tex.)2012
CRM1 plays a nuclear role in transporting snoRNPs to nucleoli in higher eukaryotes.
Review in Nucleus (Austin, Tex.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
17 citing papers in PubMed, 31 citations in OpenAlex.
- Review
- Advances in understanding telomerase assembly.Biochemical Society transactions · 2023Review
- Viral Subversion of the Chromosome Region Maintenance 1 Export Pathway and Its Consequences for the Cell Host.Viruses · 2023Review
- Karyopherin-mediated nucleocytoplasmic transport.Nature reviews. Molecular cell biology · 2022Review
- Anomalous HIV-1 RNA, How Cap-Methylation Segregates Viral Transcripts by Form and Function.Viruses · 2022Review
- Emerging Data on the Diversity of Molecular Mechanisms Involving C/D snoRNAs.Non-coding RNA · 2021Review
- Intimate functional interactions between TGS1 and the Smn complex revealed by an analysis of the Drosophila eye development.PLoS genetics · 2020Article
- Loss of Human TGS1 Hypermethylase Promotes Increased Telomerase RNA and Telomere Elongation.Cell reports · 2020Article
- An Exportin-1-dependent microRNA biogenesis pathway during human cell quiescence.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- RNA modification in Cajal bodies.RNA biology · 2017Review
- Nucleocytoplasmic transport of nucleocapsid proteins of enveloped RNA viruses.Frontiers in microbiology · 2015Review
- Binding of carbonic anhydrase IX to 45S rDNA genes is prevented by exportin-1 in hypoxic cells.BioMed research international · 2015Article
- Separate responses of karyopherins to glucose and amino acid availability regulate nucleocytoplasmic transport.Molecular biology of the cell · 2014Article
- Nuclear export of human hepatitis B virus core protein and pregenomic RNA depends on the cellular NXF1-p15 machinery.PloS one · 2014Article
- NC-mediated nucleolar localization of retroviral gag proteins.Virus research · 2013Article
- CRM1 and its ribosome export adaptor NMD3 localize to the nucleolus and affect rRNA synthesis.Nucleus (Austin, Tex.)Article
- Early embryonic lethality of mice with disrupted transcription cofactor PIMT/NCOA6IP/Tgs1 gene.Mechanisms of developmentArticle
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Here, we review the sn- and sno-RNA transport pathways in S. cerevisiae and humans, aiming at understanding how they evolved and how common factors can have distinct functions depending on the RNA they bind. We give a particular emphasis on Tgs1, the cap hypermethylase that is conserved from yeast to humans and appears to play a central role in both sn- and sno-RNA biogenesis. In yeast, Tgs1 hypermethylates sn- and sno-RNAs in the nucleolus. In humans, Tgs1 occurs in two forms: a long isoform (Tgs1 LF), which locates in the cytoplasm and Cajal bodies, which is predominantly associated with snRNAs and a short isoform (Tgs1 SF), which is nuclear and mainly associates with snoRNAs. We show that Tgs1 LF is exported by CRM1 and that interaction with CRM1 competes for binding with the C-terminal domain of the core protein Nop58, which contains the Nucleolar localization signal of Box C/D snoRNPs (NoLS). Our data suggest a model where CRM1 removes Tgs1 LF from snoRNPs, thereby promoting nucleolar targeting via activation of their NoLS. In this review, we argue that CRM1, while first described as an export receptor, can also control the composition of nucleoplasmic complexes. Thus, it could coordinate the fate of these complexes with the general nucleo-cytoplasmic trafficking.
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