ArticleProceedings of the National Academy of Sciences of the United States of America1999
Evidence for specific nucleocytoplasmic transport pathways used by leucine-rich nuclear export signals.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 95 citations in OpenAlex.
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- Nucleus-exported CLOCK acetylates PRPS to promote de novo nucleotide synthesis and liver tumour growth.Nature cell biology · 2023Article
- Human Retrovirus Genomic RNA Packaging.Viruses · 2022Review
- Bracovirus Sneaks Into Apoptotic Bodies Transmitting Immunosuppressive Signaling Driven by Integration-Mediated eIF5A Hypusination.Frontiers in immunology · 2022Article
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- A translational program that suppresses metabolism to shield the genome.Nature communications · 2020Article
- Article
- Hypusination of eIF5A as a Target for Antiviral Therapy.DNA and cell biology · 2017Article
- Nuclear Export Signal Masking Regulates HIV-1 Rev Trafficking and Viral RNA Nuclear Export.Journal of virology · 2017Article
- Statistical dissection of cyto-nuclear epistasis subject to genomic imprinting in line crosses.PloS one · 2014Article
- Proteomic and functional analyses of protein-DNA complexes during gene transfer.Molecular therapy : the journal of the American Society of Gene Therapy · 2013Article
- A nuclear export signal in the matrix protein of Influenza A virus is required for efficient virus replication.Journal of virology · 2012Article
- Probing of the nuclear import and export signals and subcellular transport mechanism of varicella-zoster virus tegument protein open reading frame 10.Medical microbiology and immunology · 2012Article
- Contribution of DEAF1 structural domains to the interaction with the breast cancer oncogene LMO4.PloS one · 2012Article
- The first identified nucleocytoplasmic shuttling herpesviral capsid protein: herpes simplex virus type 1 VP19C.PloS one · 2012Article
- RceIF5A, encoding an eukaryotic translation initiation factor 5A in Rosa chinensis, can enhance thermotolerance, oxidative and osmotic stress resistance of Arabidopsis thaliana.Plant molecular biology · 2011Article
- Inhibition of deoxyhypusine synthase enhances islet {beta} cell function and survival in the setting of endoplasmic reticulum stress and type 2 diabetes.The Journal of biological chemistry · 2010Article
- Domain- and nucleotide-specific Rev response element regulation of feline immunodeficiency virus production.Virology · 2010Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Various proteins with different biological activities have been observed to be translocated from the nucleus to the cytoplasm in an energy- and signal-dependent manner in eukaryotic cells. This nuclear export is directed by nuclear export signals (NESs), typically characterized by hydrophobic, primarily leucine, amino acid residues. Moreover, it has been shown that CRM1/exportin 1 is an export receptor for leucine-rich NESs. However, additional NES-interacting proteins have been described. In particular, eukaryotic initiation factor 5A (eIF-5A) has been shown to be a critical cellular cofactor for the nuclear export of the HIV type 1 (HIV-1) Rev trans-activator protein. In this study we compared the nuclear export activity of NESs of different origin. Microinjection of export substrates into the nucleus of somatic cells in combination with specific inhibitors indicated that specific nuclear export pathways exist for different NES-containing proteins. In particular, inhibition of eIF-5A blocked the nuclear export of NESs derived from the HIV-1 Rev and human T cell leukemia virus type I Rex trans-activators, whereas nucleocytoplasmic translocation of the protein kinase inhibitor-NES was unaffected. In contrast, however, inhibition of CRM1/exportin 1 blocked the nuclear export of all NES-containing proteins investigated. Our data confirm that CRM1/exportin 1 is a general export receptor for leucine-rich NESs and suggest that eIF-5A acts either upstream of CRM1/exportin 1 or forms a complex with the NES and CRM1/exportin 1 in the nucleocytoplasmic translocation of the HIV-1 Rev and human T cell leukemia virus type I Rex RNA export factors.
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