ArticleNucleic acids research2010
hMSH5 is a nucleocytoplasmic shuttling protein whose stability depends on its subcellular localization.
Article in Nucleic acids research, 2010. 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.
- Myospreader improves gene editing in skeletal muscle by myonuclear propagation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Myospreader improves gene editing in skeletal muscle by myonuclear propagation.bioRxiv : the preprint server for biology · 2023Article
- Catalytically Active Proteasomes Function Predominantly in the Cytosol.The Journal of biological chemistry · 2016Article
- Yeast importin-α (Srp1) performs distinct roles in the import of nuclear proteins and in targeting proteasomes to the nucleus.The Journal of biological chemistry · 2014Article
- Degradation of specific nuclear proteins occurs in the cytoplasm in Saccharomyces cerevisiae.Genetics · 2014Article
- MutS Homologues hMSH4 and hMSH5: Genetic Variations, Functions, and Implications in Human Diseases.Current genomics · 2013Article
- Nucleocytoplasmic shuttling and CRM1-dependent MHC class I peptide presentation of human cytomegalovirus pp65.Medical microbiology and immunology · 2012Article
- MutS homologue hMSH5: role in cisplatin-induced DNA damage response.Molecular cancer · 2012Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
MSH5 is a MutS-homologous protein required for meiotic DNA recombination. In addition, recent studies suggest that the human MSH5 protein (hMSH5) participates to mitotic recombination and to the cellular response to DNA damage and thus raise the possibility that a tight control of hMSH5 function(s) may be important for genomic stability. With the aim to characterize mechanisms potentially involved in the regulation of hMSH5 activity, we investigated its intracellular trafficking properties. We demonstrate that hMSH5 possesses a CRM1-dependent nuclear export signal (NES) and a nuclear localization signal that participates to its nuclear targeting. Localization analysis of various mutated forms of hMSH5 by confocal microscopy indicates that hMSH5 shuttles between the nucleus and the cytoplasm. We also provide evidence suggesting that hMSH5 stability depends on its subcellular compartmentalization, hMSH5 being much less stable in the nucleus than in the cytoplasm. Together, these data suggest that hMSH5 activity may be regulated by nucleocytoplasmic shuttling and nuclear proteasomal degradation, both of these mechanisms contributing to the control of nuclear hMSH5 content. Moreover, data herein also support that in tissues where both hMSH5 and hMSH4 proteins are expressed, hMSH5 might be retained in the nucleus through masking of its NES by binding of hMSH4.
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