CRM1-dependent nuclear export and dimerization with hMSH5 contribute to the regulation of hMSH4 subcellular localization
| Autor: | Sabine Santucci-Darmanin, Pascal Staccini, Sophie Neyton, François Lahaye, Véronique Paquis-Flucklinger, Françoise Lespinasse |
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| Přispěvatelé: | Institut de signalisation, biologie du développement et cancer (ISBDC), Centre National de la Recherche Scientifique (CNRS)-Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Université Côte d'Azur (UCA), Equipe M3R, COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Université Côte d'Azur (UCA)-Centre National de la Recherche Scientifique (CNRS)-Université Nice Sophia Antipolis (... - 2019) (UNS) |
| Jazyk: | angličtina |
| Rok vydání: | 2007 |
| Předmět: |
Male
Cytoplasm [SDV]Life Sciences [q-bio] Molecular Sequence Data Active Transport Cell Nucleus Receptors Cytoplasmic and Nuclear Mutagenesis (molecular biology technique) Cell Cycle Proteins Mice Inbred Strains Karyopherins Biology Mice 03 medical and health sciences 0302 clinical medicine Testis Animals Humans Amino Acid Sequence Nuclear export signal ComputingMilieux_MISCELLANEOUS 030304 developmental biology Cell Nucleus Nuclear Export Signals 0303 health sciences Cell Biology Subcellular localization Mice Mutant Strains Protein Structure Tertiary Cell biology MSH5 MSH4 030220 oncology & carcinogenesis Fatty Acids Unsaturated Homologous recombination Dimerization Nuclear localization sequence |
| Zdroj: | Experimental Cell Research Experimental Cell Research, Elsevier, 2007, 313 (17), pp.3680-3693. ⟨10.1016/j.yexcr.2007.08.010⟩ |
| ISSN: | 0014-4827 1090-2422 |
| DOI: | 10.1016/j.yexcr.2007.08.010⟩ |
| Popis: | MSH4 and MSH5 are members of the MutS homolog family, a conserved group of proteins involved in DNA mismatch correction and homologous recombination. Although several studies have provided compelling evidences suggesting that MSH4 and MSH5 could act together in early and late stages of meiotic recombination, their precise roles are poorly understood and recent findings suggest that the human MSH4 protein may also exert a cytoplasmic function. Here we show that MSH4 is present in the cytoplasm and the nucleus of both testicular cells and transfected somatic cells. Confocal studies on transfected cells provide the first evidence that the subcellular localization of MSH4 is regulated, at least in part, by an active nuclear export pathway dependent on the exportin CRM1. We used deletion mapping and mutagenesis to define two functional nuclear export sequences within the C-terminal part of hMSH4 that mediate nuclear export through the CRM1 pathway. Our results suggest that CRM1 is also involved in MSH5 nuclear export. In addition, we demonstrate that dimerization of MSH4 and MSH5 facilitates their nuclear localization suggesting that dimerization may regulate the intracellular trafficking of these proteins. Our findings suggest that nucleocytoplasmic traffic may constitute a regulatory mechanism for MSH4 and MSH5 functions. |
| Databáze: | OpenAIRE |
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