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Characterization of an Importin α/β‐recognized nuclear localization signal in β‐dystroglycan by Bárbara Lara‐Chacón; Mario Bermúdez de León; Daniel Leocadio; Pablo Gómez; Lizeth Fuentes‐Mera; Ivette Martínez‐Vieyra; Arturo Ortega; David A. Jans; Bulmaro Cisneros is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
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## Abstract β‐dystroglycan (β‐DG) is a widely expressed transmembrane protein that plays important roles in connecting the extracellular matrix to the cytoskeleton, and thereby contributing to plasma membrane integrity and signal transduction. We previously observed nuclear localization of β‐DG in cultured cell lines, implying the existence of a nuclear targeting mechanism that directs it to the nucleus instead of the plasma membrane. In this study, we delineate the nuclear import pathway of β‐DG, characterizing a functional nuclear localization signal (NLS) in the β‐DG cytoplasmic domain, within amino acids 776–782. The NLS either alone or in the context of the whole β‐DG protein was able to target the heterologous GFP protein to the nucleus, with site‐directed mutagenesis indicating that amino acids R^779^ and K^780^ are critical for NLS functionality. The nuclear transport molecules Importin (Imp)α and Impβ bound with high affinity to the NLS of β‐DG and were found to be essential for NLS‐dependent nuclear import in an in vitro reconstituted nuclear transport assay; cotransfection experiments confirmed the dependence on Ran for nuclear accumulation. Intriguingly, experiments sug
Who reads Characterization of an Importin α/β‐recognized nuclear localization signal in β‐dystroglycan?
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- Author
- Bárbara Lara‐Chacón; Mario Bermúdez de León; Daniel Leocadio; Pablo Gómez; Lizeth Fuentes‐Mera; Ivette Martínez‐Vieyra; Arturo Ortega; David A. Jans; Bulmaro Cisneros
- Publisher
- John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0730-2312)
- Published
- 2010
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)