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Ankyrin-G induces nucleoporin Nup358 to associate with the axon initial segment of neurons.
Khalaf, Bouchra; Roncador, Alessandro; Pischedda, Francesca; Casini, Antonio; Thomas, Sabine; Piccoli, Giovanni; Kiebler, Michael; Macchi, Paolo.
Afiliação
  • Khalaf B; Laboratory of Molecular and Cellular Neurobiology, Department of Cellular, Computational and Integrative Biology-CIBIO, University of Trento, 38123 Trento, Italy.
  • Roncador A; Laboratory of Molecular and Cellular Neurobiology, Department of Cellular, Computational and Integrative Biology-CIBIO, University of Trento, 38123 Trento, Italy.
  • Pischedda F; Dulbecco Telethon Laboratory of Biology of Synapses, Department of Cellular, Computational and Integrative Biology-CIBIO, University of Trento, 38123 Trento, Italy.
  • Casini A; Laboratory of Molecular Virology, Department of Cellular, Computational and Integrative Biology-CIBIO, University of Trento, 38123 Trento, Italy.
  • Thomas S; Department for Cell Biology, Biomedical Center, Medical Faculty, Ludwig-Maximilian University of Munich, Großhaderner Straße 9, 82152 Planegg-Martinsried, Germany.
  • Piccoli G; Dulbecco Telethon Laboratory of Biology of Synapses, Department of Cellular, Computational and Integrative Biology-CIBIO, University of Trento, 38123 Trento, Italy.
  • Kiebler M; Department for Cell Biology, Biomedical Center, Medical Faculty, Ludwig-Maximilian University of Munich, Großhaderner Straße 9, 82152 Planegg-Martinsried, Germany.
  • Macchi P; Laboratory of Molecular and Cellular Neurobiology, Department of Cellular, Computational and Integrative Biology-CIBIO, University of Trento, 38123 Trento, Italy paolo.macchi@unitn.it.
J Cell Sci ; 132(18)2019 09 26.
Article em En | MEDLINE | ID: mdl-31427429
ABSTRACT
Nup358 (also known as RanBP2) is a member of the large nucleoporin family that constitutes the nuclear pore complex. Depending on the cell type and the physiological state, Nup358 interacts with specific partner proteins and influences distinct mechanisms independent of its role in nucleocytoplasmic transport. Here, we provide evidence that Nup358 associates selectively with the axon initial segment (AIS) of mature neurons, mediated by the AIS scaffold protein ankyrin-G (AnkG, also known as Ank3). The N-terminus of Nup358 is demonstrated to be sufficient for its localization at the AIS. Further, we show that Nup358 is expressed as two isoforms, one full-length and another shorter form of Nup358. These isoforms differ in their subcellular distribution in neurons and expression level during neuronal development. Overall, the present study highlights an unprecedented localization of Nup358 within the AIS and suggests its involvement in neuronal function.This article has an associated First Person interview with the first author of the paper.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Axônios / Anquirinas / Chaperonas Moleculares / Complexo de Proteínas Formadoras de Poros Nucleares / Embrião de Mamíferos / Neurônios Tipo de estudo: Risk_factors_studies Limite: Animals / Humans Idioma: En Ano de publicação: 2019 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Axônios / Anquirinas / Chaperonas Moleculares / Complexo de Proteínas Formadoras de Poros Nucleares / Embrião de Mamíferos / Neurônios Tipo de estudo: Risk_factors_studies Limite: Animals / Humans Idioma: En Ano de publicação: 2019 Tipo de documento: Article