Ankyrin-G induces nucleoporin RanBP2/Nup358 to associate with the axon initial segment of neurons

Author:

Khalaf Bouchra1ORCID,Roncador Alessandro1,Pischedda Francesca2,Casini Antonio3,Thomas Sabine4,Piccoli Giovanni2,Kiebler Michael4,Macchi Paolo1ORCID

Affiliation:

1. Laboratory of Molecular and Cellular Neurobiology, Department of Cellular, Computational and Integrative Biology-CIBIO, University of Trento, Italy

2. Dulbecco Telethon Laboratory of Biology of Synapses, Department of Cellular, Computational and Integrative Biology-CIBIO, University of Trento, Italy

3. Laboratory of Molecular Virology, Department of Cellular, Computational and Integrative Biology-CIBIO, University of Trento, Italy

4. Department for Cell Biology, Biomedical Center, Medical Faculty, Ludwig-Maximilian University of Munich, Großhaderner Straße 9, 82152 Planegg-Martinsried, Germany

Abstract

RanBP2/Nup358 is a member of the large nucleoporin family constituting the nuclear pore complex (NPC). 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 and mediated by the AIS scaffold ankyrin-G. The N-terminus of Nup358 is found 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.

Funder

University of Trento

Publisher

The Company of Biologists

Subject

Cell Biology

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