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.
Ankyrin-G induces nucleoporin RanBP2/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. - In: JOURNAL OF CELL SCIENCE. - ISSN 0021-9533. - 132:18(2019), pp. 1-17. [10.1242/jcs.222802]
Ankyrin-G induces nucleoporin RanBP2/Nup358 to associate with the axon initial segment of neurons
Khalaf, BouchraPrimo
;Roncador, Alessandro;Pischedda, Francesca;Casini, Antonio;Piccoli, Giovanni;Macchi, Paolo
Ultimo
2019-01-01
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione