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

被引:6
|
作者
Khalaf, Bouchra [1 ]
Roncador, Alessandro [1 ]
Pischedda, Francesca [2 ]
Casini, Antonio [3 ]
Thomas, Sabine [4 ]
Piccoli, Giovanni [2 ]
Kiebler, Michael [4 ]
Macchi, Paolo [1 ]
机构
[1] Univ Trento, Lab Mol & Cellular Neurobiol, Dept Cellular Computat & Integrat Biol CIBIO, I-38123 Trento, Italy
[2] Univ Trento, Dulbecco Telethon Lab Biol Synapses, Dept Cellular Computat & Integrat Biol CIBIO, I-38123 Trento, Italy
[3] Univ Trento, Lab Mol Virol, Dept Cellular Computat & Integrat Biol CIBIO, I-38123 Trento, Italy
[4] Ludwig Maximilian Univ Munich, Med Fac, Biomed Ctr, Dept Cell Biol, Grosshaderner Str 9, D-82152 Planegg Martinsried, Germany
关键词
Nucleoporin; RanBP2; Nup358; Ankyrin-G; Axon initial segment; NUCLEAR-PORE COMPLEX; PROTEIN; RANBP2; DOMAIN; MAINTENANCE; DISRUPTION; NUP98; IDENTIFICATION; DEGRADATION; TRANSPORT;
D O I
10.1242/jcs.222802
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
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.
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页数:17
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