NUP62 localizes to ALS/FTLD pathological assemblies and contributes to TDP-43 insolubility

ALS and FTLD are both characterized by insoluble cytoplasmic depositions of TDP43. Here the authors show that the nucleopore protein NUP62 is mislocalized in C9orf72 and sporadic ALS/FTLD and propose that it interacts with TDP-43 to promote its insolubility.

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Bibliografiska uppgifter
Huvudupphov:	Amanda M. Gleixner, Brandie Morris Verdone, Charlton G. Otte, Eric N. Anderson, Nandini Ramesh, Olivia R. Shapiro, Jenna R. Gale, Jocelyn C. Mauna, Jacob R. Mann, Katie E. Copley, Elizabeth L. Daley, Juan A. Ortega, Maria Elena Cicardi, Evangelos Kiskinis, Julia Kofler, Udai B. Pandey, Davide Trotti, Christopher J. Donnelly
Materialtyp:	Artigo
Språk:	Inglês
Utgiven:	Nature Portfolio 2022-06-01
Serie:	Nature Communications
Länkar:	https://doi.org/10.1038/s41467-022-31098-6
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NUP62 localizes to ALS/FTLD pathological assemblies and contributes to TDP-43 insolubility

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