Nature Communications (Jun 2022)
NUP62 localizes to ALS/FTLD pathological assemblies and contributes to TDP-43 insolubility
- 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
Affiliations
- Amanda M. Gleixner
- Department of Neurobiology, University of Pittsburgh School of Medicine
- Brandie Morris Verdone
- Department of Neuroscience, Jefferson Weinberg ALS Center, Vickie and Jack Farber Institute for Neuroscience, Thomas Jefferson University
- Charlton G. Otte
- Department of Neurobiology, University of Pittsburgh School of Medicine
- Eric N. Anderson
- Department of Pediatrics, Children’s Hospital of Pittsburgh, University of Pittsburgh Medical Center
- Nandini Ramesh
- Department of Pediatrics, Children’s Hospital of Pittsburgh, University of Pittsburgh Medical Center
- Olivia R. Shapiro
- Department of Neurobiology, University of Pittsburgh School of Medicine
- Jenna R. Gale
- Department of Neurobiology, University of Pittsburgh School of Medicine
- Jocelyn C. Mauna
- Department of Neurobiology, University of Pittsburgh School of Medicine
- Jacob R. Mann
- Department of Neurobiology, University of Pittsburgh School of Medicine
- Katie E. Copley
- Department of Neurobiology, University of Pittsburgh School of Medicine
- Elizabeth L. Daley
- The Ken & Ruth Davee Department of Neurology, Northwestern University of Feinberg School of Medicine
- Juan A. Ortega
- The Ken & Ruth Davee Department of Neurology, Northwestern University of Feinberg School of Medicine
- Maria Elena Cicardi
- Department of Neuroscience, Jefferson Weinberg ALS Center, Vickie and Jack Farber Institute for Neuroscience, Thomas Jefferson University
- Evangelos Kiskinis
- The Ken & Ruth Davee Department of Neurology, Northwestern University of Feinberg School of Medicine
- Julia Kofler
- LiveLikeLou Center for ALS Research, University of Pittsburgh Brain Institute
- Udai B. Pandey
- LiveLikeLou Center for ALS Research, University of Pittsburgh Brain Institute
- Davide Trotti
- Department of Neuroscience, Jefferson Weinberg ALS Center, Vickie and Jack Farber Institute for Neuroscience, Thomas Jefferson University
- Christopher J. Donnelly
- Department of Neurobiology, University of Pittsburgh School of Medicine
- DOI
- https://doi.org/10.1038/s41467-022-31098-6
- Journal volume & issue
-
Vol. 13,
no. 1
pp. 1 – 17
Abstract
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.
