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Updated: May 23, 2026

Assay to Measure Nucleocytoplasmic Transport in Real Time within Motor Neuron-like NSC-34 Cells
Published on: May 16, 2017
Nuclear carrier and RNA-binding proteins in frontotemporal lobar degeneration associated with fused in sarcoma (FUS)
Y S Davidson1, A C Robinson1, Q Hu1
1Mental Health and Neurodegeneration Research Group, Faculty of Human and Medical Sciences, University of Manchester, ManchesterCerebral Function Unit, Greater Manchester Neuroscience Centre, Salford Royal Foundation Trust, SalfordDepartment of Neuropathology, Walton Centre for Neurology and Neurosurgery, LiverpoolNeuropathology/Cellular Pathology, Royal Victoria InfirmaryInstitute for Ageing and Health, Campus for Ageing and Vitality, Newcastle University, Newcastle upon Tyne, UKNorthwestern CNADC Neuropathology Core, Northwestern University Feinberg School of Medicine, Chicago, Illinois, Departments ofNeurologyPathology & Immunology, Washington University School of Medicine, St Louis, Missouri, USA.
Aims:
We aimed to investigate the role of the nuclear carrier and binding proteins, transportin 1 (TRN1) and transportin 2 (TRN2), TATA-binding protein-associated factor 15 (TAF15) and Ewing's sarcoma protein (EWS) in inclusion body formation in cases of frontotemporal lobar degeneration (FTLD) associated with fused in sarcoma protein (FTLD-FUS).
Methods:
Eight cases of FTLD-FUS (five cases of atypical FTLD-U, two of neuronal intermediate filament inclusion body disease and one of basophilic inclusion body disease) were immunostained for FUS, TRN1, TRN2, TAF15 and EWS. Ten cases of FTLD associated with TDP-43 inclusions served as reference cases.
Results:
The inclusion bodies in FTLD-FUS contained TRN1 and TAF15 and, to a lesser extent, EWS, but not TRN2. The patterns of immunostaining for TRN1 and TAF15 were very similar to that of FUS. None of these proteins was associated with tau or TDP-43 aggregations in FTLD.
Conclusions:
Data suggest that FUS, TRN1 and TAF15 may participate in a functional pathway in an interdependent way, and imply that the function of TDP-43 may not necessarily be in parallel with, or complementary to, that of FUS, despite each protein sharing many similar structural elements.
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