{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T18:00:19Z","timestamp":1779386419325,"version":"3.53.1"},"reference-count":65,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2018,11,26]],"date-time":"2018-11-26T00:00:00Z","timestamp":1543190400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100002661","name":"Fonds De La Recherche Scientifique - FNRS","doi-asserted-by":"publisher","award":["J.0102.18"],"award-info":[{"award-number":["J.0102.18"]}],"id":[{"id":"10.13039\/501100002661","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002661","name":"Fonds De La Recherche Scientifique - FNRS","doi-asserted-by":"publisher","award":["T.0082.14F"],"award-info":[{"award-number":["T.0082.14F"]}],"id":[{"id":"10.13039\/501100002661","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002910","name":"F\u00e9d\u00e9ration Wallonie-Bruxelles","doi-asserted-by":"publisher","award":["ARC 4.110.F.000092F"],"award-info":[{"award-number":["ARC 4.110.F.000092F"]}],"id":[{"id":"10.13039\/501100002910","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003977","name":"Israel Science Foundation","doi-asserted-by":"publisher","award":["958\/15"],"award-info":[{"award-number":["958\/15"]}],"id":[{"id":"10.13039\/501100003977","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>Neurodegenerative diseases, such as amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), and Huntington\u2019s disease (HD), are characterized by intracellular aggregation of proteins. In the case of ALS and FTD, these protein aggregates are found in the cytoplasm of affected neurons and contain certain RNA-binding proteins (RBPs), namely the TAR DNA-binding protein of 43 kDa (TDP-43) and the fused in sarcoma (FUS) gene product. TDP-43 and FUS are nuclear proteins and their displacement to the cytoplasm is thought to be adverse in at least two ways: loss-of-function in the nucleus and gain-of-toxicity in the cytoplasm. In the case of HD, expansion of a polyglutamine (polyQ) stretch within the N-terminal domain of the Huntingtin (HTT) protein leads to nuclear accumulation of polyQ HTT (or mHTT) and a toxic gain-of-function phenotype resulting in neurodegeneration. Numerous studies in recent years have provided evidence that defects in nucleocytoplasmic transport critically contribute to the pathology of these neurodegenerative diseases. A new mechanistic view is emerging, implicating three types of perturbations in normal cellular pathways that rely on nucleocytoplasmic transport: displacement of nuclear transport receptors and nucleoporins from nuclear pore complexes (NPCs), mislocalization and aggregation of RNA-binding proteins, and weakening of the chaperone activity of nuclear import receptors.<\/jats:p>","DOI":"10.3390\/cells7120232","type":"journal-article","created":{"date-parts":[[2018,11,27]],"date-time":"2018-11-27T03:31:33Z","timestamp":1543289493000},"page":"232","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":36,"title":["Perturbations in Traffic: Aberrant Nucleocytoplasmic Transport at the Heart of Neurodegeneration"],"prefix":"10.3390","volume":"7","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4080-9413","authenticated-orcid":false,"given":"Birthe","family":"Fahrenkrog","sequence":"first","affiliation":[{"name":"Institute of Molecular Biology and Medicine, Universit\u00e9 Libre de Bruxelles, 6041 Charleroi, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4230-7468","authenticated-orcid":false,"given":"Amnon","family":"Harel","sequence":"additional","affiliation":[{"name":"Azrieli Faculty of Medicine, Bar-Ilan University, Safed 1311502, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2018,11,26]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1080\/19491034.2016.1172152","article-title":"Nucleocytoplasmic transport in C9orf72-mediated ALS\/FTD","volume":"7","author":"Zhang","year":"2016","journal-title":"Nucleus"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1489","DOI":"10.1002\/1873-3468.12646","article-title":"TDP-43 and FUS en route from the nucleus to the cytoplasm","volume":"591","author":"Ederle","year":"2017","journal-title":"FEBS Lett."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.neuron.2017.03.032","article-title":"Huntington\u2019s disease: Nuclear gatekeepers under attack","volume":"94","author":"Veldman","year":"2017","journal-title":"Neuron"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1016\/j.semcdb.2017.05.004","article-title":"The functional versatility of the nuclear pore complex proteins","volume":"68","author":"Hezwani","year":"2017","journal-title":"Semin. 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