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Wild type TDP-43 inclusions are a pathological hallmark of &amp;gt;95% of patients with sporadic ALS and of the majority of familial ALS cases, and they are also found in a significant proportion of FTLD cases. ALS is the most common form of motor neuron disease, characterized by progressive weakness and muscular wasting, and typically leads to death within a few years of diagnosis. To determine how the translocation and misfolding of TDP-43 contribute to ALS pathogenicity, it is crucial to define the dynamic behavior of this protein within the cellular environment. It is therefore necessary to develop cell models that allow the location of the protein to be defined. We report the use of TDP-43 with a tetracysteine tag for visualization using fluorogenic biarsenical compounds and show that this model displays features of ALS observed in other cell models. We also demonstrate that this labeling procedure enables live-cell imaging of the translocation of the protein from the nucleus into the cytosol.<\/jats:p>","DOI":"10.1021\/acs.biochem.9b00592","type":"journal-article","created":{"date-parts":[[2019,9,6]],"date-time":"2019-09-06T07:53:28Z","timestamp":1567756408000},"page":"4086-4095","source":"Crossref","is-referenced-by-count":14,"title":["Using Tetracysteine-Tagged TDP-43 with a Biarsenical\nDye To Monitor Real-Time Trafficking in a Cell Model of Amyotrophic\nLateral Sclerosis"],"prefix":"10.1021","volume":"58","author":[{"given":"Janice S. W.","family":"Ng","sequence":"first","affiliation":[{"name":"University of Cambridge , , Lensfield Road , ,","place":["Cambridge, U.K., CB2 1EW"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maya A.","family":"Hanspal","sequence":"additional","affiliation":[{"name":"University of Cambridge , , Lensfield Road , ,","place":["Cambridge, U.K., CB2 1EW"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Naunehal S.","family":"Matharu","sequence":"additional","affiliation":[{"name":"University of Cambridge , , Lensfield Road , ,","place":["Cambridge, U.K., CB2 1EW"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Teresa P.","family":"Barros","sequence":"additional","affiliation":[{"name":"University of Cambridge , , Lensfield Road , ,","place":["Cambridge, U.K., CB2 1EW"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1253-6342","authenticated-orcid":true,"given":"Elin K.","family":"Esbjo\u0308rner","sequence":"additional","affiliation":[{"name":"Chalmers University of Technology , , Kemiva\u0308gen 10 , ,","place":["Gothenburg, Sweden, 412 96"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark R.","family":"Wilson","sequence":"additional","affiliation":[{"name":"Illawarra Health and Medical Research Institute , , ,","place":["Wollongong, NSW, Australia, 2522"]},{"name":"University of Wollongong , , Northfields Avenue , , ,","place":["Wollongong, NSW, Australia, 2522"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2528-7039","authenticated-orcid":true,"given":"Justin J.","family":"Yerbury","sequence":"additional","affiliation":[{"name":"Illawarra Health and Medical Research Institute , , ,","place":["Wollongong, NSW, Australia, 2522"]},{"name":"University of Wollongong , , Northfields Avenue , , ,","place":["Wollongong, NSW, Australia, 2522"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher M.","family":"Dobson","sequence":"additional","affiliation":[{"name":"University of Cambridge , , Lensfield Road , ,","place":["Cambridge, U.K., CB2 1EW"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3887-4964","authenticated-orcid":true,"given":"Janet R.","family":"Kumita","sequence":"additional","affiliation":[{"name":"University of Cambridge , , Lensfield Road , ,","place":["Cambridge, U.K., CB2 1EW"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2019,9,6]]},"reference":[{"key":"2026090301515567300_cit1","doi-asserted-by":"publisher","first-page":"602","DOI":"10.1016\/j.bbrc.2006.10.093","article-title":"TDP-43 is a component of ubiquitin-positive\ntau-negative inclusions in frontotemporal lobar degeneration and amyotrophic\nlateral sclerosis","volume":"351","author":"Arai","year":"2006","journal-title":"Biochem. 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Acad. Sci. U. S. A."},{"key":"2026090301515567300_cit5","doi-asserted-by":"publisher","first-page":"36337","DOI":"10.1074\/jbc.M104236200","article-title":"Characterization\nand functional implications of the\nRNA binding properties of nuclear factor TDP-43, a novel splicing\nregulator of CFTR exon 9","volume":"276","author":"Buratti","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2026090301515567300_cit6","doi-asserted-by":"publisher","first-page":"13416","DOI":"10.1038\/srep13416","article-title":"Distinct partitioning of ALS associated\nTDP-43, FUS and SOD1 mutants into cellular inclusions","volume":"5","author":"Farrawell","year":"2015","journal-title":"Sci. Rep."},{"key":"2026090301515567300_cit7","doi-asserted-by":"publisher","first-page":"236","DOI":"10.1016\/j.nbd.2016.08.007","article-title":"In vitro prion-like\nbehaviour of\nTDP-43 in ALS","volume":"96","author":"Smethurst","year":"2016","journal-title":"Neurobiol. 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Biol. Chem."},{"key":"2026090301515567300_cit22","doi-asserted-by":"publisher","first-page":"e13250","DOI":"10.1371\/journal.pone.0013250","article-title":"Tar DNA binding protein-43 (TDP-43) associates with\nstress granules: analysis of cultured cells and pathological brain\ntissue","volume":"5","author":"Liu-Yesucevitz","year":"2010","journal-title":"PLoS One"},{"key":"2026090301515567300_cit23","doi-asserted-by":"publisher","first-page":"3703","DOI":"10.1093\/hmg\/dds205","article-title":"The ALS disease protein\nTDP-43 is\nactively transported in motor neuron axons and regulates axon outgrowth","volume":"21","author":"Fallini","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"2026090301515567300_cit24","doi-asserted-by":"publisher","first-page":"3353","DOI":"10.1093\/hmg\/ddp275","article-title":"Truncation\nand pathogenic mutations facilitate the formation of intracellular\naggregates of TDP-43","volume":"18","author":"Nonaka","year":"2009","journal-title":"Hum. Mol. Genet."},{"key":"2026090301515567300_cit25","doi-asserted-by":"publisher","first-page":"1263","DOI":"10.1242\/jcs.140087","article-title":"Differential roles of the ubiquitin\nproteasome system and autophagy in the clearance of soluble and aggregated\nTDP-43 species","volume":"127","author":"Scotter","year":"2014","journal-title":"J. Cell Sci."},{"key":"2026090301515567300_cit26","doi-asserted-by":"publisher","first-page":"182","DOI":"10.2353\/ajpath.2008.080003","article-title":"Enrichment of C-terminal fragments\nin TAR DNA-binding\nprotein-43 cytoplasmic inclusions in brain but not in spinal cord\nof frontotemporal lobar degeneration and amyotrophic lateral sclerosis","volume":"173","author":"Igaz","year":"2008","journal-title":"Am. J. Pathol."},{"key":"2026090301515567300_cit27","doi-asserted-by":"publisher","first-page":"822","DOI":"10.1038\/nsmb.2053","article-title":"An ALS-associated mutation affecting\nTDP-43 enhances protein aggregation, fibril formation and neurotoxicity","volume":"18","author":"Guo","year":"2011","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2026090301515567300_cit28","doi-asserted-by":"publisher","first-page":"544","DOI":"10.1038\/s41598-017-00657-z","article-title":"Single cell\nimaging and quantification of TDP-43 and alpha-synuclein intercellular\npropagation","volume":"7","author":"Peled","year":"2017","journal-title":"Sci. Rep."},{"key":"2026090301515567300_cit29","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1007\/978-1-62703-640-5_2","article-title":"Considerations for the Use of SH-SY5Y\nNeuroblastoma\nCells in Neurobiology","volume":"1078","author":"Kovalevich","year":"2013","journal-title":"Methods Mol. Biol."},{"key":"2026090301515567300_cit30","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1038\/s41467-018-07699-5","article-title":"Trodusquemine enhances A beta(42) aggregation but suppresses\nits toxicity by displacing oligomers from cell membranes","volume":"10","author":"Limbocker","year":"2019","journal-title":"Nat. Commun."},{"key":"2026090301515567300_cit31","doi-asserted-by":"publisher","first-page":"4167","DOI":"10.1523\/JNEUROSCI.2350-13.2014","article-title":"ALS-linked mutations\nenlarge TDP-43-enriched neuronal\nRNA granules in the dendritic arbor","volume":"34","author":"Liu-Yesucevitz","year":"2014","journal-title":"J. Neurosci."},{"key":"2026090301515567300_cit32","doi-asserted-by":"publisher","first-page":"1098","DOI":"10.1128\/MCB.01279-10","article-title":"TDP-43 is directed\nto stress granules by sorbitol, a novel physiological\nosmotic and oxidative stressor","volume":"31","author":"Dewey","year":"2011","journal-title":"Mol. Cell. 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Genet."},{"key":"2026090301515567300_cit36","doi-asserted-by":"publisher","first-page":"7607","DOI":"10.1073\/pnas.0900688106","article-title":"Aberrant cleavage\nof TDP-43 enhances aggregation and cellular toxicity","volume":"106","author":"Zhang","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2026090301515567300_cit37","doi-asserted-by":"publisher","first-page":"56","DOI":"10.1186\/1750-1326-7-56","article-title":"Regulated\nprotein aggregation: stress granules and neurodegeneration","volume":"7","author":"Wolozin","year":"2012","journal-title":"Mol. 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Neurochem."},{"key":"2026090301515567300_cit41","doi-asserted-by":"publisher","first-page":"837","DOI":"10.1097\/NEN.0000000000000102","article-title":"Poly-A binding protein-1\nlocalization\nto a subset of TDP-43 inclusions in amyotrophic lateral sclerosis\noccurs more frequently in patients harboring an expansion in C9orf72","volume":"73","author":"McGurk","year":"2014","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"2026090301515567300_cit42","doi-asserted-by":"publisher","first-page":"361","DOI":"10.1083\/jcb.201302044","article-title":"Stress granules\nas crucibles of ALS pathogenesis","volume":"201","author":"Li","year":"2013","journal-title":"J. Cell Biol."},{"key":"2026090301515567300_cit43","doi-asserted-by":"publisher","first-page":"2899","DOI":"10.1016\/j.febslet.2008.07.027","article-title":"Abnormal phosphorylation\nof Ser409\/410\nof TDP-43 in FTLD-U and ALS","volume":"582","author":"Inukai","year":"2008","journal-title":"FEBS Lett."},{"key":"2026090301515567300_cit44","doi-asserted-by":"publisher","first-page":"743","DOI":"10.1007\/s00418-005-0136-3","article-title":"Accumulation of FlAsH\/Lumio Green\nin active mitochondria can be reversed by beta-mercaptoethanol for\nspecific staining of tetracysteine-tagged proteins","volume":"125","author":"Langhorst","year":"2006","journal-title":"Histochem. Cell Biol."},{"key":"2026090301515567300_cit45","doi-asserted-by":"publisher","first-page":"171","DOI":"10.1016\/j.ijcard.2010.07.011","article-title":"The prevalence\nand risk factors for cholelithiasis and asymptomatic gallstones in\nadults with congenital heart disease","volume":"152","author":"Shiina","year":"2011","journal-title":"Int. J.\nCardiol."},{"key":"2026090301515567300_cit46","doi-asserted-by":"publisher","first-page":"705","DOI":"10.1074\/mcp.M800390-MCP200","article-title":"Multiplex\nSILAC analysis of a cellular TDP-43 proteinopathy model reveals protein\ninclusions associated with SUMOylation and diverse polyubiquitin chains","volume":"9","author":"Seyfried","year":"2010","journal-title":"Mol. Cell. Proteomics"},{"key":"2026090301515567300_cit47","doi-asserted-by":"publisher","first-page":"139","DOI":"10.1016\/j.brainres.2012.02.031","article-title":"Role of selected\nmutations in the Q\/N rich region of\nTDP-43 in EGFP-12xQ\/N-induced aggregate formation","volume":"1462","author":"Budini","year":"2012","journal-title":"Brain Res."},{"key":"2026090301515567300_cit48","doi-asserted-by":"publisher","first-page":"49","DOI":"10.1186\/2051-5960-1-49","article-title":"Reducing TDP-43\naggregation does not prevent its cytotoxicity","volume":"1","author":"Liu","year":"2013","journal-title":"Acta Neuropathol. 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Neurol."},{"key":"2026090301515567300_cit51","doi-asserted-by":"publisher","first-page":"137","DOI":"10.1007\/s00401-008-0477-9","article-title":"Phosphorylation of S409\/410 of TDP-43\nis a consistent feature in all sporadic and familial forms of TDP-43\nproteinopathies","volume":"117","author":"Neumann","year":"2009","journal-title":"Acta Neuropathol."},{"key":"2026090301515567300_cit52","doi-asserted-by":"publisher","first-page":"38","DOI":"10.1038\/nrn3121","article-title":"Gains or\nlosses: molecular mechanisms\nof TDP43-mediated neurodegeneration","volume":"13","author":"Lee","year":"2012","journal-title":"Nat. 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