{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T19:35:02Z","timestamp":1791142502938,"version":"4.1.0"},"reference-count":68,"publisher":"The Company of Biologists","issue":"20","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2008,10,15]]},"abstract":"<jats:p>A specific mutation (\u0394E) in torsinA underlies most cases of the dominantly inherited movement disorder, early-onset torsion dystonia (DYT1). TorsinA, a member of the AAA+ ATPase superfamily, is located within the lumen of the nuclear envelope (NE) and endoplasmic reticulum (ER). We investigated an association between torsinA and nesprin-3, which spans the outer nuclear membrane (ONM) of the NE and links it to vimentin via plectin in fibroblasts. Mouse nesprin-3\u03b1 co-immunoprecipitated with torsinA and this involved the C-terminal region of torsinA and the KASH domain of nesprin-3\u03b1. This association with human nesprin-3 appeared to be stronger for torsinA\u0394E than for torsinA. TorsinA also associated with the KASH domains of nesprin-1 and -2 (SYNE1 and 2), which link to actin. In the absence of torsinA, in knockout mouse embryonic fibroblasts (MEFs), nesprin-3\u03b1 was localized predominantly in the ER. Enrichment of yellow fluorescent protein (YFP)-nesprin-3 in the ER was also seen in the fibroblasts of DYT1 patients, with formation of YFP-positive globular structures enriched in torsinA, vimentin and actin. TorsinA-null MEFs had normal NE structure, but nuclear polarization and cell migration were delayed in a wound-healing assay, as compared with wild-type MEFs. These studies support a role for torsinA in dynamic interactions between the KASH domains of nesprins and their protein partners in the lumen of the NE, with torsinA influencing the localization of nesprins and associated cytoskeletal elements and affecting their role in nuclear and cell movement.<\/jats:p>","DOI":"10.1242\/jcs.029454","type":"journal-article","created":{"date-parts":[[2008,10,1]],"date-time":"2008-10-01T02:53:47Z","timestamp":1222829627000},"page":"3476-3486","source":"Crossref","is-referenced-by-count":154,"title":["TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton"],"prefix":"10.1242","volume":"121","author":[{"given":"Fla\u0301via C.","family":"Nery","sequence":"first","affiliation":[{"name":"Molecular Neurogenetics Unit, Department of Neurology and Center for Molecular Imaging Research, Department of Radiology, Massachusetts General Hospital and Program in Neuroscience, Harvard Medical School, Boston, MA 02114, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Juan","family":"Zeng","sequence":"additional","affiliation":[{"name":"Molecular Neurogenetics Unit, Department of Neurology and Center for Molecular Imaging Research, Department of Radiology, Massachusetts General Hospital and Program in Neuroscience, Harvard Medical School, Boston, MA 02114, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brian P.","family":"Niland","sequence":"additional","affiliation":[{"name":"Molecular Neurogenetics Unit, Department of Neurology and Center for Molecular Imaging Research, Department of Radiology, Massachusetts General Hospital and Program in Neuroscience, Harvard Medical School, Boston, MA 02114, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeffrey","family":"Hewett","sequence":"additional","affiliation":[{"name":"Molecular Neurogenetics Unit, Department of Neurology and Center for Molecular Imaging Research, Department of Radiology, Massachusetts General Hospital and Program in Neuroscience, Harvard Medical School, Boston, MA 02114, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jonathan","family":"Farley","sequence":"additional","affiliation":[{"name":"Molecular Neurogenetics Unit, Department of Neurology and Center for Molecular Imaging Research, Department of Radiology, Massachusetts General Hospital and Program in Neuroscience, Harvard Medical School, Boston, MA 02114, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel","family":"Irimia","sequence":"additional","affiliation":[{"name":"BioMEMS Resource Center, Department of Surgery and Bioengineering, Massachusetts General Hospital, Boston, MA 02114, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuqing","family":"Li","sequence":"additional","affiliation":[{"name":"Department of Neurology and Center for Neurodegeneration and Experimental Therapeutics, University of Alabama, Birmingham, AL 35294, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gerhard","family":"Wiche","sequence":"additional","affiliation":[{"name":"Department of Molecular Cell Biology, Max F. Perutz Laboratories, University of Vienna, A-1030 Vienna, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arnoud","family":"Sonnenberg","sequence":"additional","affiliation":[{"name":"Department of Cell Biology, Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xandra O.","family":"Breakefield","sequence":"additional","affiliation":[{"name":"Molecular Neurogenetics Unit, Department of Neurology and Center for Molecular Imaging Research, Department of Radiology, Massachusetts General Hospital and Program in Neuroscience, Harvard Medical School, Boston, MA 02114, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","reference":[{"key":"2021042523534123200_REF1","doi-asserted-by":"crossref","unstructured":"Andra\u0308, K., Nikolic, B., Stocher, M., Drenckhahn, D. and Wiche, G. (1998). Not just scaffolding: plectin regulates actin dynamics in cultured cells. Genes Dev.12, 3442-3451.","DOI":"10.1101\/gad.12.21.3442"},{"key":"2021042523534123200_REF2","doi-asserted-by":"crossref","unstructured":"Andra\u0308, K., Kornacker, I., Jo\u0308rgl, A., Zo\u0308rer, M., Spazierer, D., Fuchs, P., Fischer, I. and Wiche, G. (2003). Plectin-isoform-specific rescue of hemidesmosomal defects in plectin (-\/-) keratinocytes. J. Invest. Dermatol.120, 189-197.","DOI":"10.1046\/j.1523-1747.2003.12027.x"},{"key":"2021042523534123200_REF3","doi-asserted-by":"crossref","unstructured":"Asanuma, K., Carbon-Correll, M. and Eidelberg, D. (2005). Neuroimaging in human dystonia. J. Med. Invest.52, 272-279.","DOI":"10.2152\/jmi.52.272"},{"key":"2021042523534123200_REF4","unstructured":"Basham, S. E. and Rose, L. S. (2001). The Caenorhabditis elegans polarity gene ooc-5 encodes a Torsin-related protein of the AAA ATPase superfamily. Development128, 4645-4656."},{"key":"2021042523534123200_REF5","doi-asserted-by":"crossref","unstructured":"Berardelli, A., Rothwell, J. C., Hallett, M., Thompson, P. D., Manfredi, M. and Marsden, C. D. (1998). The pathophysiology of primary dystonia. Brain121, 1195-1212.","DOI":"10.1093\/brain\/121.7.1195"},{"key":"2021042523534123200_REF6","doi-asserted-by":"crossref","unstructured":"Bragg, D. C., Camp, S. M., Kaufman, C. A., Wilbur, J. D., Boston, H., Schuback, D. E., Hanson, P. I., Sena-Esteves, M. and Breakefield, X. O. (2004). Perinuclear biogenesis of mutant torsin-A inclusions in cultured cells infected with tetracycline-regulated herpes simplex virus type 1 amplicon vectors. Neuroscience125, 651-661.","DOI":"10.1016\/j.neuroscience.2004.01.053"},{"key":"2021042523534123200_REF7","doi-asserted-by":"crossref","unstructured":"Breakefield, X. O., Blood, A. J., Li, Y., Hallett, M., Hanson, P. I. and Standaert, D. G. (2008). The pathophysiologic basis of the dystonias. Nat. Rev. Neurosci.9, 222-234.","DOI":"10.1038\/nrn2337"},{"key":"2021042523534123200_REF8","doi-asserted-by":"crossref","unstructured":"Callan, A. C., Bunning, S., Jones, O. T., High, S. and Swanton, E. (2007). Biosynthesis of the dystonia-associated AAA+ ATPase torsinA at the endoplasmic reticulum. Biochem. J.401, 607-612.","DOI":"10.1042\/BJ20061313"},{"key":"2021042523534123200_REF9","doi-asserted-by":"crossref","unstructured":"Carbon, M., Kingsley, P. B., Tang, C., Bressman, S. and Eidelberg, D. (2008). Microstructural white matter changes in primary torsion dystonia. Mov. Disord.23, 234-239.","DOI":"10.1002\/mds.21806"},{"key":"2021042523534123200_REF10","doi-asserted-by":"crossref","unstructured":"Chang, L. and Goldman, R. D. (2004). Intermediate filaments mediate cytoskeletal crosstalk. Nat. Rev. Mol. Cell Biol.5, 601-613.","DOI":"10.1038\/nrm1438"},{"key":"2021042523534123200_REF11","doi-asserted-by":"crossref","unstructured":"Clarimon, J., Asgeirsson, H., Singleton, A., Jakobsson, F., Hjaltason, H., Hardy, J. and Sveinbjornsdottir, S. (2005). Torsin A haplotype predisposes to idiopathic dystonia. Ann. Neurol.57, 765-767.","DOI":"10.1002\/ana.20485"},{"key":"2021042523534123200_REF12","doi-asserted-by":"crossref","unstructured":"Colucci-Guyon, E., Gimenez, Y. R. M., Maurice, T., Babinet, C. and Privat, A. (1999). Cerebellar defect and impaired motor coordination in mice lacking vimentin. Glia25, 33-43.","DOI":"10.1002\/(SICI)1098-1136(19990101)25:1<33::AID-GLIA4>3.0.CO;2-J"},{"key":"2021042523534123200_REF13","doi-asserted-by":"crossref","unstructured":"Crisp, M., Liu, Q., Roux, K., Rattner, J. B., Shanahan, C., Burke, B., Stahl, P. D. and Hodzic, D. (2006). Coupling of the nucleus and cytoplasm: role of the LINC complex. J. Cell Biol.172, 41-53.","DOI":"10.1083\/jcb.200509124"},{"key":"2021042523534123200_REF14","doi-asserted-by":"crossref","unstructured":"Dang, M. T., Yokoi, F., McNaught, K. S., Jengelley, T. A., Jackson, T., Li, J. and Li, Y. (2005). Generation and characterization of Dyt1 DeltaGAG knock-in mouse as a model for early-onset dystonia. Exp. Neurol.196, 452-463.","DOI":"10.1016\/j.expneurol.2005.08.025"},{"key":"2021042523534123200_REF15","doi-asserted-by":"crossref","unstructured":"Dang, M. T., Yokoi, F., Pence, M. A. and Li, Y. (2006). Motor deficits and hyperactivity in Dyt1 knockdown mice. Neurosci. Res.56, 470-474.","DOI":"10.1016\/j.neures.2006.09.005"},{"key":"2021042523534123200_REF16","unstructured":"Djabali, K. (1999). Cytoskeletal proteins connecting intermediate filaments to cytoplasmic and nuclear periphery. Histol. Histopathol.14, 501-509."},{"key":"2021042523534123200_REF17","doi-asserted-by":"crossref","unstructured":"Dubey, M., Hoda, S., Chan, W. K., Pimenta, A., Ortiz, D. D. and Shea, T. B. (2004). Reexpression of vimentin in differentiated neuroblastoma cells enhances elongation of axonal neurites. J. Neurosci. Res.78, 245-249.","DOI":"10.1002\/jnr.20146"},{"key":"2021042523534123200_REF18","doi-asserted-by":"crossref","unstructured":"Eckes, B., Dogic, D., Colucci-Guyon, E., Wang, N., Maniotis, A., Ingber, D., Merckling, A., Langa, F., Aumailley, M., Delouvee, A. et al. (1998). Impaired mechanical stability, migration and contractile capacity in vimentin-deficient fibroblasts. J. Cell Sci.111, 245-249.","DOI":"10.1242\/jcs.111.13.1897"},{"key":"2021042523534123200_REF19","unstructured":"Eidelberg, D. (1998). Abnormal brain networks in DYT1 dystonia. Adv. Neurol.78, 127-133."},{"key":"2021042523534123200_REF20","doi-asserted-by":"crossref","unstructured":"Eriksson, J. E., He, T., Trejo-Skalli, A. V., Harmala-Brasken, A. S., Hellman, J., Chou, Y. H. and Goldman, R. D. (2004). Specific in vivo phosphorylation sites determine the assembly dynamics of vimentin intermediate filaments. J. Cell Sci.117, 919-932.","DOI":"10.1242\/jcs.00906"},{"key":"2021042523534123200_REF21","doi-asserted-by":"crossref","unstructured":"Esue, O., Carson, A. A., Tseng, Y. and Wirtz, D. (2006). A direct interaction between actin and vimentin filaments mediated by the tail domain of vimentin. J. Biol. Chem.281, 30393-30399.","DOI":"10.1074\/jbc.M605452200"},{"key":"2021042523534123200_REF22","doi-asserted-by":"crossref","unstructured":"Foisner, R., Traub, P. and Wiche, G. (1991). Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin. Proc. Natl. Acad. Sci. USA88, 3812-3816.","DOI":"10.1073\/pnas.88.9.3812"},{"key":"2021042523534123200_REF23","doi-asserted-by":"crossref","unstructured":"Gerace, L. (2004). TorsinA and torsion dystonia: unraveling the architecture of the nuclear envelope. Proc. Natl. Acad. Sci. USA101, 8839-8840.","DOI":"10.1073\/pnas.0402441101"},{"key":"2021042523534123200_REF24","doi-asserted-by":"crossref","unstructured":"Gomes, E. R. and Gundersen, G. G. (2006). Real-time centrosome reorientation during fibroblast migration. Methods Enzymol.406, 579-592.","DOI":"10.1016\/S0076-6879(06)06045-9"},{"key":"2021042523534123200_REF25","doi-asserted-by":"crossref","unstructured":"Gomes, E. R., Jani, S. and Gundersen, G. G. (2005). Nuclear movement regulated by Cdc42, MRCK, myosin, and actin flow establishes MTOC polarization in migrating cells. Cell121, 451-463.","DOI":"10.1016\/j.cell.2005.02.022"},{"key":"2021042523534123200_","doi-asserted-by":"crossref","unstructured":"Gonzalez-Agosti, P. and Paulson, H. L. (2004). Aberrant cellular behavior of mutant torsinA implicates nuclear envelope dysfunction in DYT1 dystonia. J. Neurosci.24, 2593-2601.","DOI":"10.1523\/JNEUROSCI.4461-03.2004"},{"key":"2021042523534123200_REF27","doi-asserted-by":"crossref","unstructured":"Goodchild, R. E. and Dauer, W. T. (2005). The AAA+ protein torsinA interacts with a conserved domain present in LAP1 and a novel ER protein. J. Cell Biol.168, 855-862.","DOI":"10.1083\/jcb.200411026"},{"key":"2021042523534123200_REF28","doi-asserted-by":"crossref","unstructured":"Goodchild, R. E., Kim, C. E. and Dauer, W. T. (2005). Loss of the dystonia-associated protein torsinA selectively disrupts the neuronal nuclear envelope. Neuron48, 923-932.","DOI":"10.1016\/j.neuron.2005.11.010"},{"key":"2021042523534123200_REF29","doi-asserted-by":"crossref","unstructured":"Grundmann, K., Reischmann, B., Vanhoutte, G., Hubener, J., Teismann, P., Hauser, T. K., Bonin, M., Wilbertz, J., Horn, S., Nguyen, H. P. et al. (2007). Overexpression of human wildtype torsinA and human DeltaGAG torsinA in a transgenic mouse model causes phenotypic abnormalities. Neurobiol. Dis.27, 190-206.","DOI":"10.1016\/j.nbd.2007.04.015"},{"key":"2021042523534123200_REF30","doi-asserted-by":"crossref","unstructured":"Hanson, P. I. and Whiteheart, S. W. (2005). AAA+ proteins: have engine, will work. Nat. Rev. Mol. Cell Biol.6, 519-529.","DOI":"10.1038\/nrm1684"},{"key":"2021042523534123200_REF31","doi-asserted-by":"crossref","unstructured":"Herrmann, H., Ba\u0308r, H., Kreplak, L., Strelkov, S. V. and Aebi, U. (2007). Intermediate filaments: from cell architecture to nanomechanics. Nat. Rev. Mol. Cell Biol.8, 562-573.","DOI":"10.1038\/nrm2197"},{"key":"2021042523534123200_REF32","doi-asserted-by":"crossref","unstructured":"Hewett, J., Ziefer, P., Bergeron, D., Naismith, T., Boston, H., Slater, D., Wilbur, J., Schuback, D., Kamm, C., Smith, N. et al. (2003). TorsinA in PC12 cells: localization in the endoplasmic reticulum and response to stress. J. Neurosci. Res.72, 158-168.","DOI":"10.1002\/jnr.10567"},{"key":"2021042523534123200_REF33","doi-asserted-by":"crossref","unstructured":"Hewett, J. W., Kamm, C., Boston, H., Beauchamp, R., Naismith, T., Ozelius, L., Hanson, P. I., Breakefield, X. O. and Ramesh, V. (2004). TorsinB-perinuclear location and association with torsinA. J. Neurochem.89, 1186-1194.","DOI":"10.1111\/j.1471-4159.2004.02404.x"},{"key":"2021042523534123200_REF34","doi-asserted-by":"crossref","unstructured":"Hewett, J. W., Zeng, J., Niland, B. P., Bragg, D. C. and Breakefield, X. O. (2006). Dystonia-causing mutant torsinA inhibits cell adhesion and neurite extension through interference with cytoskeletal dynamics. Neurobiol. Dis.22, 98-111.","DOI":"10.1016\/j.nbd.2005.10.012"},{"key":"2021042523534123200_REF35","doi-asserted-by":"crossref","unstructured":"Hewett, J. W., Tannous, B., Niland, B. P., Nery, F. C. and Breakefield, X. O. (2007). Mutant torsinA interferes with protein processing through the secretory pathway in DYT1 dystonia cells. Proc. Natl. Acad. Sci. USA104, 7271-7276.","DOI":"10.1073\/pnas.0701185104"},{"key":"2021042523534123200_REF36","doi-asserted-by":"crossref","unstructured":"Hewett, J. W., Nery, F. C., Niland, B., Ge, P., Tan, P., Hadwiger, P., Tannous, B. A., Sah, D. W. and Breakefield, X. O. (2008). siRNA knock-down of mutant torsinA restores processing through secretory pathway in DYT1 dystonia cells. Hum. Mol. Genet.17, 1436-1445.","DOI":"10.1093\/hmg\/ddn032"},{"key":"2021042523534123200_REF37","doi-asserted-by":"crossref","unstructured":"Hunter, A., Archer, C. W., Walker, P. S. and Blunn, G. W. (1995). Attachment and proliferation of osteoblasts and fibroblasts on biomaterials for orthopaedic use. Biomaterials16, 298-295.","DOI":"10.1016\/0142-9612(95)93256-D"},{"key":"2021042523534123200_REF38","doi-asserted-by":"crossref","unstructured":"Kamm, C., Boston, H., Hewett, J., Wilbur, J., Corey, D. P., Hanson, P. I., Ramesh, V. and Breakefield, X. O. (2004). The early onset dystonia protein torsinA interacts with kinesin light chain 1. J. Biol. Chem.279, 19882-19892.","DOI":"10.1074\/jbc.M401332200"},{"key":"2021042523534123200_REF39","doi-asserted-by":"crossref","unstructured":"Kamm, C., Asmus, F., Muller, J., Mayer, P., Sharma, M., Muller, U., Bekert, S., Ehling, R., Illig, T., Wichmann, H. et al. (2006). Strong genetic evidence for association of TOR1A\/TOR1B with idiopathic dystonia. Neurology67, 1857-1859.","DOI":"10.1212\/01.wnl.0000244423.63406.17"},{"key":"2021042523534123200_REF40","doi-asserted-by":"crossref","unstructured":"Kamm, C., Ozelius, L. J. and Breakefield, X. O. (2008). TorsinA and DYT1 early onset dystonia. Funct. Neurol.61-72.","DOI":"10.2217\/14796708.3.1.61"},{"key":"2021042523534123200_REF41","doi-asserted-by":"crossref","unstructured":"Ketema, M., Wilhelmsen, K., Kuikman, I., Janssen, H., Hodzic, D. and Sonnenberg, A. (2007). Requirements for the localization of nesprin-3 at the nuclear envelope and its interaction with plectin. J. Cell Sci.120, 3384-3394.","DOI":"10.1242\/jcs.014191"},{"key":"2021042523534123200_REF42","doi-asserted-by":"crossref","unstructured":"Kock, N., Naismith, T. V., Boston, H. E., Ozelius, L. J., Corey, D. P., Breakefield, X. O. and Hanson, P. I. (2006). Effects of genetic variations in the dystonia protein torsinA: identification of polymorphism at residue 216 as protein modifier. Hum. Mol. Genet.15, 1355-1364.","DOI":"10.1093\/hmg\/ddl055"},{"key":"2021042523534123200_REF43","unstructured":"Kustedjo, K., Bracey, M. H. and Cravatt, B. F. (2000). TorsinA and its torsion dystonia-associated mutant forms are lumenal glycoproteins that exhibit distinct subcellular localizations. J. Biol. Chem.275, 680-685."},{"key":"2021042523534123200_REF44","doi-asserted-by":"crossref","unstructured":"Liu, Z., Zolkiewska, A. and Zolkiewski, M. (2003). Characterization of human torsinA and its dystonia-associated mutant form. Biochem. J.374, 117-122.","DOI":"10.1042\/bj20030258"},{"key":"2021042523534123200_REF45","doi-asserted-by":"crossref","unstructured":"Lupas, A., Flanagan, J. M., Tamura, T. and Baumeister, W. (1997). Self-compartmentalizing proteases. Trends Biochem. Sci.22, 399-404.","DOI":"10.1016\/S0968-0004(97)01117-1"},{"key":"2021042523534123200_REF46","doi-asserted-by":"crossref","unstructured":"Maison, C., Pyrpasopoulou, A., Theodoropoulos, P. A. and Georgatos, S. D. (1997). The inner nuclear membrane protein LAP1 forms a native complex with B-type lamins and partitions with spindle-associated mitotic vesicles. EMBO J.16, 4839-4850.","DOI":"10.1093\/emboj\/16.16.4839"},{"key":"2021042523534123200_REF47","unstructured":"Malone, C. J., Misner, L., Le Bot, N., Tsai, M. C., Campbell, J. M., Ahringer, J. and White, J. G. (2003). The C. elegans hook protein, ZYG-12, mediates the essential attachment between the centrosome and nucleus. Cell115, 825-836."},{"key":"2021042523534123200_REF48","doi-asserted-by":"crossref","unstructured":"McNaught, K. S., Kapustin, A., Jackson, T., Jengelley, T. A., Jnobaptiste, R., Shashidharan, P., Perl, D. P., Pasik, P. and Olanow, C. W. (2004). Brainstem pathology in DYT1 primary torsion dystonia. Ann. Neurol.56, 540-547.","DOI":"10.1002\/ana.20225"},{"key":"2021042523534123200_REF49","doi-asserted-by":"crossref","unstructured":"Naismith, T. V., Heuser, J. E., Breakefield, X. O. and Hanson, P. I. (2004). TorsinA in the nuclear envelope. Proc. Natl. Acad. Sci. USA101, 7612-7617.","DOI":"10.1073\/pnas.0308760101"},{"key":"2021042523534123200_REF50","doi-asserted-by":"crossref","unstructured":"Neuwald, A. F., Aravind, L., Spouge, J. L. and Koonin, E. V. (1999). AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res.9, 27-43.","DOI":"10.1101\/gr.9.1.27"},{"key":"2021042523534123200_REF51","doi-asserted-by":"crossref","unstructured":"Ozelius, L. J., Hewett, J. W., Page, C. E., Bressman, S. B., Kramer, P. L., Shalish, C., de Leon, D., Brin, M. F., Raymond, D., Corey, D. P. et al. (1997). The early-onset torsion dystonia gene (DYT1) encodes an ATP-binding protein. Nat. Genet.17, 40-48.","DOI":"10.1038\/ng0997-40"},{"key":"2021042523534123200_REF52","doi-asserted-by":"crossref","unstructured":"Perlson, E., Hanz, S., Ben-Yaakov, K., Segal-Ruder, Y., Seger, R. and Fainzilber, M. (2005). Vimentin-dependent spatial translocation of an activated MAP kinase in injured nerve. Neuron45, 715-726.","DOI":"10.1016\/j.neuron.2005.01.023"},{"key":"2021042523534123200_REF53","doi-asserted-by":"crossref","unstructured":"Pham, P., Frei, K. P., Woo, W. and Truong, D. D. (2006). Molecular defects of the dystonia-causing torsinA mutation. NeuroReport17, 1725-1728.","DOI":"10.1097\/WNR.0b013e3280101220"},{"key":"2021042523534123200_REF54","doi-asserted-by":"crossref","unstructured":"Rostasy, K., Augood, S. J., Hewett, J. W., Leung, J. C., Sasaki, H., Ozelius, L. J., Ramesh, V., Standaert, D. G., Breakefield, X. O. and Hedreen, J. C. (2003). TorsinA protein and neuropathology in early onset generalized dystonia with GAG deletion. Neurobiol. Dis.12, 11-24.","DOI":"10.1016\/S0969-9961(02)00010-4"},{"key":"2021042523534123200_REF55","doi-asserted-by":"crossref","unstructured":"Sarria, A. J., Lieber, J. G., Nordeen, S. K. and Evans, R. M. (1994). The presence or absence of a vimentin-type intermediate filament network affects the shape of the nucleus in human SW-13 cells. J. Cell Sci.107, 1593-1607.","DOI":"10.1242\/jcs.107.6.1593"},{"key":"2021042523534123200_REF56","doi-asserted-by":"crossref","unstructured":"Sena-Esteves, M., Tebbets, J. C., Steffens, S., Crombleholme, T. and Flake, A. W. (2004). Optimized large-scale production of high titer lentivirus vector pseudotypes. J. Virol. Methods122, 131-139.","DOI":"10.1016\/j.jviromet.2004.08.017"},{"key":"2021042523534123200_REF57","doi-asserted-by":"crossref","unstructured":"Siegert, S., Bahn, E., Kramer, M. L., Schulz-Schaeffer, W. J., Hewett, J. W., Breakefield, X. O., Hedreen, J. C. and Rostasy, K. M. (2005). TorsinA expression is detectable in human infants as young as 4 weeks old. Brain Res. Dev. Brain Res.157, 19-26.","DOI":"10.1016\/j.devbrainres.2005.02.019"},{"key":"2021042523534123200_REF58","doi-asserted-by":"crossref","unstructured":"Sonnenberg, A. and Liem, R. K. (2007). Plakins in development and disease. Exp. Cell Res.313, 2189-2203.","DOI":"10.1016\/j.yexcr.2007.03.039"},{"key":"2021042523534123200_REF59","doi-asserted-by":"crossref","unstructured":"Starr, D. A. and Fischer, J. A. (2005). KASH `n Karry: the KASH domain family of cargo-specific cytoskeletal adaptor proteins. BioEssays27, 1136-1146.","DOI":"10.1002\/bies.20312"},{"key":"2021042523534123200_REF60","doi-asserted-by":"crossref","unstructured":"Torres, G. E., Sweeney, A. L., Beaulieu, J. M., Shashidharan, P. and Caron, M. G. (2004). Effect of torsinA on membrane proteins reveals a loss of function and a dominant-negative phenotype of the dystonia-associated DeltaE-torsinA mutant. Proc. Natl. Acad. Sci. USA101, 15650-15655.","DOI":"10.1073\/pnas.0308088101"},{"key":"2021042523534123200_REF61","doi-asserted-by":"crossref","unstructured":"Vasudevan, A., Breakefield, X. O. and Bhide, P. (2006). Developmental patterns of torsinA and torsinB expression. Brain Res.1073-1074, 139-145.","DOI":"10.1016\/j.brainres.2005.12.087"},{"key":"2021042523534123200_REF62","doi-asserted-by":"crossref","unstructured":"Wiche, G. (1998). Role of plectin in cytoskeleton organization and dynamics. J. Cell Sci.111, 2477-2486.","DOI":"10.1242\/jcs.111.17.2477"},{"key":"2021042523534123200_REF63","doi-asserted-by":"crossref","unstructured":"Wilhelmsen, K., Litjens, S. H., Kuikman, I., Tshimbalanga, N., Janssen, H., van den Bout, I., Raymond, K. and Sonnenberg, A. (2005). Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin. J. Cell Biol.171, 799-810.","DOI":"10.1083\/jcb.200506083"},{"key":"2021042523534123200_REF64","doi-asserted-by":"crossref","unstructured":"Wilhelmsen, K., Ketema, M., Truong, H. and Sonnenberg, A. (2006). KASH-domain proteins in nuclear migration, anchorage and other processes. J. Cell Sci.119, 5021-5029.","DOI":"10.1242\/jcs.03295"},{"key":"2021042523534123200_REF65","doi-asserted-by":"crossref","unstructured":"Worman, H. J. and Gundersen, G. G. (2006). Here come the SUNs: a nucleocytoskeletal missing link. Trends Cell Biol.16, 67-69.","DOI":"10.1016\/j.tcb.2005.12.006"},{"key":"2021042523534123200_REF66","doi-asserted-by":"crossref","unstructured":"Xiao, J., Gong, S., Zhao, Y. and LeDoux, M. S. (2004). Developmental expression of rat torsinA transcript and protein. Brain Res. Dev. Brain Res.152, 47-60.","DOI":"10.1016\/j.devbrainres.2004.05.012"},{"key":"2021042523534123200_REF67","unstructured":"Yokoi, F., Dang, M. T., Mitsui, S., Li, J. and Li, Y. (2008). Motor deficits and hyperactivity in cerebral cortex-specific Dyt1 conditional knockout mice. J. Biochem.143, 39-47."},{"key":"2021042523534123200_REF68","doi-asserted-by":"crossref","unstructured":"Young, K. G., Pinheiro, B. and Kothary, R. (2006). A Bpag1 isoform involved in cytoskeletal organization surrounding the nucleus. Exp. Cell Res.312, 121-134.","DOI":"10.1016\/j.yexcr.2005.10.002"}],"container-title":["Journal of Cell Science"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/journals.biologists.com\/jcs\/article-pdf\/121\/20\/3476\/1504400\/3476.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"http:\/\/journals.biologists.com\/jcs\/article-pdf\/121\/20\/3476\/1504400\/3476.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,20]],"date-time":"2023-05-20T05:50:14Z","timestamp":1684561814000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.biologists.com\/jcs\/article\/121\/20\/3476\/35334\/TorsinA-binds-the-KASH-domain-of-nesprins-and"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2008,10,15]]},"references-count":68,"journal-issue":{"issue":"20","published-print":{"date-parts":[[2008,10,15]]}},"URL":"https:\/\/doi.org\/10.1242\/jcs.029454","relation":{},"ISSN":["1477-9137","0021-9533"],"issn-type":[{"value":"1477-9137","type":"electronic"},{"value":"0021-9533","type":"print"}],"subject":[],"published":{"date-parts":[[2008,10,15]]}}}