{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,19]],"date-time":"2025-10-19T06:05:57Z","timestamp":1760853957092,"version":"3.41.2"},"reference-count":55,"publisher":"Frontiers Media SA","funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["1R01GM114401"],"award-info":[{"award-number":["1R01GM114401"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Mol. Biosci."],"DOI":"10.3389\/fmolb.2017.00029","type":"journal-article","created":{"date-parts":[[2017,5,11]],"date-time":"2017-05-11T12:10:17Z","timestamp":1494504617000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":20,"title":["Torsin ATPases: Harnessing Dynamic Instability for Function"],"prefix":"10.3389","volume":"4","author":[{"given":"Anna R.","family":"Chase","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ethan","family":"Laudermilch","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christian","family":"Schlieker","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1965","published-online":{"date-parts":[[2017,5,11]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"E4017","DOI":"10.1073\/pnas.1500257112","article-title":"Unique double-ring structure of the peroxisomal Pex1\/Pex6 ATPase complex revealed by cryo-electron microscopy","volume":"112","author":"Blok","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B2","doi-asserted-by":"publisher","first-page":"E4822","DOI":"10.1073\/pnas.1415271111","article-title":"The mechanism of Torsin ATPase activation","volume":"111","author":"Brown","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B3","doi-asserted-by":"publisher","first-page":"371","DOI":"10.1002\/mds.26880","article-title":"Membrane defects and genetic redundancy: are we at a turning point for DYT1 dystonia?","volume":"32","author":"Cascalho","year":"2017","journal-title":"Mov. Disord."},{"key":"B4","doi-asserted-by":"publisher","first-page":"3502","DOI":"10.1093\/hmg\/ddq266","article-title":"The early-onset torsion dystonia-associated protein, torsinA, is a homeostatic regulator of endoplasmic reticulum stress response","volume":"19","author":"Chen","year":"2010","journal-title":"Hum. Mol. Genet."},{"key":"B5","doi-asserted-by":"publisher","first-page":"17983","DOI":"10.7554\/eLife.17983","article-title":"Structures of TorsinA and its disease-mutant complexed with an activator reveal the molecular basis for primary dystonia","volume":"5","author":"Demircioglu","year":"2016","journal-title":"Elife"},{"key":"B6","doi-asserted-by":"publisher","first-page":"1030","DOI":"10.1016\/j.cell.2010.04.036","article-title":"Cell cycle-dependent differences in nuclear pore complex assembly in metazoa","volume":"141","author":"Doucet","year":"2010","journal-title":"Cell"},{"key":"B7","doi-asserted-by":"publisher","first-page":"141","DOI":"10.1111\/tra.12141","article-title":"Enriching the pore: splendid complexity from humble origins","volume":"15","author":"Field","year":"2014","journal-title":"Traffic"},{"key":"B8","doi-asserted-by":"publisher","first-page":"1267","DOI":"10.1016\/0092-8674(93)90355-T","article-title":"Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation","volume":"73","author":"Foisner","year":"1993","journal-title":"Cell"},{"key":"B9","doi-asserted-by":"publisher","first-page":"2854","DOI":"10.1242\/jcs.167452","article-title":"Access of torsinA to the inner nuclear membrane is activity dependent and regulated in the endoplasmic reticulum","volume":"128","author":"Goodchild","year":"2015","journal-title":"J. Cell Sci."},{"key":"B10","doi-asserted-by":"publisher","first-page":"847","DOI":"10.1073\/pnas.0304375101","article-title":"Mislocalization to the nuclear envelope: an effect of the dystonia-causing torsinA mutation","volume":"101","author":"Goodchild","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B11","doi-asserted-by":"publisher","first-page":"855","DOI":"10.1083\/jcb.200411026","article-title":"The AAA+ protein torsinA interacts with a conserved domain present in LAP1 and a novel ER protein","volume":"168","author":"Goodchild","year":"2005","journal-title":"J. Cell Biol."},{"key":"B12","doi-asserted-by":"publisher","first-page":"923","DOI":"10.1016\/j.neuron.2005.11.010","article-title":"Loss of the dystonia-associated protein torsinA selectively disrupts the neuronal nuclear envelope","volume":"48","author":"Goodchild","year":"2005","journal-title":"Neuron"},{"key":"B13","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1016\/j.devcel.2016.06.017","article-title":"Torsins are essential regulators of cellular lipid metabolism","volume":"38","author":"Grillet","year":"2016","journal-title":"Dev. Cell"},{"key":"B14","doi-asserted-by":"publisher","first-page":"519","DOI":"10.1038\/nrm1684","article-title":"AAA+ proteins: have engine, will work","volume":"6","author":"Hanson","year":"2005","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"B15","doi-asserted-by":"publisher","first-page":"a010165","DOI":"10.1101\/cshperspect.a010165","article-title":"Replication clamps and clamp loaders","volume":"5","author":"Hedglin","year":"2013","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"B16","doi-asserted-by":"publisher","first-page":"988","DOI":"10.1016\/j.celrep.2013.03.015","article-title":"Torsin mediates primary envelopment of large ribonucleoprotein granules at the nuclear envelope","volume":"3","author":"Jokhi","year":"2013","journal-title":"Cell Rep."},{"key":"B17","doi-asserted-by":"publisher","first-page":"888","DOI":"10.1093\/hmg\/ddp557","article-title":"Relative tissue expression of homologous torsinB correlates with the neuronal specific importance of DYT1 dystonia-associated torsinA","volume":"19","author":"Jungwirth","year":"2010","journal-title":"Hum. Mol. Genet."},{"key":"B18","doi-asserted-by":"publisher","first-page":"532","DOI":"10.1002\/bip.22827","article-title":"Review: the lord of the rings: structure and mechanism of the sliding clamp loader","volume":"105","author":"Kelch","year":"2016","journal-title":"Biopolymers"},{"key":"B19","doi-asserted-by":"publisher","first-page":"9861","DOI":"10.1073\/pnas.0912877107","article-title":"A molecular mechanism underlying the neural-specific defect in torsinA mutant mice","volume":"107","author":"Kim","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B20","doi-asserted-by":"publisher","first-page":"1162","DOI":"10.1016\/j.cell.2016.01.034","article-title":"The nuclear pore complex as a flexible and dynamic gate","volume":"164","author":"Knockenhauer","year":"2016","journal-title":"Cell"},{"key":"B21","doi-asserted-by":"publisher","first-page":"363","DOI":"10.1126\/science.aaf0643","article-title":"Molecular architecture of the inner ring scaffold of the human nuclear pore complex","volume":"352","author":"Kosinski","year":"2016","journal-title":"Science"},{"key":"B22","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.ceb.2016.01.001","article-title":"Torsin ATPases: structural insights and functional perspectives","volume":"40","author":"Laudermilch","year":"2016","journal-title":"Curr. Opin. Cell Biol."},{"key":"B23","doi-asserted-by":"publisher","first-page":"3964","DOI":"10.1091\/mbc.E16-07-0511","article-title":"Dissecting Torsin\/cofactor function at the nuclear envelope: a genetic study","volume":"27","author":"Laudermilch","year":"2016","journal-title":"Mol. Biol. Cell"},{"key":"B24","doi-asserted-by":"publisher","first-page":"3080","DOI":"10.1172\/JCI72830","article-title":"TorsinA hypofunction causes abnormal twisting movements and sensorimotor circuit neurodegeneration","volume":"124","author":"Liang","year":"2014","journal-title":"J. Clin. Invest."},{"key":"B25","doi-asserted-by":"publisher","first-page":"aaf1015","DOI":"10.1126\/science.aaf1015","article-title":"Architecture of the symmetric core of the nuclear pore","volume":"352","author":"Lin","year":"2016","journal-title":"Science"},{"key":"B26","doi-asserted-by":"publisher","first-page":"173","DOI":"10.4161\/nucl.2.3.16243","article-title":"TAN lines: a novel nuclear envelope structure involved in nuclear positioning","volume":"2","author":"Luxton","year":"2011","journal-title":"Nucleus"},{"key":"B27","doi-asserted-by":"publisher","first-page":"1147","DOI":"10.1038\/nsmb.1503","article-title":"Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding","volume":"15","author":"Martin","year":"2008","journal-title":"Nat. Struct. Mol. Biol."},{"key":"B28","doi-asserted-by":"publisher","first-page":"17615","DOI":"10.1074\/jbc.M209686200","article-title":"Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity","volume":"278","author":"Mogk","year":"2003","journal-title":"J. Biol. Chem."},{"key":"B29","doi-asserted-by":"publisher","first-page":"27866","DOI":"10.1074\/jbc.M109.020164","article-title":"Interaction of torsinA with its major binding partners is impaired by the dystonia-associated DeltaGAG deletion","volume":"284","author":"Naismith","year":"2009","journal-title":"J. Biol. Chem."},{"key":"B30","doi-asserted-by":"publisher","first-page":"7612","DOI":"10.1073\/pnas.0308760101","article-title":"TorsinA in the nuclear envelope","volume":"101","author":"Naismith","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B31","doi-asserted-by":"publisher","first-page":"393","DOI":"10.1038\/ncomms1383","article-title":"TorsinA participates in endoplasmic reticulum-associated degradation","volume":"2","author":"Nery","year":"2011","journal-title":"Nat. Commun."},{"key":"B32","doi-asserted-by":"publisher","first-page":"33","DOI":"10.1038\/nrmicro.2015.4","article-title":"Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines","volume":"14","author":"Olivares","year":"2016","journal-title":"Nat. Rev. Microbiol."},{"key":"B33","doi-asserted-by":"publisher","first-page":"e19071","DOI":"10.7554\/eLife.19071","article-title":"Nuclear pore assembly proceeds by an inside-out extrusion of the nuclear envelope","volume":"5","author":"Otsuka","year":"2016","journal-title":"Elife"},{"key":"B34","doi-asserted-by":"publisher","first-page":"40","DOI":"10.1038\/ng0997-40","article-title":"The early-onset torsion dystonia gene (DYT1) encodes an ATP-binding protein","volume":"17","author":"Ozelius","year":"1997","journal-title":"Nat. Genet."},{"key":"B35","doi-asserted-by":"publisher","first-page":"e08352","DOI":"10.7554\/elife.08352","article-title":"Forebrain deletion of the dystonia protein torsinA causes dystonic-like movements and loss of striatal cholinergic neurons","volume":"4","author":"Pappas","year":"2015","journal-title":"Elife"},{"key":"B36","doi-asserted-by":"publisher","first-page":"532","DOI":"10.3109\/10409238.2015.1091804","article-title":"Torsins: not your typical AAA+ ATPases","volume":"50","author":"Rose","year":"2015","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"B37","doi-asserted-by":"publisher","first-page":"552","DOI":"10.1074\/jbc.M113.515791","article-title":"Arresting a Torsin ATPase reshapes the endoplasmic reticulum","volume":"289","author":"Rose","year":"2014","journal-title":"J. Biol. Chem."},{"key":"B38","doi-asserted-by":"publisher","first-page":"657","DOI":"10.1083\/jcb.201507113","article-title":"TorsinA controls TAN line assembly and the retrograde flow of dorsal perinuclear actin cables during rearward nuclear movement","volume":"216","author":"Saunders","year":"2017","journal-title":"J. Cell Biol."},{"key":"B39","doi-asserted-by":"publisher","first-page":"257","DOI":"10.1016\/S0968-0004(98)01224-9","article-title":"GTPase-activating proteins: helping hands to complement an active site","volume":"23","author":"Scheffzek","year":"1998","journal-title":"Trends Biochem. Sci."},{"key":"B40","doi-asserted-by":"publisher","first-page":"e03239","DOI":"10.7554\/elife.03239","article-title":"How lamina-associated polypeptide 1 (LAP1) activates Torsin","volume":"3","author":"Sosa","year":"2014","journal-title":"Elife"},{"key":"B41","doi-asserted-by":"publisher","first-page":"1035","DOI":"10.1016\/j.cell.2012.03.046","article-title":"LINC Complexes Form by Binding of three Kash peptides to domain interfaces of trimeric Sun Proteins","volume":"149","author":"Sosa","year":"2012","journal-title":"Cell"},{"key":"B42","doi-asserted-by":"publisher","first-page":"3322","DOI":"10.1016\/j.celrep.2016.08.044","article-title":"Neuronal nuclear membrane budding occurs during a developmental window modulated by torsin paralogs","volume":"16","author":"Tanabe","year":"2016","journal-title":"Cell Rep."},{"key":"B43","doi-asserted-by":"publisher","first-page":"971","DOI":"10.1016\/j.cell.2013.07.037","article-title":"Identification of long-lived proteins reveals exceptional stability of essential cellular structures","volume":"154","author":"Toyama","year":"2013","journal-title":"Cell"},{"key":"B44","doi-asserted-by":"publisher","first-page":"e16011","DOI":"10.7554\/eLife.16011","article-title":"The Lamin B receptor is essential for cholesterol synthesis and perturbed by disease-causing mutations","volume":"5","author":"Tsai","year":"2016","journal-title":"Elife"},{"key":"B45","doi-asserted-by":"publisher","first-page":"687","DOI":"10.1083\/jcb.201409127","article-title":"Diffusion and retention are major determinants of protein targeting to the inner nuclear membrane","volume":"209","author":"Ungricht","year":"2015","journal-title":"J. Cell Biol."},{"key":"B46","doi-asserted-by":"publisher","first-page":"2661","DOI":"10.1091\/mbc.E09-01-0094","article-title":"LULL1 retargets TorsinA to the nuclear envelope revealing an activity that is impaired by the DYT1 dystonia mutation","volume":"20","author":"Vander Heyden","year":"2009","journal-title":"Mol. Biol. Cell"},{"key":"B47","doi-asserted-by":"publisher","first-page":"1752","DOI":"10.1091\/mbc.E14-07-1239","article-title":"A novel function for the Caenorhabditis elegans torsin OOC-5 in nucleoporin localization and nuclear import","volume":"26","author":"VanGompel","year":"2015","journal-title":"Mol. Biol. Cell"},{"key":"B48","doi-asserted-by":"publisher","first-page":"388","DOI":"10.1016\/j.cell.2014.09.012","article-title":"Surveillance of nuclear pore complex assembly by ESCRT-III\/Vps4","volume":"159","author":"Webster","year":"2014","journal-title":"Cell"},{"key":"B49","doi-asserted-by":"publisher","first-page":"29","DOI":"10.1016\/j.tcb.2015.08.002","article-title":"Border safety: quality control at the nuclear envelope","volume":"26","author":"Webster","year":"2016","journal-title":"Trends Cell Biol."},{"key":"B50","doi-asserted-by":"publisher","first-page":"830","DOI":"10.1038\/nsmb.3277","article-title":"Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation","volume":"23","author":"Yokom","year":"2016","journal-title":"Nat. Struct. Mol. Biol."},{"key":"B51","doi-asserted-by":"publisher","first-page":"E1545","DOI":"10.1073\/pnas.1300676110","article-title":"Regulation of Torsin ATPases by LAP1 and LULL1","volume":"110","author":"Zhao","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B52","doi-asserted-by":"publisher","first-page":"9469","DOI":"10.1074\/jbc.M115.709337","article-title":"Site-specific proteolysis mobilizes torsina from the membrane of the Endoplasmic Reticulum (ER) in response to ER Stress and B cell stimulation","volume":"291","author":"Zhao","year":"2016","journal-title":"J. Biol. Chem."},{"key":"B53","doi-asserted-by":"publisher","first-page":"61","DOI":"10.1038\/nature14148","article-title":"Mechanistic insights into the recycling machine of the SNARE complex","volume":"518","author":"Zhao","year":"2015","journal-title":"Nature"},{"key":"B54","doi-asserted-by":"publisher","first-page":"37271","DOI":"10.1074\/jbc.M110.123471","article-title":"A unique redox-sensing sensor II motif in TorsinA plays a critical role in nucleotide and partner binding","volume":"285","author":"Zhu","year":"2010","journal-title":"J. Biol. Chem."},{"key":"B55","doi-asserted-by":"publisher","first-page":"3599","DOI":"10.1091\/mbc.E08-01-0015","article-title":"The torsin-family AAA+ protein OOC-5 contains a critical disulfide adjacent to Sensor-II that couples redox state to nucleotide binding","volume":"19","author":"Zhu","year":"2008","journal-title":"Mol. Biol. Cell"}],"container-title":["Frontiers in Molecular Biosciences"],"original-title":[],"link":[{"URL":"http:\/\/journal.frontiersin.org\/article\/10.3389\/fmolb.2017.00029\/full","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2017,5,12]],"date-time":"2017-05-12T07:24:21Z","timestamp":1494573861000},"score":1,"resource":{"primary":{"URL":"http:\/\/journal.frontiersin.org\/article\/10.3389\/fmolb.2017.00029\/full"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,5,11]]},"references-count":55,"alternative-id":["10.3389\/fmolb.2017.00029"],"URL":"https:\/\/doi.org\/10.3389\/fmolb.2017.00029","relation":{},"ISSN":["2296-889X"],"issn-type":[{"type":"electronic","value":"2296-889X"}],"subject":[],"published":{"date-parts":[[2017,5,11]]},"article-number":"29"}}