{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T13:48:51Z","timestamp":1790430531712,"version":"4.1.0"},"reference-count":131,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2019,12,10]],"date-time":"2019-12-10T00:00:00Z","timestamp":1575936000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2019,12,10]],"date-time":"2019-12-10T00:00:00Z","timestamp":1575936000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"name":"Endeavour Scholarship"},{"name":"University of Malta Research Fund; Malta Council for Science & Technology Internationalisation Partnership Award"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Sci Rep"],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    The predominant motor neuron disease in infants and adults is spinal muscular atrophy (SMA) and amyotrophic lateral sclerosis (ALS), respectively. SMA is caused by insufficient levels of the Survival Motor Neuron (SMN) protein, which operates as part of the multiprotein SMN complex that includes the DEAD-box RNA helicase Gemin3\/DDX20\/DP103.\n                    <jats:italic>C9orf72<\/jats:italic>\n                    ,\n                    <jats:italic>SOD1<\/jats:italic>\n                    ,\n                    <jats:italic>TDP-43<\/jats:italic>\n                    and\n                    <jats:italic>FUS<\/jats:italic>\n                    are ranked as the four major genes causing familial ALS. Accumulating evidence has revealed a surprising molecular overlap between SMA and ALS. Here, we ask the question of whether\n                    <jats:italic>Drosophila<\/jats:italic>\n                    can also be exploited to study shared pathogenic pathways. Focusing on motor behaviour, muscle mass and survival, we show that disruption of either TBPH\/TDP-43 or Caz\/FUS enhance defects associated with Gemin3 loss-of-function. Gemin3-associated neuromuscular junction overgrowth was however suppressed. Sod1 depletion had a modifying effect in late adulthood. We also show that Gemin3 self-interacts and\n                    <jats:italic>Gem3<\/jats:italic>\n                    <jats:sup>\n                      <jats:italic>\u0394N<\/jats:italic>\n                    <\/jats:sup>\n                    , a helicase domain deletion mutant, retains the ability to interact with its wild-type counterpart. Importantly, mutant:wild-type dimers are favoured more than wild-type:wild-type dimers. In addition to reinforcing the link between SMA and ALS, further exploration of mechanistic overlaps is now possible in a genetically tractable model organism. Notably, Gemin3 can be elevated to a candidate for modifying motor neuron degeneration.\n                  <\/jats:p>","DOI":"10.1038\/s41598-019-53508-4","type":"journal-article","created":{"date-parts":[[2019,12,10]],"date-time":"2019-12-10T06:03:32Z","timestamp":1575957812000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":25,"title":["SMN complex member Gemin3 self-interacts and has a functional relationship with ALS-linked proteins TDP-43, FUS and Sod1"],"prefix":"10.1038","volume":"9","author":[{"given":"Rebecca","family":"Cacciottolo","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joanna","family":"Ciantar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maia","family":"Lanfranco","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rebecca M.","family":"Borg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Neville","family":"Vassallo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R\u00e9my","family":"Bordonn\u00e9","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6150-1608","authenticated-orcid":false,"given":"Ruben J.","family":"Cauchi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2019,12,10]]},"reference":[{"key":"53508_CR1","doi-asserted-by":"publisher","first-page":"323","DOI":"10.1146\/annurev-pathol-011110-130307","volume":"7","author":"F Ibrahim","year":"2012","unstructured":"Ibrahim, F., Nakaya, T. & Mourelatos, Z. RNA dysregulation in diseases of motor neurons. Annu Rev Pathol 7, 323\u2013352, https:\/\/doi.org\/10.1146\/annurev-pathol-011110-130307 (2012).","journal-title":"Annu Rev Pathol"},{"key":"53508_CR2","doi-asserted-by":"publisher","first-page":"e21","DOI":"10.1017\/S1462399410001523","volume":"12","author":"D Baumer","year":"2010","unstructured":"Baumer, D., Ansorge, O., Almeida, M. & Talbot, K. The role of RNA processing in the pathogenesis of motor neuron degeneration. Expert reviews in molecular medicine 12, e21, https:\/\/doi.org\/10.1017\/S1462399410001523 (2010).","journal-title":"Expert reviews in molecular medicine"},{"issue":"415","key":"53508_CR3","doi-asserted-by":"publisher","first-page":"eaah5436","DOI":"10.1126\/scitranslmed.aah5436","volume":"9","author":"Daisuke Ito","year":"2017","unstructured":"Ito, D., Hatano, M. & Suzuki, N. RNA binding proteins and the pathological cascade in ALS\/FTD neurodegeneration. 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