{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T20:03:40Z","timestamp":1792785820689,"version":"4.5.0"},"reference-count":72,"publisher":"Oxford University Press (OUP)","license":[{"start":{"date-parts":[[2026,3,10]],"date-time":"2026-03-10T00:00:00Z","timestamp":1773100800000},"content-version":"am","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Australian National Health and Medical Research Council","award":["1095215"],"award-info":[{"award-number":["1095215"]}],"id":[{"id":"https:\/\/ror.org\/011kf5r70","id-type":"ROR","asserted-by":"crossref"}]},{"name":"Macquarie University Postgraduate Research Scholarship","id":[{"id":"https:\/\/ror.org\/01sf06y89","id-type":"ROR","asserted-by":"crossref"}]},{"DOI":"10.13039\/100016887","name":"Motor Neuron Disease Research Australia","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100016887","id-type":"DOI","asserted-by":"publisher"}]},{"name":"NHMRC Investigator","award":["2009564"],"award-info":[{"award-number":["2009564"]}]},{"name":"ARC Centre of Excellence for Innovations","award":["CE200100012"],"award-info":[{"award-number":["CE200100012"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Pathological forms of TAR-binding protein 43 (TDP-43), involving its aberrant mislocalization to the cytoplasm, inclusion formation, hyperphosphorylation and fragmentation, are present in \u223c45%\u201350% frontotemporal dementia and Alzheimer\u2019s disease individuals and most (97%) amyotrophic lateral sclerosis (ALS) cases. Hence, identifying mechanisms that induce TDP-43 pathology are central to neurodegeneration and developing new therapeutic targets in these conditions. Cofilin is a multifunctional protein with a crucial role in regulating the actin cytoskeleton. Actin has important neuronal-specific activities in dendritic spines, axonal growth cones and synapses and it is in constant equilibrium between two forms: monomeric globular actin (G-actin) and polymeric filamentous actin (F-actin). Cofilin controls actin dynamics by depolymerizing and severing actin filaments. When cofilin is phosphorylated (at serine-3, Ser3) by LIM kinase1 (LIMK1), it becomes inactive, leading to production of more F-actin. Defects in cofilin are well described in other neurodegenerative disorders, unlike in ALS.<\/jats:p>\n                  <jats:p>We examined phosphorylation of cofilin and actin dynamics in post-mortem spinal cord tissue from sporadic ALS (SALS) patients, the TDP-43 rNLS8 transgenic mouse model and NSC-34 motor neuronal cells expressing cytoplasmic TDP-43. F-actin was pharmacologically stabilized to mimic cofilin hyperphosphorylation and TDP-43 pathology was assessed. Neuronal cells were treated with a non-phosphorylatable cofilin S3A peptide (MAAGVAVSDGVIKVFN) and TDP-43 pathology and apoptosis were evaluated.<\/jats:p>\n                  <jats:p>Here, we show that cofilin is hyperphosphorylated in human ALS and disease models compared to controls. This was detected in spinal motor neurons from SALS patients and a TDP-43 mouse model (rNLS8) displaying key ALS phenotypes, and in motor neuronal NSC-34 cells expressing cytoplasmic TDP-43. Supporting this observation, more F-actin relative to G-actin was present in cortical\/spinal cord lysates from SALS patients and TDP-43 rNLS8 mice, and NSC-34 cells expressing TDP-43. We also show that mimicking cofilin hyperphosphorylation by pharmacological stabilization of F-actin induced TDP-43 pathology: cytoplasmic mislocalization, inclusion formation, hyperphosphorylation and fragmentation, and promoted its recruitment into stress granules (SGs). Furthermore, we detected increased levels of LIMK1 phosphorylation and tropomyosin isoforms 4.1 and 4.2 in SALS patients. These findings reveal aberrant cofilin hyperphosphorylation disrupts actin dynamics, triggering TDP-43 pathology and SG recruitment in SALS. They imply that preventing cofilin phosphorylation is a novel therapeutic strategy applicable to most ALS cases. Treatment of neuronal cells with the S3A peptide prevented features of TDP-43 pathology and apoptosis compared to control peptides. These findings thus describe a novel pathogenic mechanism producing TDP-43 pathology, applicable to most ALS cases and other neurodegenerative diseases.<\/jats:p>","DOI":"10.1093\/brain\/awag096","type":"journal-article","created":{"date-parts":[[2026,3,9]],"date-time":"2026-03-09T12:27:10Z","timestamp":1773059230000},"source":"Crossref","is-referenced-by-count":1,"title":["Cofilin hyperphosphorylation triggers TDP-43 pathology in sporadic amyotrophic lateral sclerosis"],"prefix":"10.1093","author":[{"given":"Cyril Jones","family":"Jagaraj","sequence":"first","affiliation":[{"name":"MND Research Centre, Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, Macquarie University , Sydney, NSW 2109 ,","place":["Australia"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sayanthooran","family":"Saravanabavan","sequence":"additional","affiliation":[{"name":"MND Research Centre, Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, 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,","place":["Australia"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fabiha","family":"Farzana","sequence":"additional","affiliation":[{"name":"MND Research Centre, Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, Macquarie University , Sydney, NSW 2109 ,","place":["Australia"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexandra K","family":"Suchowerska","sequence":"additional","affiliation":[{"name":"Translational Neuroscience Facility and Department of Physiology, School of Biomedical Sciences, University of New South Wales , Sydney, NSW 2052 ,","place":["Australia"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kuok","family":"Yap","sequence":"additional","affiliation":[{"name":"Institute of Molecular Bioscience, Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science, The University of Queensland , Brisbane, QLD 4072 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