{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,5]],"date-time":"2026-08-05T02:23:10Z","timestamp":1785896590781,"version":"3.56.0"},"reference-count":65,"publisher":"American Association for the Advancement of Science (AAAS)","issue":"21","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Sci. Adv."],"published-print":{"date-parts":[[2022,5,27]]},"abstract":"<jats:p>While amyloid-\u03b2 lies upstream of tau pathology in Alzheimer\u2019s disease, key drivers for other tauopathies, including progressive supranuclear palsy (PSP), are largely unknown. Various tau mutations are known to facilitate tau aggregation, but how the nonmutated tau, which most cases with PSP share, increases its propensity to aggregate in neurons and glial cells has remained elusive. Here, we identified genetic variations and protein abundance of filamin-A in the PSP brains without tau mutations. We provided in vivo biochemical evidence that increased filamin-A levels enhance the phosphorylation and insolubility of tau through interacting actin filaments. In addition, reduction of filamin-A corrected aberrant tau levels in the culture cells from PSP cases. Moreover, transgenic mice carrying human filamin-A recapitulated tau pathology in the neurons. Our data highlight that filamin-A promotes tau aggregation, providing a potential mechanism by which filamin-A contributes to PSP pathology.<\/jats:p>","DOI":"10.1126\/sciadv.abm5029","type":"journal-article","created":{"date-parts":[[2022,5,25]],"date-time":"2022-05-25T17:57:46Z","timestamp":1653501466000},"source":"Crossref","is-referenced-by-count":30,"title":["Actin-binding protein filamin-A drives tau aggregation and contributes to progressive supranuclear palsy pathology"],"prefix":"10.1126","volume":"8","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9316-2476","authenticated-orcid":true,"given":"Koyo","family":"Tsujikawa","sequence":"first","affiliation":[{"name":"Department of Neurology, Nagoya University Graduate School of Medicine, Nagoya, Japan."},{"name":"Department of Neurology, Japanese Red Cross Aichi Medical Center Nagoya Daini Hospital, Nagoya, Japan."},{"name":"Department of Neurology , National Hospital Organization Suzuka National Hospital, Suzuka, 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mitogen-activated protein kinase (MAPK\/ERK-P), protein kinase of 38kDa (p38-P), stress-activated protein kinase (SAPK\/JNK-P), and calcium\/calmodulin-dependent kinase II (CaM kinase II) are differentially expressed in tau deposits in neurons and glial cells in tauopathies","volume":"108","author":"Ferrer I.","year":"2001","unstructured":"I. 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Fromer, S. M. Purcell, Using XHMM software to detect copy number variation in whole-exome sequencing data. Curr. Protoc. Hum. Genet. 81, 7.23.1\u20137.23.21 (2014).","journal-title":"Curr. Protoc. Hum. Genet."},{"key":"e_1_3_3_62_2","doi-asserted-by":"publisher","DOI":"10.1038\/s41586-020-2329-2"},{"key":"e_1_3_3_63_2","doi-asserted-by":"publisher","DOI":"10.1038\/ng.2562"},{"key":"e_1_3_3_64_2","first-page":"1877","article-title":"Pin1 has opposite effects on wild-type and P301L tau stability and tauopathy","volume":"118","author":"Lim J.","year":"2008","unstructured":"J. Lim, M. Balastik, T. H. Lee, K. Nakamura, Y. C. Liou, A. Sun, G. Finn, L. Pastorino, V. M. Y. Lee, K. P. Lu, Pin1 has opposite effects on wild-type and P301L tau stability and tauopathy. J. Clin. Investig. 118, 1877\u20131889 (2008).","journal-title":"J. Clin. 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