{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,11]],"date-time":"2026-02-11T12:45:01Z","timestamp":1770813901417,"version":"3.50.1"},"reference-count":57,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2026,2,11]],"date-time":"2026-02-11T00:00:00Z","timestamp":1770768000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Cell. Neurosci."],"abstract":"<jats:sec>\n                    <jats:title>Background<\/jats:title>\n                    <jats:p>Makorin-2 (MKRN2) is an E3 ubiquitin ligase involved in multiple biological processes, yet its role in neurological disorders remains poorly understood. This study aims to elucidate how MKRN2 regulates the RNA-binding protein CSDE1\u2014a molecule linked to autism-related genes\u2014and to explore the functional implications of this interaction in neurodevelopment.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>\n                      Using mass-spectrometry screening, we identified CSDE1 as a direct substrate of MKRN2. Ubiquitination sites were validated through mutagenesis of conserved lysine residues. Liquid\u2013liquid phase separation (LLPS) assays were performed in HEK293 and SH-SY5Y cells, and behavioral phenotypes were assessed in\n                      <jats:italic>Mkrn2<\/jats:italic>\n                      -knockout mice. Statistical analyses included appropriate tests for comparing ubiquitination levels, condensate formation, and social behavior outcomes.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>\n                      MKRN2 mediates CSDE1 ubiquitination at four lysine residues (K81, K91, K208, K727). Deletion of\n                      <jats:italic>MKRN2<\/jats:italic>\n                      or mutation of these sites abolished ubiquitination. MKRN2 and CSDE1 formed co-localized condensates via LLPS, which was disrupted by functional impairment of either protein.\n                      <jats:italic>Mkrn2<\/jats:italic>\n                      -knockout mice exhibited sex-specific social abnormalities\u2014increased sociability in males and social withdrawal in females\u2014recapitulating autism-spectrum disorder (ASD) heterogeneity. We further identified\n                      <jats:italic>MARK1<\/jats:italic>\n                      and\n                      <jats:italic>HNRNPUL2<\/jats:italic>\n                      , ASD-associated mRNAs, as ubiquitination-dependent targets of CSDE1, linking aberrant condensate dynamics to synaptic plasticity deficits.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusion<\/jats:title>\n                    <jats:p>Our study reveals an LLPS-coupled ubiquitination mechanism by which MKRN2 regulates CSDE1, providing a novel molecular pathway underlying neurodevelopmental disorders. These findings offer new insights for understanding and treating neurological diseases such as ASD.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.3389\/fncel.2026.1757304","type":"journal-article","created":{"date-parts":[[2026,2,11]],"date-time":"2026-02-11T07:22:18Z","timestamp":1770794538000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":0,"title":["Liquid\u2013liquid phase separation couples MKRN2-mediated ubiquitination of CSDE1 with neurodevelopmental disorders"],"prefix":"10.3389","volume":"20","author":[{"given":"Zi","family":"Wang","sequence":"first","affiliation":[{"name":"National Center for Mental Disorders, Shanghai Mental Health Center, Brain Health Institute, Shanghai Jiao Tong University School of Medicine","place":["Shanghai, China"]},{"name":"State Key Laboratory of Molecular Biology, Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences","place":["Shanghai, China"]},{"name":"Department of Regeneration Science and Engineering, Institute for Frontier Life and Medical Sciences, Kyoto University","place":["Kyoto, Japan"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yaning","family":"Han","sequence":"additional","affiliation":[{"name":"Joint Laboratory of Guangdong-Hong Kong Universities for Vascular Homeostasis and Diseases, Department of Pharmacology, SUSTech Homeostatic Medicine Institute, School of Medicine, Southern University of Science and Technology","place":["Shenzhen, China"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Peng","family":"Yang","sequence":"additional","affiliation":[{"name":"School of Life Science and Technology, ShanghaiTech University","place":["Shanghai, China"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Caiwei","family":"Jia","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Molecular Biology, Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences","place":["Shanghai, China"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chuanyin","family":"Li","sequence":"additional","affiliation":[{"name":"Department of Colorectal Surgery and Oncology (Key Laboratory of Cancer and Intervention, China National Ministry of Education), The Second Affiliated Hospital, Zhejiang University School of Medicine","place":["Hangzhou, China"]},{"name":"Center for Medical Research and Innovation in Digestive System Tumors, Ministry of Education","place":["Hangzhou, China"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shilin","family":"Yuan","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Molecular Biology, Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences","place":["Shanghai, China"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pengfei","family":"Wei","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Digital Medicine, School of Biological Science and Medical Engineering, Southeast University","place":["Nanjing, China"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ronggui","family":"Hu","sequence":"additional","affiliation":[{"name":"National Center for Mental Disorders, Shanghai Mental Health Center, Brain Health Institute, Shanghai Jiao Tong University School of Medicine","place":["Shanghai, China"]},{"name":"State Key Laboratory of Molecular Biology, Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences","place":["Shanghai, China"]},{"name":"Department of Colorectal Surgery and Oncology (Key Laboratory of Cancer and Intervention, China National Ministry of Education), The Second Affiliated Hospital, Zhejiang University School of Medicine","place":["Hangzhou, China"]},{"name":"Center for Medical Research and Innovation in Digestive System Tumors, Ministry of Education","place":["Hangzhou, China"]},{"name":"Liangzhu Laboratory, State Key Laboratory of Brain-Machine Intelligence, MOE Frontier Science Center for Brain Science and Brain-Machine Integration, Zhejiang University","place":["Hangzhou, China"]}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1965","published-online":{"date-parts":[[2026,2,11]]},"reference":[{"key":"ref1","doi-asserted-by":"publisher","first-page":"4806","DOI":"10.1016\/j.jmb.2018.06.038","article-title":"A User's Guide for Phase Separation Assays with Purified Proteins","volume":"430","author":"Alberti","year":"2018","journal-title":"J. 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