Coronin1C SUMOylation modulates filopodia formation, neuritogenesis, and neuronal differentiation

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Abstract Actin dynamics in the cytosol and at the cell periphery are critical for metabolic processes and the formation of cellular projections. Coronin1C, a versatile cytoskeletal regulator, is an actin-binding protein that associates with actin at the leading edge. The effects of Coronin1C interactions on actin dynamics enable actin-mediated filopodia and neurite formation. Here, we report that Coronin1C is SUMOylated, but preferentially by SUMO1 at multiple lysine residues in its C-terminus. SUMOylation of Coronin1C impacts filopodia formation in cells; thus, cellular migration is significantly impaired when all five SUMOylatable residues are mutated. Further, we observe that Coronin1C SUMOylation is critically required for efficient neurite formation and extensive cellular projections during neuronal differentiation. Moreover, the non-SUMOylatable Coronin1C mutant forms cytoplasmic aggregates under neuronal differentiation conditions, a hallmark of neurodegenerative diseases. In conclusion, we report that Coronin1C is SUMOylated in its carboxy-terminus and COR1C SUMOylation is critical for cellular projections formation and neuronal differentiation.
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Coronin1C SUMOylation modulates filopodia formation, neuritogenesis, and neuronal differentiation | Research Square window.SnipcartSettings = { analytics: { enabled: false } }; (function() { var accessVector = localStorage.getItem('access_vector') || ''; window.dataLayer = window.dataLayer || []; if (accessVector) { window.dataLayer.push({ user: { profile: { profileInfo: { snid: accessVector } } } }); } })(); (function(w,d,s,l,i){w[l]=w[l]||[];w[l].push({'gtm.start':new Date().getTime(),event:'gtm.js'});var f=d.getElementsByTagName(s)[0],j=d.createElement(s),dl=l!='dataLayer'?'&l='+l:'';j.async=true;j.src='https://www.googletagmanager.com/gtm.js?id='+i+dl;f.parentNode.insertBefore(j,f);})(window,document,'script','dataLayer','GTM-K279D39R'); Browse Preprints In Review Journals COVID-19 Preprints AJE Video Bytes Research Tools Research Promotion AJE Professional Editing AJE Rubriq About Preprint Platform In Review Editorial Policies Our Team Advisory Board Help Center Sign In Submit a Preprint Cite Share Download PDF Article Coronin1C SUMOylation modulates filopodia formation, neuritogenesis, and neuronal differentiation Ram Mishra This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-7742445/v1 This work is licensed under a CC BY 4.0 License Status: Under Review Version 1 posted You are reading this latest preprint version Abstract Actin dynamics in the cytosol and at the cell periphery are critical for metabolic processes and the formation of cellular projections. Coronin1C, a versatile cytoskeletal regulator, is an actin-binding protein that associates with actin at the leading edge. The effects of Coronin1C interactions on actin dynamics enable actin-mediated filopodia and neurite formation. Here, we report that Coronin1C is SUMOylated, but preferentially by SUMO1 at multiple lysine residues in its C-terminus. SUMOylation of Coronin1C impacts filopodia formation in cells; thus, cellular migration is significantly impaired when all five SUMOylatable residues are mutated. Further, we observe that Coronin1C SUMOylation is critically required for efficient neurite formation and extensive cellular projections during neuronal differentiation. Moreover, the non-SUMOylatable Coronin1C mutant forms cytoplasmic aggregates under neuronal differentiation conditions, a hallmark of neurodegenerative diseases. In conclusion, we report that Coronin1C is SUMOylated in its carboxy-terminus and COR1C SUMOylation is critical for cellular projections formation and neuronal differentiation. Biological sciences/Cell biology/Post-translational modifications/Sumoylation Biological sciences/Cell biology/Cytoskeleton/Actin Full Text Additional Declarations There is NO Competing Interest. Supplementary Files supplementaryinformation29925.pdf Supplementary information file RS1203.pdf Reporting Summary Cite Share Download PDF Status: Under Review Version 1 posted You are reading this latest preprint version Research Square lets you share your work early, gain feedback from the community, and start making changes to your manuscript prior to peer review in a journal. As a division of Research Square Company, we’re committed to making research communication faster, fairer, and more useful. We do this by developing innovative software and high quality services for the global research community. Our growing team is made up of researchers and industry professionals working together to solve the most critical problems facing scientific publishing. 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