دورية أكاديمية
Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension
العنوان: | Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension |
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المؤلفون: | Biancospino M., Buel G. R., Nino C. A., Maspero E., di Perrotolo R. S., Raimondi A., Redlingshofer L., Weber J., Brodsky F. M., Walters K. J., Polo S. |
المساهمون: | M. Biancospino, G.R. Buel, C.A. Nino, E. Maspero, R.S. di Perrotolo, A. Raimondi, L. Redlingshofer, J. Weber, F.M. Brodsky, K.J. Walter, S. Polo |
بيانات النشر: | Nature Publishing Group |
سنة النشر: | 2019 |
المجموعة: | The University of Milan: Archivio Istituzionale della Ricerca (AIR) |
مصطلحات موضوعية: | Actin, Adaptor Proteins, Signal Transducing, Caco-2 Cell, Cell Culture Technique, Clathrin Light Chain, Clathrin-Coated Vesicle, Coated Pits, Cell-Membrane, Cyst, Endocytosi, Human, Magnetic Resonance Spectroscopy, Microfilament Protein, Myosin Heavy Chain, Protein Binding, Protein Conformation, Protein Isoforms, Settore MED/04 - Patologia Generale |
الوصف: | Clathrin light chains (CLCa and CLCb) are major constituents of clathrin-coated vesicles. Unique functions for these evolutionary conserved paralogs remain elusive, and their role in clathrin-mediated endocytosis in mammalian cells is debated. Here, we find and structurally characterize a direct and selective interaction between CLCa and the long isoform of the actin motor protein myosin VI, which is expressed exclusively in highly polarized tissues. Using genetically-reconstituted Caco-2 cysts as proxy for polarized epithelia, we provide evidence for coordinated action of myosin VI and CLCa at the apical surface where these proteins are essential for fission of clathrin-coated pits. We further find that myosin VI and Huntingtin-interacting protein 1-related protein (Hip1R) are mutually exclusive interactors with CLCa, and suggest a model for the sequential function of myosin VI and Hip1R in actin-mediated clathrin-coated vesicle budding. |
نوع الوثيقة: | article in journal/newspaper |
اللغة: | English |
العلاقة: | info:eu-repo/semantics/altIdentifier/pmid/31672988; info:eu-repo/semantics/altIdentifier/wos/WOS:000493438700022; volume:10; issue:1; numberofpages:15; journal:NATURE COMMUNICATIONS; http://hdl.handle.net/2434/801707Test; info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85074249548 |
DOI: | 10.1038/s41467-019-12855-6 |
الإتاحة: | https://doi.org/10.1038/s41467-019-12855-6Test http://hdl.handle.net/2434/801707Test |
حقوق: | info:eu-repo/semantics/openAccess |
رقم الانضمام: | edsbas.DA76C352 |
قاعدة البيانات: | BASE |
DOI: | 10.1038/s41467-019-12855-6 |
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