Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/137135
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dc.contributor.authorMiao, Yansongen_US
dc.contributor.authorTipakornsaowapak, Teepiyanuten_US
dc.contributor.authorZheng, Liangzhenen_US
dc.contributor.authorMu, Yuguangen_US
dc.contributor.authorLewellyn, Ericen_US
dc.date.accessioned2020-03-02T03:47:57Z-
dc.date.available2020-03-02T03:47:57Z-
dc.date.issued2018-
dc.identifier.citationMiao, Y., Tipakornsaowapak, T., Zheng, L., Mu, Y., & Lewellyn, E. (2018). Phospho‐regulation of intrinsically disordered proteins for actin assembly and endocytosis. The FEBS journal, 285(15), 2762-2784. doi:10.1111/febs.14493en_US
dc.identifier.issn1742-464Xen_US
dc.identifier.urihttps://hdl.handle.net/10356/137135-
dc.description.abstractActin filament assembly contributes to the endocytic pathway pleiotropically, with active roles in clathrin‐dependent and clathrin‐independent endocytosis as well as subsequent endosomal trafficking. Endocytosis comprises a series of dynamic events, including the initiation of membrane curvature, bud invagination, vesicle abscission and subsequent vesicular transport. The ultimate success of endocytosis requires the coordinated activities of proteins that trigger actin polymerization, recruit actin‐binding proteins (ABPs) and organize endocytic proteins (EPs) that promote membrane curvature through molecular crowding or scaffolding mechanisms. A particularly interesting phenomenon is that multiple EPs and ABPs contain a substantial percentage of intrinsically disordered regions (IDRs), which can contribute to protein coacervation and phase separation. In addition, intrinsically disordered proteins (IDPs) frequently contain sites for post‐translational modifications (PTMs) such as phosphorylation, and these modifications exhibit a high preference for IDR residues [Groban ES et al. (2006) PLoS Comput Biol 2, e32]. PTMs are implicated in regulating protein function by modulating the protein conformation, protein–protein interactions and the transition between order and disorder states of IDPs. The molecular mechanisms by which IDRs of ABPs and EPs fine‐tune actin assembly and endocytosis remain mostly unexplored and elusive. In this review, we analyze protein sequences of budding yeast EPs and ABPs, and discuss the potential underlying mechanisms for regulating endocytosis and actin assembly through the emerging concept of IDR‐mediated protein multivalency, coacervation, and phase transition, with an emphasis on the phospho‐regulation of IDRs. Finally, we summarize the current understanding of how these mechanisms coordinate actin cytoskeleton assembly and membrane curvature formation during endocytosis in budding yeast.en_US
dc.description.sponsorshipMOE (Min. of Education, S’pore)en_US
dc.language.isoenen_US
dc.relation.ispartofThe FEBS journalen_US
dc.rights© 2018 The Author(s). All rights reserved. This is the accepted version of the following article: Miao, Y., Tipakornsaowapak, T., Zheng, L., Mu, Y., & Lewellyn, E. (2018). Phospho‐regulation of intrinsically disordered proteins for actin assembly and endocytosis. The FEBS journal, 285(15), 2762-2784. doi:10.1111/febs.14493, which has been published in final form at https://doi.org/10.1111/febs.14493en_US
dc.subjectScience::Biological sciencesen_US
dc.titlePhospho‐regulation of intrinsically disordered proteins for actin assembly and endocytosisen_US
dc.typeJournal Articleen
dc.contributor.schoolSchool of Chemical and Biomedical Engineeringen_US
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doi10.1111/febs.14493-
dc.description.versionAccepted versionen_US
dc.identifier.pmid29722136-
dc.identifier.scopus2-s2.0-85051111352-
dc.identifier.issue15en_US
dc.identifier.volume285en_US
dc.identifier.spage2762en_US
dc.identifier.epage2784en_US
dc.subject.keywordsActin Cytoskeletonen_US
dc.subject.keywordsEndocytosisen_US
item.fulltextWith Fulltext-
item.grantfulltextopen-
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