[{"ddc":["570"],"citation":{"ieee":"F. Fäßler, M. Javoor, and F. K. Schur, “Deciphering the molecular mechanisms of actin cytoskeleton regulation in cell migration using cryo-EM,” <i>Biochemical Society Transactions</i>, vol. 51, no. 1. Portland Press, pp. 87–99, 2023.","apa":"Fäßler, F., Javoor, M., &#38; Schur, F. K. (2023). Deciphering the molecular mechanisms of actin cytoskeleton regulation in cell migration using cryo-EM. <i>Biochemical Society Transactions</i>. Portland Press. <a href=\"https://doi.org/10.1042/bst20220221\">https://doi.org/10.1042/bst20220221</a>","ama":"Fäßler F, Javoor M, Schur FK. Deciphering the molecular mechanisms of actin cytoskeleton regulation in cell migration using cryo-EM. <i>Biochemical Society Transactions</i>. 2023;51(1):87-99. doi:<a href=\"https://doi.org/10.1042/bst20220221\">10.1042/bst20220221</a>","mla":"Fäßler, Florian, et al. “Deciphering the Molecular Mechanisms of Actin Cytoskeleton Regulation in Cell Migration Using Cryo-EM.” <i>Biochemical Society Transactions</i>, vol. 51, no. 1, Portland Press, 2023, pp. 87–99, doi:<a href=\"https://doi.org/10.1042/bst20220221\">10.1042/bst20220221</a>.","chicago":"Fäßler, Florian, Manjunath Javoor, and Florian KM Schur. “Deciphering the Molecular Mechanisms of Actin Cytoskeleton Regulation in Cell Migration Using Cryo-EM.” <i>Biochemical Society Transactions</i>. Portland Press, 2023. <a href=\"https://doi.org/10.1042/bst20220221\">https://doi.org/10.1042/bst20220221</a>.","ista":"Fäßler F, Javoor M, Schur FK. 2023. Deciphering the molecular mechanisms of actin cytoskeleton regulation in cell migration using cryo-EM. Biochemical Society Transactions. 51(1), 87–99.","short":"F. Fäßler, M. Javoor, F.K. Schur, Biochemical Society Transactions 51 (2023) 87–99."},"page":"87-99","publication":"Biochemical Society Transactions","status":"public","publisher":"Portland Press","file":[{"file_name":"2023_BioChemicalSocietyTransactions_Faessler.pdf","creator":"dernst","file_id":"12728","relation":"main_file","date_updated":"2023-03-16T07:58:16Z","access_level":"open_access","date_created":"2023-03-16T07:58:16Z","success":1,"checksum":"4e7069845e3dad22bb44fb71ec624c60","content_type":"application/pdf","file_size":10045006}],"scopus_import":"1","has_accepted_license":"1","date_updated":"2025-04-23T08:47:15Z","author":[{"last_name":"Fäßler","first_name":"Florian","full_name":"Fäßler, Florian","orcid":"0000-0001-7149-769X","id":"404F5528-F248-11E8-B48F-1D18A9856A87"},{"id":"305ab18b-dc7d-11ea-9b2f-b58195228ea2","full_name":"Javoor, Manjunath","last_name":"Javoor","first_name":"Manjunath"},{"last_name":"Schur","first_name":"Florian KM","full_name":"Schur, Florian KM","id":"48AD8942-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-4790-8078"}],"year":"2023","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"oa":1,"article_type":"original","quality_controlled":"1","issue":"1","volume":51,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","day":"01","pmid":1,"intvolume":"        51","publication_status":"published","language":[{"iso":"eng"}],"date_published":"2023-02-01T00:00:00Z","keyword":["Biochemistry"],"isi":1,"_id":"12421","acknowledgement":"We apologize for not being able to mention and cite additional excellent work that would have fit the scope of this review, due to space restraints. We thank Jesse Hansen for comments on the manuscript. We acknowledge support from the Austrian Science Fund (FWF): P33367 and the Institute of Science and Technology Austria.","corr_author":"1","publication_identifier":{"eissn":["1470-8752"],"issn":["0300-5127"]},"external_id":{"isi":["000926043100001"],"pmid":["36695514"]},"project":[{"_id":"9B954C5C-BA93-11EA-9121-9846C619BF3A","name":"Structure and isoform diversity of the Arp2/3 complex","grant_number":"P33367"}],"month":"02","file_date_updated":"2023-03-16T07:58:16Z","type":"journal_article","abstract":[{"lang":"eng","text":"The actin cytoskeleton plays a key role in cell migration and cellular morphodynamics in most eukaryotes. The ability of the actin cytoskeleton to assemble and disassemble in a spatiotemporally controlled manner allows it to form higher-order structures, which can generate forces required for a cell to explore and navigate through its environment. It is regulated not only via a complex synergistic and competitive interplay between actin-binding proteins (ABP), but also by filament biochemistry and filament geometry. The lack of structural insights into how geometry and ABPs regulate the actin cytoskeleton limits our understanding of the molecular mechanisms that define actin cytoskeleton remodeling and, in turn, impact emerging cell migration characteristics. With the advent of cryo-electron microscopy (cryo-EM) and advanced computational methods, it is now possible to define these molecular mechanisms involving actin and its interactors at both atomic and ultra-structural levels in vitro and in cellulo. In this review, we will provide an overview of the available cryo-EM methods, applicable to further our understanding of the actin cytoskeleton, specifically in the context of cell migration. We will discuss how these methods have been employed to elucidate ABP- and geometry-defined regulatory mechanisms in initiating, maintaining, and disassembling cellular actin networks in migratory protrusions."}],"doi":"10.1042/bst20220221","license":"https://creativecommons.org/licenses/by/4.0/","date_created":"2023-01-27T10:08:19Z","oa_version":"Published Version","article_processing_charge":"No","title":"Deciphering the molecular mechanisms of actin cytoskeleton regulation in cell migration using cryo-EM","department":[{"_id":"FlSc"}]},{"department":[{"_id":"JiFr"}],"title":"Rho-GTPase-regulated vesicle trafficking in plant cell polarity","doi":"10.1042/BST20130269","date_created":"2018-12-11T11:54:41Z","oa_version":"None","article_processing_charge":"No","type":"journal_article","month":"02","abstract":[{"text":"ROPs (Rho of plants) belong to a large family of plant-specific Rho-like small GTPases that function as essential molecular switches to control diverse cellular processes including cytoskeleton organization, cell polarization, cytokinesis, cell differentiation and vesicle trafficking. Although the machineries of vesicle trafficking and cell polarity in plants have been individually well addressed, how ROPs co-ordinate those processes is still largely unclear. Recent progress has been made towards an understanding of the coordination of ROP signalling and trafficking of PIN (PINFORMED) transporters for the plant hormone auxin in both root and leaf pavement cells. PIN transporters constantly shuttle between the endosomal compartments and the polar plasma membrane domains, therefore the modulation of PIN-dependent auxin transport between cells is a main developmental output of ROP-regulated vesicle trafficking. The present review focuses on these cellular mechanisms, especially the integration of ROP-based vesicle trafficking and plant cell polarity.","lang":"eng"}],"external_id":{"isi":["000333444400034"],"pmid":["24450654"]},"project":[{"_id":"25716A02-B435-11E9-9278-68D0E5697425","name":"Polarity and subcellular dynamics in plants","grant_number":"282300","call_identifier":"FP7"}],"publication_identifier":{"eissn":["1470-8752"],"issn":["0300-5127"]},"acknowledgement":"This work was supported by the European Research Council [project ERC-2011-StG-20101109-PSDP], Central European Institute of Technology (CEITEC) [grant number CZ.1.05/1.1.00/02.0068], European Social Fund [grant number CZ.1.07/2.3.00/20.0043] and the Czec","corr_author":"1","_id":"1915","isi":1,"date_published":"2014-02-01T00:00:00Z","language":[{"iso":"eng"}],"intvolume":"        42","publication_status":"published","pmid":1,"publist_id":"5179","day":"01","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","volume":42,"issue":"1","article_type":"original","quality_controlled":"1","author":[{"full_name":"Chen, Xu","last_name":"Chen","first_name":"Xu","id":"4E5ADCAA-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Friml, Jirí","last_name":"Friml","first_name":"Jirí","orcid":"0000-0002-8302-7596","id":"4159519E-F248-11E8-B48F-1D18A9856A87"}],"year":"2014","date_updated":"2025-09-29T12:22:54Z","publisher":"Portland Press","scopus_import":"1","ec_funded":1,"status":"public","publication":"Biochemical Society Transactions","citation":{"short":"X. Chen, J. Friml, Biochemical Society Transactions 42 (2014) 212–218.","ista":"Chen X, Friml J. 2014. Rho-GTPase-regulated vesicle trafficking in plant cell polarity. Biochemical Society Transactions. 42(1), 212–218.","chicago":"Chen, Xu, and Jiří Friml. “Rho-GTPase-Regulated Vesicle Trafficking in Plant Cell Polarity.” <i>Biochemical Society Transactions</i>. Portland Press, 2014. <a href=\"https://doi.org/10.1042/BST20130269\">https://doi.org/10.1042/BST20130269</a>.","mla":"Chen, Xu, and Jiří Friml. “Rho-GTPase-Regulated Vesicle Trafficking in Plant Cell Polarity.” <i>Biochemical Society Transactions</i>, vol. 42, no. 1, Portland Press, 2014, pp. 212–18, doi:<a href=\"https://doi.org/10.1042/BST20130269\">10.1042/BST20130269</a>.","ieee":"X. Chen and J. Friml, “Rho-GTPase-regulated vesicle trafficking in plant cell polarity,” <i>Biochemical Society Transactions</i>, vol. 42, no. 1. Portland Press, pp. 212–218, 2014.","apa":"Chen, X., &#38; Friml, J. (2014). Rho-GTPase-regulated vesicle trafficking in plant cell polarity. <i>Biochemical Society Transactions</i>. Portland Press. <a href=\"https://doi.org/10.1042/BST20130269\">https://doi.org/10.1042/BST20130269</a>","ama":"Chen X, Friml J. Rho-GTPase-regulated vesicle trafficking in plant cell polarity. <i>Biochemical Society Transactions</i>. 2014;42(1):212-218. doi:<a href=\"https://doi.org/10.1042/BST20130269\">10.1042/BST20130269</a>"},"page":"212 - 218"}]