{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chung JM"],"funding":["National Institutes of Health Grants","NHLBI NIH HHS","National Research Foundation of Korea (NRF) grant funded by the Korea government (MSIT)","Korea government"],"pagination":["843"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9224989"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(6)"],"pubmed_abstract":["Fascin, a major actin cross-linking protein, is expressed in most vertebrate epithelial tissues. It organizes actin filaments into well-ordered bundles that are responsible for the extension of dynamic membrane protrusions, including microspikes, filopodia, and invadopodia from cell surfaces, which are involved in cell migration and invasion as critical components of cancer metastasis. However, it is not well-understood how fascin-1 induces actin binding/bundling and where fascin-1 localizes along the actin filaments, thus facilitating actin bundle formation. In the present study, we attempted to clarify these problems by using biochemical and electron microscopic analyses using various fascin-1 constructs. Three dimensional structures of actin/fascin-1 complex were obtained by electron mi"],"journal":["Life (Basel, Switzerland)"],"pubmed_title":["Structural Analysis of Human Fascin-1: Essential Protein for Actin Filaments Bundling."],"pmcid":["PMC9224989"],"funding_grant_id":["NRF-2022R1C1C1003352","2021R1A2C1009404","DC006103, AR048526, AR048898, HL073050 to M.I.","HL073050","DC006103","2021R1A2C1009404 to H.S.J","AR048526","R01 HL142853","NRF-2022R1C1C1003352 to J.M.C","AR048898"],"pubmed_authors":["Chung JM","Lee S","Ikebe R","Jung HS","Sato O","Ikebe M"],"additional_accession":[]},"is_claimable":false,"name":"Structural Analysis of Human Fascin-1: Essential Protein for Actin Filaments Bundling.","description":"Fascin, a major actin cross-linking protein, is expressed in most vertebrate epithelial tissues. It organizes actin filaments into well-ordered bundles that are responsible for the extension of dynamic membrane protrusions, including microspikes, filopodia, and invadopodia from cell surfaces, which are involved in cell migration and invasion as critical components of cancer metastasis. However, it is not well-understood how fascin-1 induces actin binding/bundling and where fascin-1 localizes along the actin filaments, thus facilitating actin bundle formation. In the present study, we attempted to clarify these problems by using biochemical and electron microscopic analyses using various fascin-1 constructs. Three dimensional structures of actin/fascin-1 complex were obtained by electron mi","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jun","modification":"2026-05-06T03:09:13.514Z","creation":"2025-05-18T12:05:08.659Z"},"accession":"S-EPMC9224989","cross_references":{"pubmed":["35743874"],"doi":["10.3390/life12060843"]}}