{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Young LE"],"funding":["National Institutes of Health","NIGMS NIH HHS"],"pagination":["jcs220814"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6240302"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["131(21)"],"pubmed_abstract":["Filopodia are actin-dependent finger-like structures that protrude from the plasma membrane. Actin filament barbed-end-binding proteins localized to filopodial tips are key to filopodial assembly. Two classes of barbed-end-binding proteins are formins and Ena/VASP proteins, and both classes have been localized to filopodial tips in specific cellular contexts. Here, we examine the filopodial roles of the FMNL formins and Ena/VASP proteins in U2OS cells. FMNL3 suppression reduces filopodial assembly by 90%, and FMNL3 is enriched at >95% of filopodial tips. Suppression of VASP or Mena (also known as ENAH) reduces filopodial assembly by >75%. However, VASP and Mena do not display consistent filopodial tip localization, but are enriched in focal adhesions (FAs). Interestingly, >85% of FMNL3-containing filopodia are associated with FAs. Two situations increase Ena/VASP filopodial localization: (1) expression of myosin-X, and (2) actively spreading cells. In spreading cells, filopodia often mark sites of nascent adhesions. Interestingly, VASP suppression in spreading cells causes a significant increase in adhesion assembly at filopodial tips. This work demonstrates that, in U2OS cells, Ena/VASP proteins play roles in filopodia beyond those at filopodial tips.This article has an associated First Person interview with the first author of the paper."],"journal":["Journal of cell science"],"pubmed_title":["Roles for Ena/VASP proteins in FMNL3-mediated filopodial assembly."],"pmcid":["PMC6240302"],"funding_grant_id":["R01 GM109965","R35 GM122545","P20 GM113132"],"pubmed_authors":["Young LE","Latario CJ","Higgs HN"],"additional_accession":[]},"is_claimable":false,"name":"Roles for Ena/VASP proteins in FMNL3-mediated filopodial assembly.","description":"Filopodia are actin-dependent finger-like structures that protrude from the plasma membrane. Actin filament barbed-end-binding proteins localized to filopodial tips are key to filopodial assembly. Two classes of barbed-end-binding proteins are formins and Ena/VASP proteins, and both classes have been localized to filopodial tips in specific cellular contexts. Here, we examine the filopodial roles of the FMNL formins and Ena/VASP proteins in U2OS cells. FMNL3 suppression reduces filopodial assembly by 90%, and FMNL3 is enriched at >95% of filopodial tips. Suppression of VASP or Mena (also known as ENAH) reduces filopodial assembly by >75%. However, VASP and Mena do not display consistent filopodial tip localization, but are enriched in focal adhesions (FAs). Interestingly, >85% of FMNL3-containing filopodia are associated with FAs. Two situations increase Ena/VASP filopodial localization: (1) expression of myosin-X, and (2) actively spreading cells. In spreading cells, filopodia often mark sites of nascent adhesions. Interestingly, VASP suppression in spreading cells causes a significant increase in adhesion assembly at filopodial tips. This work demonstrates that, in U2OS cells, Ena/VASP proteins play roles in filopodia beyond those at filopodial tips.This article has an associated First Person interview with the first author of the paper.","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Oct","modification":"2024-11-15T00:26:13.957Z","creation":"2019-11-07T08:02:30Z"},"accession":"S-EPMC6240302","cross_references":{"pubmed":["30373894"],"doi":["10.1242/jcs.220814"]}}