{"doi":"10.1091/mbc.e14-04-0863","title":"Induction of focal adhesions and motility in\n                    <i>Drosophila</i>\n                    S2 cells","abstract":"<jats:p>Focal adhesions are dynamic structures that interact with the extracellular matrix on the cell exterior and actin filaments on the cell interior, enabling cells to adhere and crawl along surfaces. We describe a system for inducing the formation of focal adhesions in normally non–ECM-adherent, nonmotile Drosophila S2 cells. These focal adhesions contain the expected molecular markers such as talin, vinculin, and p130Cas, and they require talin for their formation. The S2 cells with induced focal adhesions also display a nonpolarized form of motility on vitronectin-coated substrates. Consistent with findings in mammalian cells, the degree of motility can be tuned by changing the stiffness of the substrate and was increased after the depletion of PAK3, a p21-activated kinase. A subset of nonmotile, nonpolarized cells also exhibited focal adhesions that rapidly assembled and disassembled around the cell perimeter. Such cooperative and dynamic fluctuations of focal adhesions were decreased by RNA interference (RNAi) depletion of myosin II and focal adhesion kinase, suggesting that this behavior requires force and focal adhesion maturation. These results demonstrate that S2 cells, a cell line that is well studied for cytoskeletal dynamics and readily amenable to protein manipulation by RNAi, can be used to study the assembly and dynamics of focal adhesions and mechanosensitive cell motility.</jats:p>","journal":"Molecular Biology of the Cell","year":2014,"id":664643,"datarank":0.42498200160843247,"base_score":2.833213344056216,"endowment":2.833213344056216,"self_citation_contribution":0.42498200160843247,"citation_network_contribution":0.0,"self_endowment_contribution":0.42498200160843247,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":16,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1735464,"name":"Michael V. D'Ambrosio","orcid":null,"position":1,"is_corresponding":false},{"id":12021,"name":"Ronald D. Vale","orcid":"0000-0003-3460-2758","position":2,"is_corresponding":false},{"id":289554,"name":"Susana A. Ribeiro","orcid":"0000-0003-3807-7540","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Induction of focal adhesions and motility in\n                    <i>Drosophila</i>\n                    S2 cells","abstract":"<jats:p>Focal adhesions are dynamic structures that interact with the extracellular matrix on the cell exterior and actin filaments on the cell interior, enabling cells to adhere and crawl along surfaces. We describe a system for inducing the formation of focal adhesions in normally non–ECM-adherent, nonmotile Drosophila S2 cells. These focal adhesions contain the expected molecular markers such as talin, vinculin, and p130Cas, and they require talin for their formation. The S2 cells with induced focal adhesions also display a nonpolarized form of motility on vitronectin-coated substrates. Consistent with findings in mammalian cells, the degree of motility can be tuned by changing the stiffness of the substrate and was increased after the depletion of PAK3, a p21-activated kinase. A subset of nonmotile, nonpolarized cells also exhibited focal adhesions that rapidly assembled and disassembled around the cell perimeter. Such cooperative and dynamic fluctuations of focal adhesions were decreased by RNA interference (RNAi) depletion of myosin II and focal adhesion kinase, suggesting that this behavior requires force and focal adhesion maturation. These results demonstrate that S2 cells, a cell line that is well studied for cytoskeletal dynamics and readily amenable to protein manipulation by RNAi, can be used to study the assembly and dynamics of focal adhesions and mechanosensitive cell motility.</jats:p>","is_dataset_classified":null,"base_score":2.833213344056216,"endowment":2.833213344056216,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"25273555","pmcid":"PMC4244196","openalex_id":"https://openalex.org/W2153280008","authors":[],"funders":[{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM097312","title":null},{"funder_name":"National Institutes of Health","grant_id":"1R01GM097312-01","title":"Structure and mechanism of the dynein motor"}],"total_grants":2,"fwci":0.703,"citation_percentile":0.67259835,"influential_citations":0,"citation_trend":[{"year":2015,"count":3},{"year":2017,"count":2},{"year":2019,"count":4},{"year":2020,"count":2},{"year":2022,"count":2},{"year":2025,"count":2},{"year":2026,"count":1}],"oa_status":"closed","license":"CC BY NC SA","oa_locations":[{"url":"https://doi.org/10.1091/mbc.e14-04-0863","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/25273555","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/4244196","host_type":"repository"},{"url":"https://escholarship.org/uc/item/6mh8b51z","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC4244196","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC4244196?pdf=render","host_type":"Europe_PMC"},{"url":"http://dx.doi.org/10.1091/mbc.E14-04-0863","host_type":""},{"url":"https://dx.doi.org/10.1091/mbc.e14-04-0863","host_type":""},{"url":"https://doi.org/https://doi.org/10.1091/mbc.e14-04-0863","host_type":""}],"fields_of_study":["Cellular Mechanics and Interactions","Silk-based biomaterials and applications","Force Microscopy Techniques and Applications","0301 basic medicine","03 medical and health sciences","0303 health sciences"],"mesh_terms":["Animals","Cell Adhesion","Cell Line","Cell Movement","Cytoskeletal Proteins","Drosophila melanogaster","Microscopy, Fluorescence","Vitronectin","Focal Adhesions","Myosin Type II","Drosophila Proteins","RNA Interference","Integrin alpha Chains","Mechanotransduction, Cellular","Green Fluorescent Proteins","Crk-Associated Substrate Protein","Focal Adhesion Protein-Tyrosine Kinases","p21-Activated Kinases","Time-Lapse Imaging"],"keywords":["Focal adhesion","Cell biology","Vinculin","PTK2","Biology","Paxillin","Motility","Extracellular matrix","Cytoskeleton","Actin","Vitronectin","Cell","Fibronectin","Kinase","Protein kinase A","Signal transduction","Biochemistry","570","Mechanotransduction","Green Fluorescent Proteins","Medical and Health Sciences","Mechanotransduction, Cellular","Time-Lapse Imaging","Fluorescence","Cell Line","Cell Movement","Genetics","Cell Adhesion","Animals","Drosophila Proteins","Myosin Type II","Microscopy","Focal Adhesions","Articles","Biological Sciences","Cytoskeletal Proteins","Crk-Associated Substrate Protein","Drosophila melanogaster","Microscopy, Fluorescence","p21-Activated Kinases","Biochemistry and cell biology","Focal Adhesion Protein-Tyrosine Kinases","RNA Interference","Generic health relevance","Cellular","Integrin alpha Chains","Biotechnology","Developmental Biology"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-13T03:38:30.949141Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}