{"doi":"10.1242/jcs.114.6.1137","title":"Distinct roles for dystroglycan, β1 integrin and perlecan in cell surface laminin organization","abstract":"<jats:title>ABSTRACT</jats:title>\n               <jats:p>Dystroglycan (DG) is a cell surface receptor for several extracellular matrix (ECM) molecules including laminins, agrin and perlecan. Recent data indicate that DG function is required for the formation of basement membranes in early development and the organization of laminin on the cell surface. Here we show that DG-mediated laminin clustering on mouse embryonic stem (ES) cells is a dynamic process in which clusters are consolidated over time into increasingly more complex structures. Utilizing various null-mutant ES cell lines, we define roles for other molecules in this process. In β1 integrin-deficient ES cells, laminin-1 binds to the cell surface, but fails to organize into more morphologically complex structures. This result indicates that β1 integrin function is required after DG function in the cell surface-mediated laminin assembly process. In perlecan-deficient ES cells, the formation of complex laminin-1 structures is defective, implicating perlecan in the laminin matrix assembly process. Moreover, laminin and perlecan reciprocally modulate the organization of the other on the cell surface. Taken together, the data support a model whereby DG serves as a receptor essential for the initial binding of laminin on the cell surface, whereas β1 integrins and perlecan are required for laminin matrix assembly processes after it binds to the cell.</jats:p>","journal":"Journal of Cell Science","year":2001,"id":616751,"datarank":0.7465100613630863,"base_score":4.976733742420574,"endowment":4.976733742420574,"self_citation_contribution":0.7465100613630863,"citation_network_contribution":0.0,"self_endowment_contribution":0.7465100613630863,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":144,"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":1590232,"name":"Jakob S. Satz","orcid":null,"position":1,"is_corresponding":false},{"id":492391,"name":"Cord Brakebusch","orcid":"0000-0002-9342-1634","position":2,"is_corresponding":false},{"id":405429,"name":"Mercedes Costell","orcid":"0000-0001-6146-996X","position":3,"is_corresponding":false},{"id":1590235,"name":"Erika Gustafsson","orcid":null,"position":4,"is_corresponding":false},{"id":138705,"name":"Reinhard Fässler","orcid":null,"position":5,"is_corresponding":false},{"id":365964,"name":"Kevin P. Campbell","orcid":"0000-0003-2066-5889","position":6,"is_corresponding":false},{"id":275281,"name":"Michael D. Henry","orcid":"0000-0002-7871-245X","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Distinct roles for dystroglycan, β1 integrin and perlecan in cell surface laminin organization","abstract":"<jats:title>ABSTRACT</jats:title>\n               <jats:p>Dystroglycan (DG) is a cell surface receptor for several extracellular matrix (ECM) molecules including laminins, agrin and perlecan. Recent data indicate that DG function is required for the formation of basement membranes in early development and the organization of laminin on the cell surface. Here we show that DG-mediated laminin clustering on mouse embryonic stem (ES) cells is a dynamic process in which clusters are consolidated over time into increasingly more complex structures. Utilizing various null-mutant ES cell lines, we define roles for other molecules in this process. In β1 integrin-deficient ES cells, laminin-1 binds to the cell surface, but fails to organize into more morphologically complex structures. This result indicates that β1 integrin function is required after DG function in the cell surface-mediated laminin assembly process. In perlecan-deficient ES cells, the formation of complex laminin-1 structures is defective, implicating perlecan in the laminin matrix assembly process. Moreover, laminin and perlecan reciprocally modulate the organization of the other on the cell surface. Taken together, the data support a model whereby DG serves as a receptor essential for the initial binding of laminin on the cell surface, whereas β1 integrins and perlecan are required for laminin matrix assembly processes after it binds to the cell.</jats:p>","is_dataset_classified":null,"base_score":4.976733742420574,"endowment":4.976733742420574,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"11228157","pmcid":null,"openalex_id":"https://openalex.org/W2149811187","authors":[],"funders":[{"funder_name":"NIDDK NIH HHS","grant_id":"DK09712","title":null}],"total_grants":1,"fwci":4.8018,"citation_percentile":0.96438884,"influential_citations":0,"citation_trend":[{"year":2012,"count":8},{"year":2013,"count":8},{"year":2014,"count":7},{"year":2015,"count":5},{"year":2016,"count":2},{"year":2017,"count":1},{"year":2018,"count":1},{"year":2019,"count":4},{"year":2020,"count":2},{"year":2021,"count":1},{"year":2022,"count":4},{"year":2024,"count":3},{"year":2025,"count":2}],"oa_status":"closed","license":"http://www.biologists.com/user-licence-1-1/","oa_locations":[{"url":"https://journals.biologists.com/jcs/article-pdf/114/6/1137/3355186/joces_114_6_1137.pdf","host_type":"publisher"},{"url":"https://doi.org/10.1242/jcs.114.6.1137","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/11228157","host_type":"repository"}],"fields_of_study":["Cell Adhesion Molecules Research","Cellular Mechanics and Interactions","Protease and Inhibitor Mechanisms","Animals","Cell Line","Cell Membrane","Cytoskeletal Proteins","Dystroglycans","Heparan Sulfate Proteoglycans","Humans","Integrin beta1","Laminin","Membrane Glycoproteins","Mice"],"mesh_terms":["Animals","Cell Line","Cell Membrane","Cytoskeletal Proteins","Humans","Laminin","Membrane Glycoproteins","Integrin beta1","Heparan Sulfate Proteoglycans","Dystroglycans","Mice"],"keywords":["Perlecan","Laminin","Dystroglycan","Agrin","Cell biology","Integrin","Biology","Extracellular matrix","Cell surface receptor","Cell","Basement membrane","Receptor","Proteoglycan","Biochemistry","Postsynaptic potential"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-02T23:44:55.475332Z","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":[]}