{"doi":"10.1002/1873-3468.14750","title":"Scaffold, mechanics and functions of nuclear lamins","abstract":"<jats:p>Nuclear lamins are type‐V intermediate filaments that are involved in many nuclear processes. In mammals, A‐ and B‐type lamins assemble into separate physical meshwork underneath the inner nuclear membrane, the nuclear lamina, with some residual fraction localized within the nucleoplasm. Lamins are the major part of the nucleoskeleton, providing mechanical strength and flexibility to protect the genome and allow nuclear deformability, while also contributing to gene regulation <jats:italic>via</jats:italic> interactions with chromatin. While lamins are the evolutionary ancestors of all intermediate filament family proteins, their ultimate filamentous assembly is markedly different from their cytoplasmic counterparts. Interestingly, hundreds of genetic mutations in the lamina proteins have been causally linked with a broad range of human pathologies, termed laminopathies. These include muscular, neurological and metabolic disorders, as well as premature aging diseases. Recent technological advances have contributed to resolving the filamentous structure of lamins and the corresponding lamina organization. In this review, we revisit the multiscale lamin organization and discuss its implications on nuclear mechanics and chromatin organization within lamina‐associated domains.</jats:p>","journal":"FEBS Letters","year":2023,"id":600235,"datarank":0.5533319181170905,"base_score":3.6888794541139363,"endowment":3.6888794541139363,"self_citation_contribution":0.5533319181170905,"citation_network_contribution":0.0,"self_endowment_contribution":0.5533319181170905,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":39,"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":563344,"name":"Rafael Kronenberg‐Tenga","orcid":"0000-0003-4774-7462","position":1,"is_corresponding":false},{"id":1538683,"name":"Sarka Salajkova","orcid":null,"position":2,"is_corresponding":false},{"id":1538684,"name":"Nili Avidan","orcid":null,"position":3,"is_corresponding":false},{"id":1538685,"name":"Hen Shahak","orcid":null,"position":4,"is_corresponding":false},{"id":1538686,"name":"Alice Thurston","orcid":null,"position":5,"is_corresponding":false},{"id":563348,"name":"Ohad Medalia","orcid":"0000-0003-0994-2937","position":6,"is_corresponding":false},{"id":1538682,"name":"Amnon Buxboim","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Scaffold, mechanics and functions of nuclear lamins","abstract":"<jats:p>Nuclear lamins are type‐V intermediate filaments that are involved in many nuclear processes. In mammals, A‐ and B‐type lamins assemble into separate physical meshwork underneath the inner nuclear membrane, the nuclear lamina, with some residual fraction localized within the nucleoplasm. Lamins are the major part of the nucleoskeleton, providing mechanical strength and flexibility to protect the genome and allow nuclear deformability, while also contributing to gene regulation <jats:italic>via</jats:italic> interactions with chromatin. While lamins are the evolutionary ancestors of all intermediate filament family proteins, their ultimate filamentous assembly is markedly different from their cytoplasmic counterparts. Interestingly, hundreds of genetic mutations in the lamina proteins have been causally linked with a broad range of human pathologies, termed laminopathies. These include muscular, neurological and metabolic disorders, as well as premature aging diseases. Recent technological advances have contributed to resolving the filamentous structure of lamins and the corresponding lamina organization. In this review, we revisit the multiscale lamin organization and discuss its implications on nuclear mechanics and chromatin organization within lamina‐associated domains.</jats:p>","is_dataset_classified":null,"base_score":3.6888794541139363,"endowment":3.6888794541139363,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"37813648","pmcid":null,"openalex_id":"https://openalex.org/W4387442799","authors":[],"funders":[{"funder_name":"Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung","grant_id":"310030_207453","title":null},{"funder_name":"Swiss National Science Foundation","grant_id":"207453","title":"Nuclear lamins: modulations, structural and functional studies"},{"funder_name":"BIRAX Regenerative Medicine Initiative","grant_id":"","title":null}],"total_grants":3,"fwci":3.68,"citation_percentile":0.94656732,"influential_citations":0,"citation_trend":[{"year":2023,"count":1},{"year":2024,"count":16},{"year":2025,"count":15},{"year":2026,"count":7}],"oa_status":"bronze","license":"Wiley Online Library User Agreement","oa_locations":[{"url":"https://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/1873-3468.14750","host_type":"journal"},{"url":"https://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/1873-3468.14750","host_type":"publisher"},{"url":"https://febs.onlinelibrary.wiley.com/doi/pdf/10.1002/1873-3468.14750","host_type":"publisher"},{"url":"https://doi.org/10.1002/1873-3468.14750","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/37813648","host_type":"repository"},{"url":"https://dx.doi.org/10.5167/uzh-252076","host_type":""},{"url":"https://www.zora.uzh.ch/id/eprint/252076/","host_type":""},{"url":"https://doi.org/10.5167/uzh-252076","host_type":""}],"fields_of_study":["Nuclear Structure and Function","Structural Analysis and Optimization","RNA Interference and Gene Delivery","0301 basic medicine","03 medical and health sciences"],"mesh_terms":["Animals","Cell Nucleus","Chromatin","Humans","Intermediate Filaments","Mammals","Nuclear Envelope","Nuclear Lamina","Lamins"],"keywords":["Lamin","Scaffold","Cell biology","Computer science","Biology","Programming language","Nucleus","Nuclear lamina","Intermediate filaments","Progeria","Mechanobiology","Lamins","Cell Nucleus","Mammals","1303 Biochemistry","Nuclear Envelope","610 Medicine & health","Chromatin","1307 Cell Biology","1315 Structural Biology","1311 Genetics","10019 Department of Biochemistry","1312 Molecular Biology","Animals","Humans","570 Life sciences; biology","610 Medicine &amp; health","1304 Biophysics"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-29T12:34:05.438447Z","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":[]}