{"doi":"10.1091/mbc.e13-11-0644","title":"Concentration-dependent lamin assembly and its roles in the localization of other nuclear proteins","abstract":"<jats:p>The nuclear lamina (NL) consists of lamin polymers and proteins that bind to the polymers. Disruption of NL proteins such as lamin and emerin leads to developmental defects and human diseases. However, the expression of multiple lamins, including lamin-A/C, lamin-B1, and lamin-B2, in mammals has made it difficult to study the assembly and function of the NL. Consequently, it has been unclear whether different lamins depend on one another for proper NL assembly and which NL functions are shared by all lamins or are specific to one lamin. Using mouse cells deleted of all or different combinations of lamins, we demonstrate that the assembly of each lamin into the NL depends primarily on the lamin concentration present in the nucleus. When expressed at sufficiently high levels, each lamin alone can assemble into an evenly organized NL, which is in turn sufficient to ensure the even distribution of the nuclear pore complexes. By contrast, only lamin-A can ensure the localization of emerin within the NL. Thus, when investigating the role of the NL in development and disease, it is critical to determine the protein levels of relevant lamins and the intricate shared or specific lamin functions in the tissue of interest.</jats:p>","journal":"Molecular Biology of the Cell","year":2014,"id":649033,"datarank":0.6628260911694899,"base_score":4.418840607796598,"endowment":4.418840607796598,"self_citation_contribution":0.6628260911694899,"citation_network_contribution":0.0,"self_endowment_contribution":0.6628260911694899,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":82,"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":1546814,"name":"Youngjo Kim","orcid":null,"position":1,"is_corresponding":false},{"id":451243,"name":"Takeshi Shimi","orcid":"0000-0002-9864-1820","position":2,"is_corresponding":false},{"id":293964,"name":"Robert D. Goldman","orcid":"0000-0003-0383-1435","position":3,"is_corresponding":false},{"id":816085,"name":"Yixian Zheng","orcid":"0000-0002-1992-4014","position":4,"is_corresponding":false},{"id":1211210,"name":"Yuxuan Guo","orcid":"0000-0001-7582-4555","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Concentration-dependent lamin assembly and its roles in the localization of other nuclear proteins","abstract":"<jats:p>The nuclear lamina (NL) consists of lamin polymers and proteins that bind to the polymers. Disruption of NL proteins such as lamin and emerin leads to developmental defects and human diseases. However, the expression of multiple lamins, including lamin-A/C, lamin-B1, and lamin-B2, in mammals has made it difficult to study the assembly and function of the NL. Consequently, it has been unclear whether different lamins depend on one another for proper NL assembly and which NL functions are shared by all lamins or are specific to one lamin. Using mouse cells deleted of all or different combinations of lamins, we demonstrate that the assembly of each lamin into the NL depends primarily on the lamin concentration present in the nucleus. When expressed at sufficiently high levels, each lamin alone can assemble into an evenly organized NL, which is in turn sufficient to ensure the even distribution of the nuclear pore complexes. By contrast, only lamin-A can ensure the localization of emerin within the NL. Thus, when investigating the role of the NL in development and disease, it is critical to determine the protein levels of relevant lamins and the intricate shared or specific lamin functions in the tissue of interest.</jats:p>","is_dataset_classified":null,"base_score":4.418840607796598,"endowment":4.418840607796598,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"24523288","pmcid":"PMC3982994","openalex_id":"https://openalex.org/W2103609151","authors":[],"funders":[{"funder_name":"NIGMS NIH HHS","grant_id":"GM106023","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM056312","title":null},{"funder_name":"NCI NIH HHS","grant_id":"R01 CA031760","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM106023","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"GM056312","title":null},{"funder_name":"NCI NIH HHS","grant_id":"CA031760","title":null},{"funder_name":"National Institutes of Health","grant_id":"5R01GM106023-06","title":"Analysis of lamin-chromatin interactions and their regulation of chromosome organization and gene expression"},{"funder_name":"National Institutes of Health","grant_id":"5R01GM056312-07","title":"Gamma tubulin ring complex in microtubule nucleation"}],"total_grants":8,"fwci":2.8601,"citation_percentile":0.91538087,"influential_citations":0,"citation_trend":[{"year":2014,"count":2},{"year":2015,"count":12},{"year":2016,"count":3},{"year":2017,"count":5},{"year":2018,"count":4},{"year":2019,"count":7},{"year":2020,"count":9},{"year":2021,"count":10},{"year":2022,"count":5},{"year":2023,"count":3},{"year":2024,"count":8},{"year":2025,"count":9},{"year":2026,"count":5}],"oa_status":"closed","license":"CC BY NC SA","oa_locations":[{"url":"https://doi.org/10.1091/mbc.e13-11-0644","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/24523288","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/3982994","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC3982994","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC3982994?pdf=render","host_type":"Europe_PMC"},{"url":"http://dx.doi.org/10.1091/mbc.E13-11-0644","host_type":""},{"url":"https://dx.doi.org/10.1091/mbc.e13-11-0644","host_type":""}],"fields_of_study":["Nuclear Structure and Function","RNA Research and Splicing","Genomics and Chromatin Dynamics","0301 basic medicine","0303 health sciences","03 medical and health sciences","Animals","Cell Differentiation","Cells, Cultured","Embryonic Stem Cells","Lamin Type A","Lamin Type B","Membrane Proteins","Mice","Nuclear Lamina","Nuclear Pore","Nuclear Pore Complex Proteins","Nuclear Proteins","RNA Interference","RNA, Small Interfering"],"mesh_terms":["Animals","Cell Differentiation","Cells, Cultured","Membrane Proteins","Nuclear Proteins","Nuclear Pore","Nuclear Pore Complex Proteins","RNA Interference","RNA, Small Interfering","Nuclear Lamina","Lamin Type A","Lamin Type B","Mice","Embryonic Stem Cells"],"keywords":["Lamin","Nuclear lamina","Biology","Cell biology","Emerin","Nuclear protein","Cell nucleus","Nucleus","Genetics","Gene","Transcription factor","Lamin Type B","Membrane Proteins","Nuclear Proteins","Cell Differentiation","Articles","Lamin Type A","Nuclear Pore Complex Proteins","Mice","Nuclear Pore","Animals","RNA Interference","RNA, Small Interfering","Cells, Cultured","Embryonic Stem Cells"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-10T03:13:48.767859Z","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":[]}