The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Nuclear lamins: major factors in the structural organization and function of the nucleus and chromatin
Abstract
Over the past few years it has become evident that the intermediate filament proteins, the types A and B nuclear lamins, not only provide a structural framework for the nucleus, but are also essential for many aspects of normal nuclear function. Insights into lamin-related functions have been derived from studies of the remarkably large number of disease-causing mutations in the human lamin A gene. This review provides an up-to-date overview of the functions of nuclear lamins, emphasizing their roles in epigenetics, chromatin organization, DNA replication, transcription, and DNA repair. In addition, we discuss recent evidence supporting the importance of lamins in viral infections.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“In addition to genomic damage affecting nuclear or mtDNA, defects in the nuclear lamina can also cause genome instability (Dechat et al., 2008).”
From The Hallmarks of Aging (2013) · cites this paper as Dechat et al., 2008
Citations
Cites
EZH2 is downstream of the pRB-E2F pathway, essential for proliferation and amplified in cancer.
Bracken, A. P., Pasini, D., Capra, M., Prosperini, E., Colli, E., & Helin, K. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg542 · Cited by 1,196
Dynamic genome architecture in the nuclear space: regulation of gene expression in three dimensions
Lanctôt, C., Cheutin, T., Cremer, M., Cavalli, G., & Cremer, T. (2007) · Nature Reviews Genetics · doi:10.1038/nrg2041 · Cited by 781
Nuclear organization of the genome and the potential for gene regulation
Fraser, P., & Bickmore, W. (2007) · Nature · doi:10.1038/nature05916 · Cited by 734
Genomic instability in laminopathy-based premature aging
Liu, B., Wang, J., Chan, K. M., Tjia, W. M., Deng, W., Guan, X., Huang, J.-D., Li, K. M., Chau, P. Y., Chen, D. J., et al. (2005) · Nature Medicine · doi:10.1038/nm1266 · Cited by 650
Accelerated ageing in mice deficient in Zmpste24 protease is linked to p53 signalling activation
Varela, I., Cadiñanos, J., Pendás, A. M., Gutiérrez-Fernández, A., Folgueras, A. R., Sánchez, L. M., Zhou, Z., Rodríguez, F. J., Stewart, C. L., Vega, J. A., et al. (2005) · Nature · doi:10.1038/nature04019 · Cited by 466
Role of the RB1 family in stabilizing histone methylation at constitutive heterochromatin
Gonzalo, S., García-Cao, M., Fraga, M. F., Schotta, G., Peters, A. H. F. M., Cotter, S. E., Eguía, R., Dean, D. C., Esteller, M., Jenuwein, T., et al. (2005) · Nature Cell Biology · doi:10.1038/ncb1235 · Cited by 343
Werner and Hutchinson–Gilford progeria syndromes: mechanistic basis of human progeroid diseases
Kudlow, B. A., Kennedy, B. K., & Monnat, R. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2161 · Cited by 304
Caron, M., Auclair, M., Donadille, B., Béréziat, V, Guerci, B., Laville, M., Narbonne, H., Bodemer, C., Lascols, O., Capeau, J., et al. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402197 · Cited by 226
Liu, Y., Wang, Y., Rusinol, A. E., Sinensky, M. S., Liu, J., Shell, S. M., & Zou, Y. (2008) · The FASEB Journal · doi:10.1096/fj.07-8598com · Cited by 115
Flagged first, then by citations
Research works printed but not linked: 260
- 10.1073/pnas.72.3.1007 · DOI
- 10.1038/323560a0 · DOI
- Amati,, 2004, Gene expression profiling of fibroblasts from a human progeroid disease (mandibuloacral dysplasia, MAD #248370) through cDNA microarrays, Gene Expr., 12, 39, 10.3727/000000004783992189 · DOI
- 10.1016/j.febslet.2004.05.019 · DOI
- 10.1093/brain/awl023 · DOI
- 10.1006/excr.2002.5605 · DOI
- 10.1016/0378-1119(96)00002-9 · DOI
- 10.1097/00002030-200008180-00023 · DOI
- 10.1083/jcb.123.6.1671 · DOI
- 10.1016/0092-8674(85)90072-8 · DOI
- 10.1083/jcb.200703081 · DOI
- 10.1016/j.virol.2005.11.053 · DOI
- 10.1038/nrg2047 · DOI · Paper page
- 10.1093/hmg/ddi480 · DOI
- 10.1038/6799 · DOI
- Boulikas,, 1986, Protein–protein and protein–DNA interactions in calf thymus nuclear matrix using cross-linking by ultraviolet irradiation, Biochem. Cell Biol., 64, 474, 10.1139/o86-066 · DOI
- 10.1016/0014-4827(85)90557-9 · DOI
- Bridger,, 1993, Internal lamin structures within G1 nuclei of human dermal fibroblasts, J. Cell Sci., 104, 297, 10.1242/jcs.104.2.297 · DOI
- 10.1007/s004180050138 · DOI
- Broers,, 1999, Dynamics of the nuclear lamina as monitored by GFP-tagged A-type lamins, J. Cell Sci., 112, 3463, 10.1242/jcs.112.20.3463 · DOI
- 10.1152/physrev.00047.2005 · DOI
- 10.1016/0014-4827(90)90223-W · DOI
- 10.1073/pnas.0611640104 · DOI
- 10.1016/S0014-4827(03)00395-1 · DOI
- 10.1016/0092-8674(82)90446-9 · DOI
- 10.1097/00002030-200311210-00005 · DOI
- 10.1073/pnas.0706529104 · DOI
- 10.1006/bbrc.1999.2023 · DOI
- 10.1073/pnas.0704212104 · DOI
- 10.1007/s00018-005-5318-6 · DOI
- 10.1634/stemcells.2004-0159 · DOI
- 10.1042/BJ20041359 · DOI
- 10.1016/j.ceb.2006.04.007 · DOI
- 10.1083/jcb.200509124 · DOI
- 10.1083/jcb.145.6.1119 · DOI
- 10.1111/j.1474-9728.2004.00105.x · DOI
- 10.1073/pnas.0601058103 · DOI
- 10.1177/39.8.1856453 · DOI
- 10.1126/science.1063957 · DOI
- 10.1126/science.1084125 · DOI · Paper page
- 10.1093/emboj/17.16.4887 · DOI · Paper page
- Dechat,, 2000, Lamina-associated polypeptide 2α binds intranuclear A-type lamins, J. Cell Sci., 113, 3473, 10.1242/jcs.113.19.3473 · DOI
- 10.1242/jcs.01529 · DOI
- 10.1073/pnas.0700854104 · DOI
- 10.1074/jbc.C200038200 · DOI
- 10.1083/jcb.200511149 · DOI
- 10.1111/j.1742-4658.2007.05695.x · DOI
- 10.1093/nar/gkf587 · DOI
- 10.1042/BC20070053 · DOI
- Ellis,, 1997, GST-lamin fusion proteins act as dominant negative mutants in Xenopus egg extract and reveal the function of the lamina in DNA replication, J. Cell Sci., 110, 2507, 10.1242/jcs.110.20.2507 · DOI
- 10.1038/nature01629 · DOI · Paper page
- 10.1006/excr.2002.5669 · DOI
- 10.1002/aja.1001190108 · DOI
- 10.1007/s00018-005-5515-3 · DOI
- Fields,, 1995, The regulation of mitotic nuclear envelope breakdown: A role for multiple lamin kinases, Prog. Cell Cycle Res., 1, 271, 10.1007/978-1-4615-1809-9_22 · DOI
- 10.1152/physiolgenomics.00060.2005 · DOI
- 10.1073/pnas.83.17.6450 · DOI
- 10.1016/0092-8674(93)90355-T · DOI
- 10.1126/science.1124875 · DOI
- 10.1172/JCI27125 · DOI
- 10.1101/gad.1364906 · DOI
- Furukawa,, 1993, cDNA cloning of a germ cell specific lamin B3 from mouse spermatocytes and analysis of its function by ectopic expression in somatic cells, EMBO J., 12, 97, 10.1002/j.1460-2075.1993.tb05635.x · DOI
- 10.1006/excr.1994.1164 · DOI
- 10.1006/bbrc.1997.7235 · DOI
- 10.1021/pr0700596 · DOI
- 10.1002/jcb.240340303 · DOI
- 10.1073/pnas.85.12.4325 · DOI
- 10.1083/jcb.79.2.546 · DOI
- 10.1038/sj.onc.1209615 · DOI
- 10.1016/S0959-437X(05)80279-5 · DOI
- 10.1083/jcb.111.3.1047 · DOI
- 10.1093/hmg/ddi326 · DOI
- 10.1073/pnas.96.6.2852 · DOI
- 10.1073/pnas.83.11.3839 · DOI
- 10.1083/jcb.119.4.725 · DOI
- 10.1101/gad.960502 · DOI
- 10.1073/pnas.0402943101 · DOI · Paper page
- 10.1128/JVI.79.6.3713-3727.2005 · DOI
- 10.1007/s00418-005-0050-8 · DOI
- 10.1242/jcs.01652 · DOI
- 10.1016/S0074-7696(03)01001-5 · DOI
- 10.1016/0014-4827(90)90267-E · DOI
- 10.1073/pnas.0506955102 · DOI
- 10.1093/gerona/62.1.3 · DOI
- 10.1128/MCB.26.10.3738-3751.2006 · DOI
- Harborth,, 2001, Identification of essential genes in cultured mammalian cells using small interfering RNAs, J. Cell Sci., 114, 4557, 10.1242/jcs.114.24.4557 · DOI
- 10.1086/505885 · DOI
- 10.1007/s00018-003-3004-0 · DOI
- 10.1093/gerona/60.1.10 · DOI
- 10.1016/0014-4827(91)90434-V · DOI
- 10.1074/jbc.M208811200 · DOI
- Houben,, 2007, Role of nuclear lamina–cytoskeleton interactions in the maintenance of cellular strength, Biochim. Biophys. Acta, 1773, 675, 10.1016/j.bbamcr.2006.09.018 · DOI
- Hozak,, 1995, Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells, J. Cell Sci., 108, 635, 10.1242/jcs.108.2.635 · DOI
- 10.1007/s00439-005-0051-7 · DOI
- 10.1016/j.yexcr.2007.08.004 · DOI
- 10.1016/j.yexcr.2005.10.011 · DOI
- 10.1073/pnas.0708572104 · DOI
- 10.1128/MCB.26.9.3659-3671.2006 · DOI · Paper page
- 10.1271/bbb.60674 · DOI
- 10.1038/nature04682 · DOI
- Jagatheesan,, 1999, Colocalization of intranuclear lamin foci with RNA splicing factors, J. Cell Sci., 112, 4651, 10.1242/jcs.112.24.4651 · DOI
- 10.1016/j.bbrc.2006.07.171 · DOI
- Jenkins,, 1993, Nuclei that lack a lamina accumulate karyophilic proteins and assemble a nuclear matrix, J. Cell Sci., 106, 275, 10.1242/jcs.106.1.275 · DOI
- 10.1073/pnas.0403250101 · DOI
- 10.1093/nar/30.10.2114 · DOI
- 10.1101/gad.842600 · DOI
- 10.1242/jcs.014191 · DOI
- 10.1101/gad.1499407 · DOI
- 10.1016/S0969-2126(02)00777-3 · DOI
- Kudlow,, 2005, HIV protease inhibitors block adipocyte differentiation independently of lamin A/C, AIDS, 19, 1565, 10.1097/01.aids.0000186827.91408.90 · DOI
- 10.1083/jcb.200706060 · DOI
- 10.1083/jcb.200204149 · DOI
- 10.1007/s00412-007-0098-4 · DOI
- 10.1083/jcb.105.3.1099 · DOI
- 10.1529/biophysj.106.102426 · DOI
- 10.1083/jcb.105.1.577 · DOI
- 10.1006/excr.1997.3735 · DOI
- 10.1091/mbc.11.11.3937 · DOI
- 10.1242/jcs.03263 · DOI · Paper page
- 10.1093/hmg/11.7.769 · DOI
- Loewinger,, 1988, Mutations in the nuclear lamin proteins resulting in their aberrant assembly in the cytoplasm, EMBO J., 7, 2301, 10.1002/j.1460-2075.1988.tb03073.x · DOI
- 10.1210/jc.2007-0116 · DOI
- Lourim,, 1996, Characterization and quantitation of three B-type lamins in Xenopus oocytes and eggs: Increase of lamin LI protein synthesis during meiotic maturation, J. Cell Sci., 109, 1775, 10.1242/jcs.109.7.1775 · DOI
- 10.1128/MCB.14.9.6297 · DOI
- 10.1074/jbc.271.16.9249 · DOI
- 10.1083/jcb.200607054 · DOI
- 10.1073/pnas.91.1.418 · DOI
- 10.1242/jcs.03009 · DOI
- 10.1016/j.tcb.2007.02.004 · DOI
- 10.1091/mbc.E04-02-0154 · DOI
- 10.1016/j.bbrc.2007.02.060 · DOI
- 10.1091/mbc.E02-07-0450 · DOI
- 10.1242/jcs.01630 · DOI
- 10.1074/jbc.M502672200 · DOI
- 10.1038/nrm1761 · DOI
- 10.1093/hmg/ddh205 · DOI
- 10.1016/0014-4827(92)90020-9 · DOI
- 10.1242/jcs.03325 · DOI
- 10.1007/s00018-003-3038-3 · DOI
- 10.1073/pnas.0511133103 · DOI
- 10.1371/journal.pone.0001269 · DOI
- 10.1038/319463a0 · DOI
- 10.1111/j.1474-9726.2007.00270.x · DOI
- 10.1007/PL00000817 · DOI
- Meier,, 1991, The role of lamin LIII in nuclear assembly and DNA replication, in cell-free extracts of Xenopus eggs, J. Cell Sci., 98, 271, 10.1242/jcs.98.3.271 · DOI
- 10.1016/j.yexcr.2007.03.004 · DOI
- 10.1093/hmg/ddi479 · DOI
- 10.1016/j.mib.2006.06.013 · DOI
- 10.1099/vir.0.82924-0 · DOI
- Miranda,, 2007, LMNA messenger RNA expression in highly active antiretroviral therapy-treated HIV-positive patients, J. Acquir. Immune Defic. Syndr., 46, 384, 10.1097/QAI.0b013e31815aba1b · DOI
- 10.1083/jcb.125.6.1201 · DOI
- 10.1083/jcb.149.6.1179 · DOI
- 10.1006/jsbi.2000.4251 · DOI
- 10.1083/jcb.151.6.1155 · DOI
- 10.1074/jbc.M509917200 · DOI
- 10.1128/JVI.00380-07 · DOI
- 10.1002/humu.20536 · DOI
- 10.1016/j.yexcr.2003.07.002 · DOI
- 10.1093/hmg/ddm137 · DOI
- 10.1172/JCI29042 · DOI
- Muralikrishna,, 2001, SP3 and AP-1 mediate transcriptional activation of the lamin A proximal promoter, Eur. J. Biochem., 268, 3736, 10.1046/j.1432-1327.2001.02281.x · DOI
- Muralikrishna,, 2001, Distinct changes in intranuclear lamin A/C organization during myoblast differentiation, J. Cell Sci., 114, 4001, 10.1242/jcs.114.22.4001 · DOI
- 10.1002/jcb.10765 · DOI
- 10.1126/science.1071506 · DOI
- 10.1083/jcb.111.6.2247 · DOI
- 10.1038/35087620 · DOI
- 10.1172/JCI200419448 · DOI
- 10.1371/journal.pone.0000963 · DOI
- 10.1016/j.bbrc.2004.05.191 · DOI
- 10.1016/j.ydbio.2005.05.022 · DOI
- Ozaki,, 1994, Complex formation between lamin A and the retinoblastoma gene product: Identification of the domain on lamin A required for its interaction, Oncogene, 9, 2649
- 10.1038/ng1872 · DOI
- 10.1242/jcs.02471 · DOI
- 10.1073/pnas.0702576104 · DOI
- 10.1128/JVI.80.1.494-504.2006 · DOI
- 10.1016/S0022-5320(67)80025-X · DOI
- 10.1083/jcb.200606139 · DOI
- 10.1038/nm0202-94 · DOI
- 10.1038/ng1852 · DOI
- 10.1038/npg.els. 0001337 · DOI
- 10.1016/j.jsb.2006.02.016 · DOI
- Radsak,, 1991, Focal nuclear envelope lesions and specific nuclear lamin A/C dephosphorylation during infection with human cytomegalovirus, Eur. J. Cell Biol., 54, 299
- 10.1073/pnas.0700794104 · DOI
- 10.1083/jcb.135.6.1441 · DOI
- 10.1242/jcs.03180 · DOI
- 10.1128/JVI.78.11.5564-5575.2004 · DOI
- Riemer,, 1995, Expression of Drosophila lamin C is developmentally regulated: Analogies with vertebrate A-type lamins, J. Cell Sci., 108, 3189, 10.1242/jcs.108.10.3189 · DOI
- Rober,, 1989, Differential timing of nuclear lamin A/C expression in the various organs of the mouse embryo and the young animal: A developmental study, Development, 105, 365, 10.1242/dev.105.2.365 · DOI
- Rober,, 1990, Cells of the cellular immune and hemopoietic system of the mouse lack lamins A/C: Distinction versus other somatic cells, J. Cell Sci., 95, 587, 10.1242/jcs.95.4.587 · DOI
- 10.1021/pr034035k · DOI
- 10.1093/emboj/21.8.1967 · DOI
- 10.1242/jcs.03156 · DOI
- Rzepecki,, 1998, In vivo association of lamins with nucleic acids in Drosophila melanogaster, J. Cell Sci., 111, 121, 10.1242/jcs.111.1.121 · DOI
- 10.1002/mus.1076 · DOI
- 10.1038/nrm1567 · DOI
- 10.1006/jsbi.1998.4006 · DOI
- Sasseville,, 1995, Lamin A precursor is localized to intranuclear foci, J. Cell Sci., 108, 273, 10.1242/jcs.108.1.273 · DOI
- 10.1038/nm1204 · DOI · Paper page
- 10.1126/science.1127168 · DOI · Paper page
- 10.1016/j.yexcr.2007.03.012 · DOI
200 of 260 shown
Cited by
Sorted by citations
López-Otín, C., Blasco, M. A., Partridge, L., Serrano, M., & Kroemer, G. (2013) · Cell · doi:10.1016/j.cell.2013.05.039 · Cited by 14,982
Lamin B1 loss is a senescence-associated biomarker
Freund, A., Laberge, R.-M., Demaria, M., & Campisi, J. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-10-0884 · Cited by 1,046
Epigenetic mechanisms of longevity and aging
Sen, P., Shah, P. P., Nativio, R., & Berger, S. L. (2016) · Cell · doi:10.1016/j.cell.2016.07.050 · Cited by 956
Human iPSC-based modeling of late-onset disease via progerin-induced aging
Miller, J. D., Ganat, Y. M., Kishinevsky, S., Bowman, R. L., Liu, B., Tu, E. Y., Mandal, P. K., Vera, E., Shim, J.-W., Kriks, S., et al. (2013) · Cell stem cell · doi:10.1016/j.stem.2013.11.006 · Cited by 777
Epigenetic regulation of ageing: linking environmental inputs to genomic stability
Benayoun, B. A., Pollina, E. A., & Brunet, A. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4048 · Cited by 610
Metadata
- Authors
- Dechat, T., Pfleghaar, K., Sengupta, K., Shimi, T., Shumaker, D. K., Solimando, L., & Goldman, R. D.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2008-04-01
- Volume
- 22
- Issue
- 7
- Pages
- 832-853
- ISSN
- 0890-9369
- 1549-5477
- Cited by
- 940
- References
- 9
- Language
- en
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review