The role of lamin B1 for the maintenance of nuclear structure and function

References

• Cremer T, Cremer M. Chromosome territories. Cold Spring Harb Perspect Biol 2010; 2:a003889; PMID:20300217; http://dx.doi.org/10.1101/cshperspect.a003889
   PubMed Web of Science ®Google Scholar
• Dechat T, Pfleghaar K, Sengupta K, Shimi T, Shumaker DK, Solimando L, Goldman RD. Nuclear lamins: major factors in the structural organization and function of the nucleus and chromatin. Genes Dev 2008; 22:832-53; PMID:18381888; http://dx.doi.org/10.1101/gad.1652708
   PubMed Web of Science ®Google Scholar
• Goldman RD, Gruenbaum Y, Moir RD, Shumaker DK, Spann TP. Nuclear lamins: building blocks of nuclear architecture. Genes Dev 2002; 16:533-47; PMID:11877373; http://dx.doi.org/10.1101/gad.960502
   PubMed Web of Science ®Google Scholar
• Broers JL, Ramaekers FC, Bonne G, Yaou RB, Hutchison CJ. Nuclear lamins: laminopathies and their role in premature ageing. Physiol Rev 2006; 86:967-1008; PMID:16816143; http://dx.doi.org/10.1152/physrev.00047.2005
   PubMed Web of Science ®Google Scholar
• Lee JM, Tu Y, Tatar A, Wu D, Nobumori C, Jung HJ, Yoshinaga Y, Coffinier C, de Jong PJ, Fong LG, et al. Reciprocal knock-in mice to investigate the functional redundancy of lamin B1 and lamin B2. Mol Biol Cell 2014; 25:1666-75; PMID:24672053; http://dx.doi.org/10.1091/mbc.E14-01-0683
   PubMed Web of Science ®Google Scholar
• Harborth J, Elbashir SM, Bechert K, Tuschl T, Weber K. Identification of essential genes in cultured mammalian cells using small interfering RNAs. J Cell Sci 2001; 114:4557-65; PMID:11792820
   PubMed Web of Science ®Google Scholar
• Yang SH, Chang SY, Yin L, Tu Y, Hu Y, Yoshinaga Y, de Jong PJ, Fong LG, Young SG. An absence of both lamin B1 and lamin B2 in keratinocytes has no effect on cell proliferation or the development of skin and hair. Hum Mol Genet 2011; 20:3537-44; PMID:21659336; http://dx.doi.org/10.1093/hmg/ddr266
   PubMed Web of Science ®Google Scholar
• Yang SH, Jung HJ, Coffinier C, Fong LG, Young SG. Are B-type lamins essential in all mammalian cells? Nucleus 2011; 2:562-9; PMID:22127257; http://dx.doi.org/10.4161/nucl.2.6.18085
   PubMed Web of Science ®Google Scholar
• Freund A, Laberge RM, Demaria M, Campisi J. Lamin B1 loss is a senescence-associated biomarker. Mol Biol Cell 2012; 23:2066-75; PMID:22496421; http://dx.doi.org/10.1091/mbc.E11-10-0884
   PubMed Web of Science ®Google Scholar
• Shimi T, Butin-Israeli V, Adam SA, Hamanaka RB, Goldman AE, Lucas CA, Shumaker DK, Kosak ST, Chandel NS, Goldman RD. The role of nuclear lamin B1 in cell proliferation and senescence. Genes Dev 2011; 25:2579-93; PMID:22155925; http://dx.doi.org/10.1101/gad.179515.111
   PubMed Web of Science ®Google Scholar
• Barascu A, Le Chalony C, Pennarun G, Genet D, Imam N, Lopez B, Bertrand P. Oxidative stress induces an ATM-independent senescence pathway through p38 MAPK-mediated lamin B1 accumulation. EMBO J 2012; 31:1080-94; PMID:22246186; http://dx.doi.org/10.1038/emboj.2011.492
   PubMed Web of Science ®Google Scholar
• Cremer T, Cremer C. Chromosome territories, nuclear architecture and gene regulation in mammalian cells. Nat Rev Genet 2001; 2:292-301; PMID:11283701; http://dx.doi.org/10.1038/35066075
   PubMed Web of Science ®Google Scholar
• Shimi T, Pfleghaar K, Kojima S, Pack CG, Solovei I, Goldman AE, Adam SA, Shumaker DK, Kinjo M, Cremer T, et al. The A- and B-type nuclear lamin networks: microdomains involved in chromatin organization and transcription. Genes Dev 2008; 22:3409-21; PMID:19141474; http://dx.doi.org/10.1101/gad.1735208
   PubMed Web of Science ®Google Scholar
• Malhas A, Lee CF, Sanders R, Saunders NJ, Vaux DJ. Defects in lamin B1 expression or processing affect interphase chromosome position and gene expression. J Cell Biol 2007; 176:593-603; PMID:17312019; http://dx.doi.org/10.1083/jcb.200607054
   PubMed Web of Science ®Google Scholar
• Camps J, Wangsa D, Falke M, Brown M, Case CM, Erdos MR, Ried T. Loss of lamin B1 results in prolongation of S phase and decondensation of chromosome territories. FASEB J 2014; 28:3423-34; PMID:24732130; http://dx.doi.org/10.1096/fj.14-250456
   PubMed Web of Science ®Google Scholar
• Columbaro M, Capanni C, Mattioli E, Novelli G, Parnaik VK, Squarzoni S, Maraldi NM, Lattanzi G. Rescue of heterochromatin organization in Hutchinson-Gilford progeria by drug treatment. Cell Mol Life Sci 2005; 62:2669-78; PMID:16261260; http://dx.doi.org/10.1007/s00018-005-5318-6
   PubMed Web of Science ®Google Scholar
• Goldman RD, Shumaker DK, Erdos MR, Eriksson M, Goldman AE, Gordon LB, Gruenbaum Y, Khuon S, Mendez M, Varga R, et al. Accumulation of mutant lamin A causes progressive changes in nuclear architecture in Hutchinson-Gilford progeria syndrome. Proc Natl Acad Sci USA 2004; 101:8963-8; PMID:15184648; http://dx.doi.org/10.1073/pnas.0402943101
   PubMed Web of Science ®Google Scholar
• Shumaker DK, Dechat T, Kohlmaier A, Adam SA, Bozovsky MR, Erdos MR, Eriksson M, Goldman AE, Khuon S, Collins FS, et al. Mutant nuclear lamin A leads to progressive alterations of epigenetic control in premature aging. Proc Natl Acad Sci U S A 2006; 103:8703-8; PMID:16738054; http://dx.doi.org/10.1073/pnas.0602569103
   PubMed Web of Science ®Google Scholar
• Shah PP, Donahue G, Otte GL, Capell BC, Nelson DM, Cao K, Aggarwala V, Cruickshanks HA, Rai TS, McBryan T, et al. Lamin B1 depletion in senescent cells triggers large-scale changes in gene expression and the chromatin landscape. Genes Dev 2013; 27:1787-99; PMID:23934658; http://dx.doi.org/10.1101/gad.223834.113
   PubMed Web of Science ®Google Scholar
• Finlan LE, Sproul D, Thomson I, Boyle S, Kerr E, Perry P, Ylstra B, Chubb JR, Bickmore WA. Recruitment to the nuclear periphery can alter expression of genes in human cells. PLoS Genet 2008; 4:e1000039; PMID:18369458; http://dx.doi.org/10.1371/journal.pgen.1000039
   PubMed Web of Science ®Google Scholar
• Kourmouli N, Theodoropoulos PA, Dialynas G, Bakou A, Politou AS, Cowell IG, Singh PB, Georgatos SD. Dynamic associations of heterochromatin protein 1 with the nuclear envelope. EMBO J 2000; 19:6558-68; PMID:11101528; http://dx.doi.org/10.1093/emboj/19.23.6558
   PubMed Web of Science ®Google Scholar
• Reddy KL, Zullo JM, Bertolino E, Singh H. Transcriptional repression mediated by repositioning of genes to the nuclear lamina. Nature 2008; 452:243-7; PMID:18272965; http://dx.doi.org/10.1038/nature06727
   PubMed Web of Science ®Google Scholar
• Shaklai S, Amariglio N, Rechavi G, Simon AJ. Gene silencing at the nuclear periphery. FEBS J 2007; 274:1383-92; PMID:17489096; http://dx.doi.org/10.1111/j.1742-4658.2007.05697.x
   PubMed Web of Science ®Google Scholar
• Guelen L, Pagie L, Brasset E, Meuleman W, Faza MB, Talhout W, Eussen BH, de Klein A, Wessels L, de Laat W, et al. Domain organization of human chromosomes revealed by mapping of nuclear lamina interactions. Nature 2008; 453:948-51; PMID:18463634; http://dx.doi.org/10.1038/nature06947
   PubMed Web of Science ®Google Scholar
• Peric-Hupkes D, Meuleman W, Pagie L, Bruggeman SW, Solovei I, Brugman W, Gräf S, Flicek P, Kerkhoven RM, van Lohuizen M, et al. Molecular maps of the reorganization of genome-nuclear lamina interactions during differentiation. Mol Cell 2010; 38:603-13; PMID:20513434; http://dx.doi.org/10.1016/j.molcel.2010.03.016
   PubMed Web of Science ®Google Scholar
• Kalverda B, Pickersgill H, Shloma VV, Fornerod M. Nucleoporins directly stimulate expression of developmental and cell-cycle genes inside the nucleoplasm. Cell 2010; 140:360-71; PMID:20144760; http://dx.doi.org/10.1016/j.cell.2010.01.011
   PubMed Web of Science ®Google Scholar
• Tang CW, Maya-Mendoza A, Martin C, Zeng K, Chen S, Feret D, Wilson SA, Jackson DA. The integrity of a lamin-B1-dependent nucleoskeleton is a fundamental determinant of RNA synthesis in human cells. J Cell Sci 2008; 121:1014-24; PMID:18334554; http://dx.doi.org/10.1242/jcs.020982
   PubMed Web of Science ®Google Scholar
• Cao K, Blair CD, Faddah DA, Kieckhaefer JE, Olive M, Erdos MR, Nabel EG, Collins FS. Progerin and telomere dysfunction collaborate to trigger cellular senescence in normal human fibroblasts. J Clin Invest 2011; 121:2833-44; PMID:21670498; http://dx.doi.org/10.1172/JCI43578
   PubMed Web of Science ®Google Scholar
• Luderus ME, van Steensel B, Chong L, Sibon OC, Cremers FF, de Lange T. Structure, subnuclear distribution, and nuclear matrix association of the mammalian telomeric complex. J Cell Biol 1996; 135:867-81; PMID:8922373; http://dx.doi.org/10.1083/jcb.135.4.867
   PubMed Web of Science ®Google Scholar
• Moir RD, Montag-Lowy M, Goldman RD. Dynamic properties of nuclear lamins: lamin B is associated with sites of DNA replication. J Cell Biol 1994; 125:1201-12; PMID:7911470; http://dx.doi.org/10.1083/jcb.125.6.1201
   PubMed Web of Science ®Google Scholar
• Lopez-Soler RI, Moir RD, Spann TP, Stick R, Goldman RD. A role for nuclear lamins in nuclear envelope assembly. J Cell Biol 2001; 154:61-70; PMID:11448990; http://dx.doi.org/10.1083/jcb.200101025
   PubMed Web of Science ®Google Scholar
• Shumaker DK, Solimando L, Sengupta K, Shimi T, Adam SA, Grunwald A, Strelkov SV, Aebi U, Cardoso MC, Goldman RD. The highly conserved nuclear lamin Ig-fold binds to PCNA: its role in DNA replication. J Cell Biol 2008; 181:269-80; PMID:18426975; http://dx.doi.org/10.1083/jcb.200708155
   PubMed Web of Science ®Google Scholar
• Ellis DJ, Jenkins H, Whitfield WG, Hutchison CJ. 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 1997; 110 (Pt 20):2507-18; PMID:9372440
   PubMed Web of Science ®Google Scholar
• Spann TP, Moir RD, Goldman AE, Stick R, Goldman RD. Disruption of nuclear lamin organization alters the distribution of replication factors and inhibits DNA synthesis. J Cell Biol 1997; 136:1201-12; PMID:9087437; http://dx.doi.org/10.1083/jcb.136.6.1201
   PubMed Web of Science ®Google Scholar
• Martins S, Eikvar S, Furukawa K, Collas P. HA95 and LAP2 beta mediate a novel chromatin-nuclear envelope interaction implicated in initiation of DNA replication. J Cell Biol 2003; 160:177-88; PMID:12538639; http://dx.doi.org/10.1083/jcb.200210026
   PubMed Web of Science ®Google Scholar
• Speck C, Stillman B. Cdc6 ATPase activity regulates ORC x Cdc6 stability and the selection of specific DNA sequences as origins of DNA replication. J Biol Chem 2007; 282:11705-14; PMID:17314092; http://dx.doi.org/10.1074/jbc.M700399200
   PubMed Web of Science ®Google Scholar
• Yoshida K, Sugimoto N, Iwahori S, Yugawa T, Narisawa-Saito M, Kiyono T, Fujita M. CDC6 interaction with ATR regulates activation of a replication checkpoint in higher eukaryotic cells. J Cell Sci 2010; 123:225-35; PMID:20048340; http://dx.doi.org/10.1242/jcs.058693
   PubMedGoogle Scholar