Nuclear Lamins and Neurobiology

REFERENCES

• Muchir A, Worman HJ. 2004. The nuclear envelope and human disease. Physiology (Bethesda) 19:309–314. http://dx.doi.org/10.1152/physiol.00022.2004.
   PubMed Web of Science ®Google Scholar
• Worman HJ, Bonne G. 2007. “Laminopathies”: a wide spectrum of human diseases. Exp. Cell Res. 313:2121–2133. http://dx.doi.org/10.1016/j.yexcr.2007.03.028.
   PubMed Web of Science ®Google Scholar
• Worman HJ, Fong LG, Muchir A, Young SG. 2009. Laminopathies and the long strange trip from basic cell biology to therapy. J. Clin. Invest. 119:1825–1836. http://dx.doi.org/10.1172/JCI37679.
   PubMed Web of Science ®Google Scholar
• Broers JL, Ramaekers FC, Bonne G, Yaou RB, Hutchison CJ. 2006. Nuclear lamins: laminopathies and their role in premature ageing. Physiol. Rev. 86:967–1008. http://dx.doi.org/10.1152/physrev.00047.2005.
   PubMed Web of Science ®Google Scholar
• Gruenbaum Y, Margalit A, Goldman RD, Shumaker DK, Wilson KL. 2005. The nuclear lamina comes of age. Nat. Rev. Mol. Cell Biol. 6:21–31. http://dx.doi.org/10.1038/nrm1550.
   PubMed Web of Science ®Google Scholar
• Dechat T, Pfleghaar K, Sengupta K, Shimi T, Shumaker DK, Solimando L, Goldman RD. 2008. Nuclear lamins: major factors in the structural organization and function of the nucleus and chromatin. Genes Dev. 22:832–853. http://dx.doi.org/10.1101/gad.1652708.
   PubMed Web of Science ®Google Scholar
• Burke B, Stewart CL. 2013. The nuclear lamins: flexibility in function. Nat. Rev. Mol. Cell Biol. 14:13–24. http://dx.doi.org/10.1038/nrm3488.
   PubMed Web of Science ®Google Scholar
• Young SG, Fong LG, Michaelis S. 2005. Prelamin A, Zmpste24, misshapen cell nuclei, and progeria—new evidence suggesting that protein farnesylation could be important for disease pathogenesis. J. Lipid Res. 46:2531–2558. http://dx.doi.org/10.1194/jlr.R500011-JLR200.
   PubMed Web of Science ®Google Scholar
• Davies BS, Coffinier C, Yang SH, Barnes RHII, Jung HJ, Young SG, Fong LG. 2011. Investigating the purpose of prelamin A processing. Nucleus 2:4–9. http://dx.doi.org/10.4161/nucl.2.1.13723.
   PubMed Web of Science ®Google Scholar
• Young SG, Yang SH, Davies BS, Jung HJ, Fong LG. 2013. Targeting protein prenylation in progeria. Sci. Transl. Med. 5:171ps173. http://dx.doi.org/10.1126/scitranslmed.3005229.
   Google Scholar
• Davies BS, Fong LG, Yang SH, Coffinier C, Young SG. 2009. The posttranslational processing of prelamin A and disease. Annu. Rev. Genomics Hum. Genet. 10:153–174. http://dx.doi.org/10.1146/annurev-genom-082908-150150.
   PubMed Web of Science ®Google Scholar
• Coffinier C, Chang SY, Nobumori C, Tu Y, Farber EA, Toth JI, Fong LG, Young SG. 2010. Abnormal development of the cerebral cortex and cerebellum in the setting of lamin B2 deficiency. Proc. Natl. Acad. Sci. U. S. A. 107:5076–5081. http://dx.doi.org/10.1073/pnas.0908790107.
   PubMed Web of Science ®Google Scholar
• Coffinier C, Fong LG, Young SG. 2010. LINCing lamin B2 to neuronal migration: growing evidence for cell-specific roles of B-type lamins. Nucleus 1:407–411. http://dx.doi.org/10.4161/nucl.1.5.12830.
   PubMed Web of Science ®Google Scholar
• Coffinier C, Jung HJ, Nobumori C, Chang S, Tu Y, Barnes RHII, Yoshinaga Y, de Jong PJ, Vergnes L, Reue K, Fong LG, Young SG. 2011. Deficiencies in lamin B1 and lamin B2 cause neurodevelopmental defects and distinct nuclear shape abnormalities in neurons. Mol. Biol. Cell 22:4683–4693. http://dx.doi.org/10.1091/mbc.E11-06-0504.
   PubMed Web of Science ®Google Scholar
• Padiath QS, Fu YH. 2010. Autosomal dominant leukodystrophy caused by lamin B1 duplications a clinical and molecular case study of altered nuclear function and disease. Methods Cell Biol. 98:337–357. http://dx.doi.org/10.1016/S0091-679X(10)98014-X.
   PubMed Web of Science ®Google Scholar
• Padiath QS, Saigoh K, Schiffmann R, Asahara H, Yamada T, Koeppen A, Hogan K, Ptacek LJ, Fu YH. 2006. Lamin B1 duplications cause autosomal dominant leukodystrophy. Nat. Genet. 38:1114–1123. http://dx.doi.org/10.1038/ng1872.
   PubMed Web of Science ®Google Scholar
• Jung HJ, Tu Y, Yang SH, Tatar A, Nobumori C, Wu D, Young SG, Fong LG. 2014. New Lmna knock-in mice provide a molecular mechanism for the ‘segmental aging' in Hutchinson-Gilford progeria syndrome. Hum. Mol. Genet. 23:1506–1515. http://dx.doi.org/10.1093/hmg/ddt537.
   PubMedGoogle Scholar
• Jung HJ, Coffinier C, Choe Y, Beigneux AP, Davies BS, Yang SH, Barnes RHII, Hong J, Sun T, Pleasure SJ, Young SG, Fong LG. 2012. Regulation of prelamin A but not lamin C by miR-9, a brain-specific microRNA. Proc. Natl. Acad. Sci. U. S. A. 109:E423–E431. http://dx.doi.org/10.1073/pnas.1111780109.
   PubMed Web of Science ®Google Scholar
• Eriksson M, Brown WT, Gordon LB, Glynn MW, Singer J, Scott L, Erdos MR, Robbins CM, Moses TY, Berglund P, Dutra A, Pak E, Durkin S, Csoka AB, Boehnke M, Glover TW, Collins FS. 2003. Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome. Nature 423:293–298. http://dx.doi.org/10.1038/nature01629.
   PubMed Web of Science ®Google Scholar
• Lin F, Worman HJ. 1993. Structural organization of the human gene encoding nuclear lamin A and nuclear lamin C. J. Biol. Chem. 268:16321–16326.
   PubMed Web of Science ®Google Scholar
• Lin F, Worman HJ. 1995. Structural organization of the human gene (LMNB1) encoding nuclear lamin B1. Genomics 27:230–236. http://dx.doi.org/10.1006/geno.1995.1036.
   PubMed Web of Science ®Google Scholar
• Biamonti G, Giacca M, Perini G, Contreas G, Zentilin L, Weighardt F, Guerra M, Della Valle G, Saccone S, Riva S, Falaschi A. 1992. The gene for a novel human lamin maps at a highly transcribed locus of chromosome 19 which replicates at the onset of S-phase. Mol. Cell. Biol. 12:3499–3506.
   PubMed Web of Science ®Google Scholar
• Lammerding J, Fong LG, Ji JY, Reue K, Stewart CL, Young SG, Lee RT. 2006. Lamins A and C but not lamin B1 regulate nuclear mechanics. J. Biol. Chem. 281:25768–25780. http://dx.doi.org/10.1074/jbc.M513511200.
   PubMed Web of Science ®Google Scholar
• Ji JY, Lee RT, Vergnes L, Fong LG, Stewart CL, Reue K, Young SG, Zhang Q, Shanahan CM, Lammerding J. 2007. Cell nuclei spin in the absence of lamin B1. J. Biol. Chem. 282:20015–20026. http://dx.doi.org/10.1074/jbc.M611094200.
   PubMed Web of Science ®Google Scholar
• Corrigan DP, Kuszczak D, Rusinol AE, Thewke DP, Hrycyna CA, Michaelis S, Sinensky MS. 2005. Prelamin A endoproteolytic processing in vitro by recombinant ZMPSTE24. Biochem. J. 387:129–138. http://dx.doi.org/10.1042/BJ20041359.
   PubMed Web of Science ®Google Scholar
• Bergo MO, Gavino B, Ross J, Schmidt WK, Hong C, Kendall LV, Mohr A, Meta M, Genant H, Jiang Y, Wisner ER, van Bruggen N, Carano RAD, Michaelis S, Griffey SM, Young SG. 2002. Zmpste24 deficiency in mice causes spontaneous bone fractures, muscle weakness, and a prelamin A processing defect. Proc. Natl. Acad. Sci. U. S. A. 99:13049–13054. http://dx.doi.org/10.1073/pnas.192460799.
   PubMed Web of Science ®Google Scholar
• Pendás AM, Zhou Z, Cadiñanos J, Freije JMP, Wang J, Hultenby K, Astudillo A, Wernerson A, Rodríguez F, Tryggvason K, Lopéz-Otín C. 2002. Defective prelamin A processing and muscular and adipocyte alterations in Zmpste24 metalloproteinase-deficient mice. Nat. Genet. 31:94–99. http://dx.doi.org/10.1038/ng871.
   PubMed Web of Science ®Google Scholar
• Sinensky M, Fantle K, Trujillo M, McLain T, Kupfer A, Dalton M. 1994. The processing pathway of prelamin A. J. Cell Sci. 107:61–67.
   PubMed Web of Science ®Google Scholar
• Barrowman J, Hamblet C, George CM, Michaelis S. 2008. Analysis of prelamin A biogenesis reveals the nucleus to be a CaaX processing compartment. Mol. Biol. Cell 19:5398–5408. http://dx.doi.org/10.1091/mbc.E08-07-0704.
   PubMed Web of Science ®Google Scholar
• Coffinier C, Jung HJ, Li Z, Nobumori C, Yun UJ, Farber EA, Davies BS, Weinstein MM, Yang SH, Lammerding J, Farahani JN, Bentolila LA, Fong LG, Young SG. 2010. Direct synthesis of lamin A, bypassing prelamin a processing, causes misshapen nuclei in fibroblasts but no detectable pathology in mice. J. Biol. Chem. 285:20818–20826. http://dx.doi.org/10.1074/jbc.M110.128835.
   PubMed Web of Science ®Google Scholar
• Davies BS, Barnes RHII, Tu Y, Ren S, Andres DA, Spielmann HP, Lammerding J, Wang Y, Young SG, Fong LG. 2010. An accumulation of non-farnesylated prelamin A causes cardiomyopathy but not progeria. Hum. Mol. Genet. 19:2682–2694. http://dx.doi.org/10.1093/hmg/ddq158.
   PubMed Web of Science ®Google Scholar
• Stewart C, Burke B. 1987. Teratocarcinoma stem cells and early mouse embryos contain only a single major lamin polypeptide closely resembling lamin B. Cell 51:383–392. http://dx.doi.org/10.1016/0092-8674(87)90634-9.
   PubMed Web of Science ®Google Scholar
• Eckersley-Maslin MA, Bergmann JH, Lazar Z, Spector DL. 2013. Lamin A/C is expressed in pluripotent mouse embryonic stem cells. Nucleus 4:53–60. http://dx.doi.org/10.4161/nucl.23384.
   PubMed Web of Science ®Google Scholar
• Röber RA, Weber K, Osborn M. 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 105:365–378.
   PubMed Web of Science ®Google Scholar
• Sullivan T, Escalante-Alcalde D, Bhatt H, Anver M, Bhat N, Nagashima K, Stewart CL, Burke B. 1999. Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy. J. Cell Biol. 147:913–919. http://dx.doi.org/10.1083/jcb.147.5.913.
   PubMed Web of Science ®Google Scholar
• Jahn D, Schramm S, Schnolzer M, Heilmann CJ, de Koster CG, Schutz W, Benavente R, Alsheimer M. 2012. A truncated lamin A in the Lmna -/- mouse line: implications for the understanding of laminopathies. Nucleus 3:463–474. http://dx.doi.org/10.4161/nucl.21676.
   PubMed Web of Science ®Google Scholar
• Solovei I, Wang AS, Thanisch K, Schmidt CS, Krebs S, Zwerger M, Cohen TV, Devys D, Foisner R, Peichl L, Herrmann H, Blum H, Engelkamp D, Stewart CL, Leonhardt H, Joffe B. 2013. LBR and lamin A/C sequentially tether peripheral heterochromatin and inversely regulate differentiation. Cell 152:584–598. http://dx.doi.org/10.1016/j.cell.2013.01.009.
   PubMed Web of Science ®Google Scholar
• Fong LG, Ng JK, Lammerding J, Vickers TA, Meta M, Cote N, Gavino B, Qiao X, Chang SY, Young SR, Yang SH, Stewart CL, Lee RT, Bennett CF, Bergo MO, Young SG. 2006. Prelamin A and lamin A appear to be dispensable in the nuclear lamina. J. Clin. Invest. 116:743–752. http://dx.doi.org/10.1172/JCI27125.
   PubMed Web of Science ®Google Scholar
• Moir RD, Montag-Lowy M, Goldman RD. 1994. Dynamic properties of nuclear lamins: lamin B is associated with sites of DNA replication. J. Cell Biol. 125:1201–1212. http://dx.doi.org/10.1083/jcb.125.6.1201.
   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, Goldman RD. 2008. The A- and B-type nuclear lamin networks: microdomains involved in chromatin organization and transcription. Genes Dev. 22:3409–3421. http://dx.doi.org/10.1101/gad.1735208.
   PubMed Web of Science ®Google Scholar
• Tang CW, Maya-Mendoza A, Martin C, Zeng K, Chen S, Feret D, Wilson SA, Jackson DA. 2008. The integrity of a lamin-B1-dependent nucleoskeleton is a fundamental determinant of RNA synthesis in human cells. J. Cell Sci. 121:1014–1024. http://dx.doi.org/10.1242/jcs.020982.
   PubMedGoogle Scholar
• Tsai MY, Wang S, Heidinger JM, Shumaker DK, Adam SA, Goldman RD, Zheng Y. 2006. A mitotic lamin B matrix induced by RanGTP required for spindle assembly. Science 311:1887–1893. http://dx.doi.org/10.1126/science.1122771.
   PubMed Web of Science ®Google Scholar
• Belmont AS, Zhai Y, Thilenius A. 1993. Lamin B distribution and association with peripheral chromatin revealed by optical sectioning and electron microscopy tomography. J. Cell Biol. 123:1671–1685. http://dx.doi.org/10.1083/jcb.123.6.1671.
   PubMed Web of Science ®Google Scholar
• Harborth J, Elbashir SM, Bechert K, Tuschl T, Weber K. 2001. Identification of essential genes in cultured mammalian cells using small interfering RNAs. J. Cell Sci. 114(Pt 24):4557–4565.
   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. 2011. 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. 20:3537–3544. http://dx.doi.org/10.1093/hmg/ddr266.
   PubMed Web of Science ®Google Scholar
• Yang SH, Jung HJ, Coffinier C, Fong LG, Young SG. 2011. Are B-type lamins essential in all mammalian cells? Nucleus 2:562–569. http://dx.doi.org/10.4161/nucl.2.6.18085.
   PubMed Web of Science ®Google Scholar
• Kim Y, Zheng X, Zheng Y. 2013. Proliferation and differentiation of mouse embryonic stem cells lacking all lamins. Cell Res. 23:1420–1423. http://dx.doi.org/10.1038/cr.2013.118.
   PubMed Web of Science ®Google Scholar
• Gupta A, Tsai LH, Wynshaw-Boris A. 2002. Life is a journey: a genetic look at neocortical development. Nat. Rev. Genet. 3:342–355. http://dx.doi.org/10.1038/nrg799.
   PubMed Web of Science ®Google Scholar
• Wynshaw-Boris A. 2007. Lissencephaly and LIS1: insights into the molecular mechanisms of neuronal migration and development. Clin. Genet. 72:296–304. http://dx.doi.org/10.1111/j.1399-0004.2007.00888.x.
   PubMed Web of Science ®Google Scholar
• Gambello MJ, Hirotsune S, Wynshaw-Boris A. 1999. Murine modelling of classical lissencephaly. Neurogenetics 2:77–86. http://dx.doi.org/10.1007/s100480050056.
   PubMedGoogle Scholar
• Kim Y, Sharov AA, McDole K, Cheng M, Hao H, Fan CM, Gaiano N, Ko MS, Zheng Y. 2011. Mouse B-type lamins are required for proper organogenesis but not by embryonic stem cells. Science 334:1706–1710. http://dx.doi.org/10.1126/science.1211222.
   PubMed Web of Science ®Google Scholar
• Solecki DJ, Govek EE, Tomoda T, Hatten ME. 2006. Neuronal polarity in CNS development. Genes Dev. 20:2639–2647. http://dx.doi.org/10.1101/gad.1462506.
   PubMed Web of Science ®Google Scholar
• Wynshaw-Boris A, Gambello MJ. 2001. LIS1 and dynein motor function in neuronal migration and development. Genes Dev. 15:639–651. http://dx.doi.org/10.1101/gad.886801.
   PubMed Web of Science ®Google Scholar
• Vallee RB, Tsai JW. 2006. The cellular roles of the lissencephaly gene LIS1, and what they tell us about brain development. Genes Dev. 20:1384–1393. http://dx.doi.org/10.1101/gad.1417206.
   PubMed Web of Science ®Google Scholar
• Crisp M, Liu Q, Roux K, Rattner JB, Shanahan C, Burke B, Stahl PD, Hodzic D. 2006. Coupling of the nucleus and cytoplasm: role of the LINC complex. J. Cell Biol. 172:41–53. http://dx.doi.org/10.1083/jcb.200509124.
   PubMed Web of Science ®Google Scholar
• Zhang X, Lei K, Yuan X, Wu X, Zhuang Y, Xu T, Xu R, Han M. 2009. SUN1/2 and Syne/Nesprin-1/2 complexes connect centrosome to the nucleus during neurogenesis and neuronal migration in mice. Neuron 64:173–187. http://dx.doi.org/10.1016/j.neuron.2009.08.018.
   PubMed Web of Science ®Google Scholar
• Vergnes L, Peterfy M, Bergo MO, Young SG, Reue K. 2004. Lamin B1 is required for mouse development and nuclear integrity. Proc. Natl. Acad. Sci. U. S. A. 101:10428–10433. http://dx.doi.org/10.1073/pnas.0401424101.
   PubMed Web of Science ®Google Scholar
• Young SG, Jung HJ, Coffinier C, Fong LG. 2012. Understanding the roles of nuclear A- and B-type lamins in brain development. J. Biol. Chem. 287:16103–16110. http://dx.doi.org/10.1074/jbc.R112.354407.
   PubMed Web of Science ®Google Scholar
• Patterson K, Molofsky AB, Robinson C, Acosta S, Cater C, Fischer JA. 2004. The functions of Klarsicht and nuclear lamin in developmentally regulated nuclear migrations of photoreceptor cells in the Drosophila eye. Mol. Biol. Cell 15:600–610. http://dx.doi.org/10.1091/mbc.E03-06-0374.
   PubMed Web of Science ®Google Scholar
• Harada T, Swift J, Irianto J, Shin JW, Spinler KR, Athirasala A, Diegmiller R, Dingal PC, Ivanovska IL, Discher DE. 2014. Nuclear lamin stiffness is a barrier to 3D migration, but softness can limit survival. J. Cell Biol. 204:669–682. http://dx.doi.org/10.1083/jcb.201308029.
   PubMed Web of Science ®Google Scholar
• Swift J, Harada T, Buxboim A, Shin JW, Tang HY, Speicher DW, Discher DE. 2013. Label-free mass spectrometry exploits dozens of detected peptides to quantify lamins in wildtype and knockdown cells. Nucleus 4:450–459. http://dx.doi.org/10.4161/nucl.27413.
   PubMed Web of Science ®Google Scholar
• Swift J, Ivanovska IL, Buxboim A, Harada T, Dingal PC, Pinter J, Pajerowski JD, Spinler KR, Shin JW, Tewari M, Rehfeldt F, Speicher DW, Discher DE. 2013. Nuclear lamin-A scales with tissue stiffness and enhances matrix-directed differentiation. Science 341:1240104. http://dx.doi.org/10.1126/science.1240104.
   PubMed Web of Science ®Google Scholar
• Rowat AC, Jaalouk DE, Zwerger M, Ung WL, Eydelnant IA, Olins DE, Olins AL, Herrmann H, Weitz DA, Lammerding J. 2013. Nuclear envelope composition determines the ability of neutrophil-type cells to passage through micron-scale constrictions. J. Biol. Chem. 288:8610–8618. http://dx.doi.org/10.1074/jbc.M112.441535.
   PubMed Web of Science ®Google Scholar
• Friedl P, Wolf K, Lammerding J. 2011. Nuclear mechanics during cell migration. Curr. Opin. Cell Biol. 23:55–64. http://dx.doi.org/10.1016/j.ceb.2010.10.015.
   PubMed Web of Science ®Google Scholar
• Dahl KN, Engler AJ, Pajerowski JD, Discher DE. 2005. Power-law rheology of isolated nuclei with deformation mapping of nuclear substructures. Biophys. J. 89:2855–2864. http://dx.doi.org/10.1529/biophysj.105.062554.
   PubMed Web of Science ®Google Scholar
• Robinson A, Partridge D, Malhas A, De Castro SC, Gustavsson P, Thompson DN, Vaux DJ, Copp AJ, Stanier P, Bassuk AG, Greene ND. 2013. Is LMNB1 a susceptibility gene for neural tube defects in humans? Birth Defects Res. A Clin. Mol. Teratol. 97:398–402. http://dx.doi.org/10.1002/bdra.23141.
   PubMedGoogle Scholar
• De Castro SC, Malhas A, Leung KY, Gustavsson P, Vaux DJ, Copp AJ, Greene ND. 2012. Lamin b1 polymorphism influences morphology of the nuclear envelope, cell cycle progression, and risk of neural tube defects in mice. PLoS Genet. 8:e1003059. http://dx.doi.org/10.1371/journal.pgen.1003059.
   PubMed Web of Science ®Google Scholar
• Jung HJ, Nobumori C, Goulbourne CN, Tu Y, Lee JM, Tatar A, Wu D, Yoshinaga Y, de Jong PJ, Coffinier C, Fong LG, Young SG. 2013. Farnesylation of lamin B1 is important for retention of nuclear chromatin during neuronal migration. Proc. Natl. Acad. Sci. U. S. A. 110:E1923–E1932. http://dx.doi.org/10.1073/pnas.1303916110.
   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, Young SG. 26 March 2014. Reciprocal knock-in mice to investigate the functional redundancy of lamin B1 and lamin B2. Mol. Biol. Cell http://dx.doi.org/10.1091/mbc.E14-01-0683.
   Google Scholar
• Eldridge R, Anayiotos CP, Schlesinger S, Cowen D, Bever C, Patronas N, McFarland H. 1984. Hereditary adult-onset leukodystrophy simulating chronic progressive multiple sclerosis. N. Engl. J. Med. 311:948–953. http://dx.doi.org/10.1056/NEJM198410113111504.
   PubMedGoogle Scholar
• Melberg A, Hallberg L, Kalimo H, Raininko R. 2006. MR characteristics and neuropathology in adult-onset autosomal dominant leukodystrophy with autonomic symptoms. Am. J. Neuroradiol. 27:904–911. http://www.ajnr.org/content/27/4/904.long.
   PubMed Web of Science ®Google Scholar
• Lin ST, Fu YH. 2009. miR-23 regulation of lamin B1 is crucial for oligodendrocyte development and myelination. Dis. Model. Mech. 2:178–188. http://dx.doi.org/10.1242/dmm.001065.
   PubMed Web of Science ®Google Scholar
• Coffeen CM, McKenna CE, Koeppen AH, Plaster NM, Maragakis N, Mihalopoulos J, Schwankhaus JD, Flanigan KM, Gregg RG, Ptacek LJ, Fu YH. 2000. Genetic localization of an autosomal dominant leukodystrophy mimicking chronic progressive multiple sclerosis to chromosome 5q31. Hum. Mol. Genet. 9:787–793. http://dx.doi.org/10.1093/hmg/9.5.787.
   PubMedGoogle Scholar
• Marklund L, Melin M, Melberg A, Giedraitis V, Dahl N. 2006. Adult-onset autosomal dominant leukodystrophy with autonomic symptoms restricted to 1.5 Mbp on chromosome 5q23. Am. J. Med. Genet. B Neuropsychiatr. Genet. 141:608–614. http://dx.doi.org/10.1002/ajmg.b.30342.
   Google Scholar
• Giorgio E, Rolyan H, Kropp L, Chakka AB, Yatsenko S, Gregorio ED, Lacerenza D, Vaula G, Talarico F, Mandich P, Toro C, Pierre EE, Labauge P, Capellari S, Cortelli P, Vairo FP, Miguel D, Stubbolo D, Marques LC, Gahl W, Boespflug-Tanguy O, Melberg A, Hassin-Baer S, Cohen OS, Pjontek R, Grau A, Klopstock T, Fogel B, Meijer I, Rouleau G, Bouchard JP, Ganapathiraju M, Vanderver A, Dahl N, Hobson G, Brusco A, Brussino A, Padiath QS. 2013. Analysis of LMNB1 duplications in autosomal dominant leukodystrophy provides insights into duplication mechanisms and allele-specific expression. Hum. Mutat. 34:1160–1171. http://dx.doi.org/10.1002/humu.22348.
   PubMedGoogle Scholar
• Brussino A, Vaula G, Cagnoli C, Panza E, Seri M, Di Gregorio E, Scappaticci S, Camanini S, Daniele D, Bradac GB, Pinessi L, Cavalieri S, Grosso E, Migone N, Brusco A. 2010. A family with autosomal dominant leukodystrophy linked to 5q23.2–q23.3 without lamin B1 mutations. Eur. J. Neurol. 17:541–549. http://dx.doi.org/10.1111/j.1468-1331.2009.02844.x.
   PubMedGoogle Scholar
• Ralle T, Grund C, Franke WW, Stick R. 2004. Intranuclear membrane structure formations by CaaX-containing nuclear proteins. J. Cell Sci. 117:6095–6104. http://dx.doi.org/10.1242/jcs.01528.
   PubMed Web of Science ®Google Scholar
• Favreau C, Dubosclard E, Ostlund C, Vigoroux C, Capeau J, Wehnert M, Higuet D, Worman H, Courvalin J-C, Buendia B. 2003. Expression of lamin A mutated in the carboxyl-terminal tail generates an aberrant nuclear phenotype similar to that observed in cells from patients with Dunnigan-type partial lipodystrophy and Emery-Dreifuss muscular dystrophy. Exp. Cell Res. 282:14–23. http://dx.doi.org/10.1006/excr.2002.5669.
   PubMed Web of Science ®Google Scholar
• Heng MY, Lin ST, Verret L, Huang Y, Kamiya S, Padiath QS, Tong Y, Palop JJ, Huang EJ, Ptacek LJ, Fu YH. 2013. Lamin B1 mediates cell-autonomous neuropathology in a leukodystrophy mouse model. J. Clin. Invest. 123:2719–2729. http://dx.doi.org/10.1172/JCI66737.
   PubMedGoogle Scholar
• Lin ST, Huang Y, Zhang L, Heng MY, Ptacek LJ, Fu YH. 2013. MicroRNA-23a promotes myelination in the central nervous system. Proc. Natl. Acad. Sci. U. S. A. 110:17468–17473. http://dx.doi.org/10.1073/pnas.1317182110.
   PubMed Web of Science ®Google Scholar
• Lin ST, Heng MY, Ptacek LJ, Fu YH. 2014. Regulation of Myelination in the central nervous system by nuclear lamin B1 and non-coding RNAs. Transl. Neurodegener. 3:4. http://dx.doi.org/10.1186/2047-9158-3-4.
   PubMedGoogle Scholar
• DeBusk FL. 1972. The Hutchinson-Gilford progeria syndrome. J. Pediatr. 80:697–724. http://dx.doi.org/10.1016/S0022-3476(72)80229-4.
   PubMed Web of Science ®Google Scholar
• Navarro CL, Cau P, Levy N. 2006. Molecular bases of progeroid syndromes. Hum. Mol. Genet. 15(Spec No 2):R151–R161. http://dx.doi.org/10.1093/hmg/ddl214.
   PubMedGoogle Scholar
• Martin GM. 1985. Genetics and aging; the Werner syndrome as a segmental progeroid syndrome. Adv. Exp. Med. Biol. 190:161–170. http://dx.doi.org/10.1007/978-1-4684-7853-2_5.
   PubMedGoogle Scholar
• Martin GM. 1982. Syndromes of accelerated aging. Natl. Cancer Inst. Monogr. 60:241–247.
   PubMedGoogle Scholar
• De Sandre-Giovannoli A, Bernard R, Cau P, Navarro C, Amiel J, Boccaccio I, Lyonnet S, Stewart CL, Munnich A, Le Merrer M, Lévy N. 2003. Lamin A truncation in Hutchinson-Gilford progeria. Science 300:2055. http://dx.doi.org/10.1126/science.1084125.
   PubMed Web of Science ®Google Scholar
• Yang SH, Andres DA, Spielmann HP, Young SG, Fong LG. 2008. Progerin elicits disease phenotypes of progeria in mice whether or not it is farnesylated. J. Clin. Invest. 118:3291–3300. http://dx.doi.org/10.1172/JCI35876.
   PubMed Web of Science ®Google Scholar
• Yang SH, Chang SY, Andres DA, Spielmann HP, Young SG, Fong LG. 2010. Assessing the efficacy of protein farnesyltransferase inhibitors in mouse models of progeria. J. Lipid Res. 51:400–405. http://dx.doi.org/10.1194/jlr.M002808.
   PubMed Web of Science ®Google Scholar
• Fong LG, Vickers TA, Farber EA, Choi C, Yun UJ, Hu Y, Yang SH, Coffinier C, Lee R, Yin L, Davies BS, Andres DA, Spielmann HP, Bennett CF, Young SG. 2009. Activating the synthesis of progerin, the mutant prelamin A in Hutchinson-Gilford progeria syndrome, with antisense oligonucleotides. Hum. Mol. Genet. 18:2462–2471. http://dx.doi.org/10.1093/hmg/ddp184.
   PubMed Web of Science ®Google Scholar
• Yang SH, Meta M, Qiao X, Frost D, Bauch J, Coffinier C, Majumdar S, Bergo MO, Young SG, Fong LG. 2006. A farnesyltransferase inhibitor improves disease phenotypes in mice with a Hutchinson-Gilford progeria syndrome mutation. J. Clin. Invest. 116:2115–2121. http://dx.doi.org/10.1172/JCI28968.
   PubMed Web of Science ®Google Scholar
• Nissan X, Blondel S, Navarro C, Maury Y, Denis C, Girard M, Martinat C, De Sandre-Giovannoli A, Levy N, Peschanski M. 2012. Unique preservation of neural cells in Hutchinson-Gilford progeria syndrome is due to the expression of the neural-specific miR-9 microRNA. Cell Rep. 2:1–9. http://dx.doi.org/10.1016/j.celrep.2012.05.015.
   PubMed Web of Science ®Google Scholar
• Bartel DP. 2009. MicroRNAs: target recognition and regulatory functions. Cell 136:215–233. http://dx.doi.org/10.1016/j.cell.2009.01.002.
   PubMed Web of Science ®Google Scholar
• Bushati N, Cohen SM. 2007. microRNA functions. Annu. Rev. Cell Dev. Biol. 23:175–205. http://dx.doi.org/10.1146/annurev.cellbio.23.090506.123406.
   PubMed Web of Science ®Google Scholar
• Gao FB. 2010. Context-dependent functions of specific microRNAs in neuronal development. Neural Dev. 5:25. http://dx.doi.org/10.1186/1749-8104-5-25.
   PubMedGoogle Scholar
• Coolen M, Bally-Cuif L. 2009. MicroRNAs in brain development and physiology. Curr. Opin. Neurobiol. 19:461–470. http://dx.doi.org/10.1016/j.conb.2009.09.006.
   PubMed Web of Science ®Google Scholar