Nucleoskeleton dynamics and functions in health and disease

References

• Lodish H, Berk A, Zipursky SL, Matsudaira P, Baltimore D, Darnell J. Molecular Cell Biology. 4th ed. New York: WH Freeman; 2000.
   Google Scholar
• Sperry AO. The dynamic cytoskeleton of the developing male germ cell. Biol Cell. 2012;104(5):297–305.
   Web of Science ®Google Scholar
• Fisher DZ, Chaudhary N, Blobel G. cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins. Proc Natl Acad Sci U S A. 1986;83(17):6450–6454.
   PubMed Web of Science ®Google Scholar
• Krohne G, Debus E, Osborn M, Weber K, Franke WW. A monoclonal antibody against nuclear lamina proteins reveals cell type-specificity in Xenopus laevis. Exp Cell Res. 1984;150(1):47–59.
   Web of Science ®Google Scholar
• Zackroff RV, Goldman AE, Jones JC, Steinert PM, Goldman RD. Isolation and characterization of keratin-like proteins from cultured cells with fibroblastic morphology. J Cell Biol. 1984;98(4):1231–1237.
   Web of Science ®Google Scholar
• Gerace L, Comeau C, Benson M. Organization and modulation of nuclear lamina structure. J Cell Sci Suppl. 1984;1:137–160.
   PubMedGoogle Scholar
• Aebi U, Cohn J, Buhle L, Gerace L. The nuclear lamina is a meshwork of intermediate-type filaments. Nature. 1986;323(6088):560–564.
   PubMed Web of Science ®Google Scholar
• Crisp M, Liu Q, Roux K, et al. Coupling of the nucleus and cytoplasm: role of the LINC complex. J Cell Biol. 2006;172(1):41–53.
   PubMed Web of Science ®Google Scholar
• Dreger M, Bengtsson L, Schoneberg T, Otto H, Hucho F. Nuclear envelope proteomics: novel integral membrane proteins of the inner nuclear membrane. Proc Natl Acad Sci U S A. 2001;98(21):11943–11948.
   Web of Science ®Google Scholar
• Schirmer EC, Florens L, Guan TL, Yates JR, Gerace L. Nuclear membrane proteins with potential disease links found by subtractive proteomics. Science. 2003;301(5638):1380–1382.
   PubMed Web of Science ®Google Scholar
• Korfali N, Wilkie GS, Swanson SK, et al. The leukocyte nuclear envelope proteome varies with cell activation and contains novel transmembrane proteins that affect genome architecture. Mol Cell Proteomics. 2010;9(12):2571–2585.
   PubMed Web of Science ®Google Scholar
• Wilkie GS, Korfali N, Swanson SK, et al. Several novel nuclear envelope transmembrane proteins identified in skeletal muscle have cytoskeletal associations. Mol Cell Proteomics. 2011;10(1):M110.003129.
   PubMed Web of Science ®Google Scholar
• Korfali N, Wilkie GS, Swanson SK, et al. The nuclear envelope proteome differs notably between tissues. Nucleus. 2012;3(6):552–564.
   PubMed Web of Science ®Google Scholar
• Dittmer TA, Sahni N, Kubben N, et al. Systematic identification of pathological lamin A interactors. Mol Biol Cell. 2014;25(9):1493–1510.
   PubMed Web of Science ®Google Scholar
• Zastrow MS, Vlcek S, Wilson KL. Proteins that bind A-type lamins: integrating isolated clues. J Cell Sci. 2004;117(pt 7):979–987.
   PubMed Web of Science ®Google Scholar
• Zuleger N, Robson MI, Schirmer EC. The nuclear envelope as a chromatin organizer. Nucleus. 2011;2(5):339–349.
   PubMed Web of Science ®Google Scholar
• Capell BC, Collins FS. Human laminopathies: nuclei gone genetically awry. Nat Rev Genet. 2006;7(12):940–952.
   PubMed Web of Science ®Google Scholar
• Meinke P, Nguyen TD, Wehnert MS. The LINC complex and human disease. Biochem Soc Trans. 2011;39:1693–1697.
   PubMed Web of Science ®Google Scholar
• de Las Heras JI, Meinke P, Batrakou DG, et al. Tissue specificity in the nuclear envelope supports its functional complexity. Nucleus. 2013;4(6):460–477.
   PubMed Web of Science ®Google Scholar
• Wilkie GS, Schirmer EC. Guilt by association: the nuclear envelope proteome and disease. Mol Cell Proteomics. 2006;5(10):1865–1875.
   Web of Science ®Google Scholar
• Fuchs E, Weber K. Intermediate filaments: structure, dynamics, function, and disease. Annu Rev Biochem. 1994;63:345–382.
   PubMed Web of Science ®Google Scholar
• Strelkov SV, Herrmann H, Aebi U. Molecular architecture of intermediate filaments. Bioessays. 2003;25(3):243–251.
   Web of Science ®Google Scholar
• Vikstrom KL, Lim SS, Goldman RD, Borisy GG. Steady-state dynamics of intermediate filament networks. J Cell Biol. 1992;118(1):121–129.
   Web of Science ®Google Scholar
• Okabe S, Hirokawa N. Dynamics of the neuronal microtubules and intermediate filaments studied by laser fluorescence photobleach recovery method and caged fluorescence UV photoactivation method. Mol Biol Cell. 1992;3:A2–A2.
   Web of Science ®Google Scholar
• Janmey PA, Euteneuer U, Traub P, Schliwa M. Viscoelastic properties of vimentin compared with other filamentous biopolymer networks. J Cell Biol. 1991;113(1):155–160.
   Web of Science ®Google Scholar
• Shen X, Ranallo R, Choi E, Wu C. Involvement of actin-related proteins in ATP-dependent chromatin remodeling. Mol Cell. 2003;12(1):147–155.
   Web of Science ®Google Scholar
• Belin BJ, Mullins RD. What we talk about when we talk about nuclear actin. Nucleus. 2013;4(4):291–297.
   PubMed Web of Science ®Google Scholar
• Wada A, Fukuda M, Mishima M, Nishida E. Nuclear export of actin: a novel mechanism regulating the subcellular localization of a major cytoskeletal protein. EMBO J. 1998;17(6):1635–1641.
   Web of Science ®Google Scholar
• Gerace L, Burke B. Functional organization of the nuclear envelope. Annu Rev Cell Biol. 1988;4:335–374.
   PubMedGoogle Scholar
• Peter M, Kitten GT, Lehner CF, et al. Cloning and sequencing of cDNA clones encoding chicken lamins A and B1 and comparison of the primary structures of vertebrate A- and B-type lamins. J Mol Biol. 1989;208(3):393–404.
   PubMed Web of Science ®Google Scholar
• Weber K, Plessmann U, Ulrich W. Cytoplasmic intermediate filament proteins of invertebrates are closer to nuclear lamins than are vertebrate intermediate filament proteins; sequence characterization of two muscle proteins of a nematode. EMBO J. 1989;8(11):3221–3227.
   Web of Science ®Google Scholar
• Loewinger L, McKeon F. Mutations in the nuclear lamin proteins resulting in their aberrant assembly in the cytoplasm. EMBO J. 1988;7(8):2301–2309.
   Web of Science ®Google Scholar
• Lazebnik YA, Takahashi A, Moir RD, et al. Studies of the lamin proteinase reveal multiple parallel biochemical pathways during apoptotic execution. Proc Natl Acad Sci U S A. 1995;92(20):9042–9046.
   PubMed Web of Science ®Google Scholar
• Holtz D, Tanaka RA, Hartwig J, McKeon F. The CaaX motif of lamin A functions in conjunction with the nuclear localization signal to target assembly to the nuclear envelope. Cell. 1989;59(6):969–977.
   Web of Science ®Google Scholar
• Nigg EA, Kitten GT, Vorburger K. Targeting lamin proteins to the nuclear envelope: the role of CaaX box modifications. Biochem Soc Trans. 1992;20(2):500–504.
   Web of Science ®Google Scholar
• Mical TI, Monteiro MJ. The role of sequences unique to nuclear intermediate filaments in the targeting and assembly of human lamin B: evidence for lack of interaction of lamin B with its putative receptor. J Cell Sci. 1998;111:3471–3485.
   Web of Science ®Google Scholar
• Monteiro MJ, Hicks C, Gu L, Janicki S. Determinants for intracellular sorting of cytoplasmic and nuclear intermediate filaments. J Cell Biol. 1994;127(5):1327–1343.
   Web of Science ®Google Scholar
• Broers JL, de Leij L, Rot MK, et al. Expression of intermediate filament proteins in fetal and adult human lung tissues. Differentiation. 1989;40(2):119–128.
   Web of Science ®Google Scholar
• Jansen MP, Machiels BM, Hopman AH, et al. Comparison of A and B-type lamin expression in reactive lymph nodes and nodular sclerosing Hodgkin’s disease. Histopathology. 1997;31(4):304–312.
   Web of Science ®Google Scholar
• Broers JL, Ramaekers FC. Dynamics of nuclear lamina assembly and disassembly. Symp Soc Exp Biol. 2004;56:177–192.
   Google Scholar
• Machiels BM, Zorenc AH, Endert JM, et al. An alternative splicing product of the lamin A/C gene lacks exon 10. J Biol Chem. 1996;271(16):9249–9253.
   Web of Science ®Google Scholar
• Alsheimer M, Benavente R. Change of karyoskeleton during mammalian spermatogenesis: expression pattern of nuclear lamin C2 and its regulation. Exp Cell Res. 1996;228(2):181–188.
   PubMed Web of Science ®Google Scholar
• Furukawa K, Hotta Y. 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. 1993;12(1):97–106.
   PubMed Web of Science ®Google Scholar
• Letai A, Fuchs E. The importance of intramolecular ion pairing in intermediate filaments. Proc Natl Acad Sci U S A. 1995;92(1):92–96.
   Web of Science ®Google Scholar
• Schirmer EC, Gerace L. The stability of the nuclear lamina polymer changes with the composition of lamin subtypes according to their individual binding strengths. J Biol Chem. 2004;279(41):42811–42817.
   Web of Science ®Google Scholar
• Panorchan P, Wirtz D, Tseng Y. Structure-function relationship of biological gels revealed by multiple-particle tracking and differential interference contrast microscopy: the case of human lamin networks. Phys Rev E Stat Nonlin Soft Matter Phys. 2004;70(4 pt 1):27.
   Web of Science ®Google Scholar
• Lammerding J. Mechanics of the nucleus. Compr Physiol. 2011;1(2):783–807.
   PubMed Web of Science ®Google Scholar
• Isermann P, Lammerding J. Nuclear mechanics and mechanotransduction in health and disease. Curr Biol. 2013;23(24):009.
   Web of Science ®Google Scholar
• von Moeller F, Barendziak T, Apte K, Goldberg MW, Stick R. Molecular characterization of Xenopus lamin LIV reveals differences in the lamin composition of sperms in amphibians and mammals. Nucleus. 2010;1(1):85–95.
   PubMed Web of Science ®Google Scholar
• Shimi T, Pfleghaar K, Kojima S, et al. The A- and B-type nuclear lamin networks: microdomains involved in chromatin organization and transcription. Genes Dev. 2008;22(24):3409–3421.
   PubMed Web of Science ®Google Scholar
• Delbarre E, Tramier M, Coppey-Moisan M, Gaillard C, Courvalin JC, Buendia B. The truncated prelamin A in Hutchinson-Gilford progeria syndrome alters segregation of A-type and B-type lamin homopolymers. Hum Mol Genet. 2006;15(7):1113–1122.
   Web of Science ®Google Scholar
• Schirmer EC, Guan T, Gerace L. Involvement of the lamin rod domain in heterotypic lamin interactions important for nuclear organization. J Cell Biol. 2001;153(3):479–489.
   Web of Science ®Google Scholar
• Lutz RJ, Trujillo MA, Denham KS, Wenger L, Sinensky M. Nucleoplasmic localization of prelamin A: implications for prenylation-dependent lamin A assembly into the nuclear lamina. Proc Natl Acad Sci U S A. 1992;89(7):3000–3004.
   Web of Science ®Google Scholar
• Firmbach-Kraft I, Stick R. The role of CaaX-dependent modifications in membrane association of Xenopus nuclear lamin B3 during meiosis and the fate of B3 in transfected mitotic cells. J Cell Biol. 1993;123(6 pt 2):1661–1670.
   Web of Science ®Google Scholar
• Young SG, Fong LG, Michaelis S. Prelamin A, Zmpste24, misshapen cell nuclei, and progeria – new evidence suggesting that protein farnesylation could be important for disease pathogenesis. J Lipid Res. 2005;46(12):2531–2558.
   PubMed Web of Science ®Google Scholar
• Navarro CL, Esteves-Vieira V, Courrier S, et al. New ZMPSTE24 (FACE1) mutations in patients affected with restrictive dermopathy or related progeroid syndromes and mutation update. Eur J Hum Genet. 2014;22(8):1002–1011.
   Web of Science ®Google Scholar
• Maniotis AJ, Chen CS, Ingber DE. Demonstration of mechanical connections between integrins, cytoskeletal filaments, and nucleoplasm that stabilize nuclear structure. Proc Natl Acad Sci U S A. 1997;94(3):849–854.
   PubMed Web of Science ®Google Scholar
• Ingber DE. Tensegrity: the architectural basis of cellular mechanotransduction. Annu Rev Physiol. 1997;59:575–599.
   PubMed Web of Science ®Google Scholar
• Mejat A, Misteli T. LINC complexes in health and disease. Nucleus. 2010;1(1):40–52.
   PubMed Web of Science ®Google Scholar
• Padmakumar VC, Libotte T, Lu W, et al. The inner nuclear membrane protein Sun1 mediates the anchorage of Nesprin-2 to the nuclear envelope. J Cell Sci. 2005;118(pt 15):3419–3430.
   PubMed Web of Science ®Google Scholar
• Stewart-Hutchinson PJ, Hale CM, Wirtz D, Hodzic D. Structural requirements for the assembly of LINC complexes and their function in cellular mechanical stiffness. Exp Cell Res. 2008;314(8):1892–1905.
   Web of Science ®Google Scholar
• Burke B, Roux KJ. Nuclei take a position: managing nuclear location. Dev Cell. 2009;17(5):587–597.
   Web of Science ®Google Scholar
• Padmakumar VC, Abraham S, Braune S, et al. Enaptin, a giant actin-binding protein, is an element of the nuclear membrane and the actin cytoskeleton. Exp Cell Res. 2004;295(2):330–339.
   Web of Science ®Google Scholar
• Zhang Q, Ragnauth C, Greener MJ, Shanahan CM, Roberts RG. The nesprins are giant actin-binding proteins, orthologous to Drosophila melanogaster muscle protein MSP-300. Genomics. 2002;80(5):473–481.
   Web of Science ®Google Scholar
• Zhen YY, Libotte T, Munck M, Noegel AA, Korenbaum E. NUANCE, a giant protein connecting the nucleus and actin cytoskeleton. J Cell Sci. 2002;115(pt 15):3207–3222.
   Web of Science ®Google Scholar
• Wilhelmsen K, Litjens SH, Kuikman I, et al. Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin. J Cell Biol. 2005;171(5):799–810.
   PubMed Web of Science ®Google Scholar
• Roux KJ, Crisp ML, Liu Q, et al. Nesprin 4 is an outer nuclear membrane protein that can induce kinesin-mediated cell polarization. Proc Natl Acad Sci U S A. 2009;106(7):2194–2199.
   Web of Science ®Google Scholar
• Morimoto A, Shibuya H, Zhu X, et al. A conserved KASH domain protein associates with telomeres, SUN1, and dynactin during mammalian meiosis. J Cell Biol. 2012;198(2):165–172.
   PubMed Web of Science ®Google Scholar
• Lu W, Schneider M, Neumann S, et al. Nesprin interchain associations control nuclear size. Cell Mol Life Sci. 2012;69(20):3493–3509.
   Web of Science ®Google Scholar
• Lombardi ML, Zwerger M, Lammerding J. Biophysical assays to probe the mechanical properties of the interphase cell nucleus: substrate strain application and microneedle manipulation. J Vis Exp. 2011;(55):ii:3087.
   Web of Science ®Google Scholar
• Khatau SB, Bloom RJ, Bajpai S, et al. The distinct roles of the nucleus and nucleus-cytoskeleton connections in three-dimensional cell migration. Sci Rep. 2012;2(488):3.
   Google Scholar
• Sullivan T, Escalante-Alcalde D, Bhatt H, et al. Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy. J Cell Biol. 1999;147(5):913–920.
   PubMed Web of Science ®Google Scholar
• Lammerding J, Schulze PC, Takahashi T, et al. Lamin A/C deficiency causes defective nuclear mechanics and mechanotransduction. J Clin Invest. 2004;113(3):370–378.
   PubMed Web of Science ®Google Scholar
• Broers JL, Peeters EA, Kuijpers HJ, et al. Decreased mechanical stiffness in LMNA-/- cells is caused by defective nucleo-cytoskeletal integrity: implications for the development of laminopathies. Hum Mol Genet. 2004;13(21):2567–2580.
   PubMed Web of Science ®Google Scholar
• Duong NT, Morris GE, Lam le T, et al. Nesprins: tissue-specific expression of epsilon and other short isoforms. PLoS One. 2014;9(4):e94380.
   PubMed Web of Science ®Google Scholar
• Mattout-Drubezki A, Gruenbaum Y. Dynamic interactions of nuclear lamina proteins with chromatin and transcriptional machinery. Cell Mol Life Sci. 2003;60(10):2053–2063.
   PubMed Web of Science ®Google Scholar
• Gudise S, Figueroa RA, Lindberg R, Larsson V, Hallberg E. Samp1 is functionally associated with the LINC complex and A-type lamina networks. J Cell Sci. 2011;124(pt 12):2077–2085.
   Web of Science ®Google Scholar
• Borrego-Pinto J, Jegou T, Osorio DS, et al. Samp1 is a component of TAN lines and is required for nuclear movement. J Cell Sci. 2012;125(pt 5):1099–1105.
   Web of Science ®Google Scholar
• Buch C, Lindberg R, Figueroa R, Gudise S, Onischenko E, Hallberg E. An integral protein of the inner nuclear membrane localizes to the mitotic spindle in mammalian cells. J Cell Sci. 2009;122(pt 12):2100–2107.
   Web of Science ®Google Scholar
• Shoeman RL, Traub P. The in vitro DNA-binding properties of purified nuclear lamin proteins and vimentin. J Biol Chem. 1990;265(16):9055–9061.
   Web of Science ®Google Scholar
• Glass JR, Gerace L. Lamins A and C bind and assemble at the surface of mitotic chromosomes. J Cell Biol. 1990;111(3):1047–1057.
   Web of Science ®Google Scholar
• Taniura H, Glass C, Gerace L. A chromatin binding site in the tail domain of nuclear lamins that interacts with core histones. J Cell Biol. 1995;131(1):33–44.
   PubMed Web of Science ®Google Scholar
• Goldberg M, Harel A, Brandeis M, et al. The tail domain of lamin Dm0 binds histones H2A and H2B. Proc Natl Acad Sci U S A. 1999;96(6):2852–2857.
   Web of Science ®Google Scholar
• Dechat T, Adam SA, Taimen P, Shimi T, Goldman RD. Nuclear lamins. Cold Spring Harb Perspect Biol. 2010;2(11):8.
   Web of Science ®Google Scholar
• Lund E, Oldenburg AR, Delbarre E, et al. Lamin A/C-promoter interactions specify chromatin state-dependent transcription outcomes. Genome Res. 2013;23(10):1580–1589.
   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(5):593–603.
   Web of Science ®Google Scholar
• Puckelwartz MJ, Depreux FF, McNally EM. Gene expression, chromosome position and lamin A/C mutations. Nucleus. 2011;2(3):162–167.
   PubMed Web of Science ®Google Scholar
• Polioudaki H, Kourmouli N, Drosou V, et al. Histones H3/H4 form a tight complex with the inner nuclear membrane protein LBR and heterochromatin protein 1. EMBO Rep. 2001;2(10):920–925.
   Web of Science ®Google Scholar
• Makatsori D, Kourmouli N, Polioudaki H, et al. The inner nuclear membrane protein lamin B receptor forms distinct microdomains and links epigenetically marked chromatin to the nuclear envelope. J Biol Chem. 2004;279(24):25567–25573.
   PubMed Web of Science ®Google Scholar
• Ye Q, Worman HJ. Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1. J Biol Chem. 1996;271(25):14653–14656.
   PubMed Web of Science ®Google Scholar
• Nili E, Cojocaru GS, Kalma Y, et al. Nuclear membrane protein LAP2beta mediates transcriptional repression alone and together with its binding partner GCL (germ-cell-less). J Cell Sci. 2001;114(pt 18):3297–3307.
   Web of Science ®Google Scholar
• Somech R, Shaklai S, Geller O, et al. The nuclear-envelope protein and transcriptional repressor LAP2beta interacts with HDAC3 at the nuclear periphery, and induces histone H4 deacetylation. J Cell Sci. 2005;118(pt 17):4017–4025.
   Web of Science ®Google Scholar
• Demmerle J, Koch AJ, Holaska JM. The nuclear envelope protein emerin binds directly to histone deacetylase 3 (HDAC3) and activates HDAC3 activity. J Biol Chem. 2012;287(26):22080–22088.
   Web of Science ®Google Scholar
• Lee KK, Haraguchi T, Lee RS, Koujin T, Hiraoka Y, Wilson KL. Distinct functional domains in emerin bind lamin A and DNA-bridging protein BAF. J Cell Sci. 2001;114(pt 24):4567–4573.
   Web of Science ®Google Scholar
• Haraguchi T, Holaska JM, Yamane M, et al. Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery-Dreifuss muscular dystrophy. Eur J Biochem. 2004;271(5):1035–1045.
   Google Scholar
• Holaska JM, Rais-Bahrami S, Wilson KL. Lmo7 is an emerin-binding protein that regulates the transcription of emerin and many other muscle-relevant genes. Hum Mol Genet. 2006;15(23):3459–3472.
   PubMed Web of Science ®Google Scholar
• Zuleger N, Boyle S, Kelly DA, et al. Specific nuclear envelope transmembrane proteins can promote the location of chromosomes to and from the nuclear periphery. Genome Biol. 2013;14(2):2013–2014.
   Web of Science ®Google Scholar
• Solovei I, Wang AS, Thanisch K, et al. LBR and lamin A/C sequentially tether peripheral heterochromatin and inversely regulate differentiation. Cell. 2013;152(3):584–598.
   PubMed Web of Science ®Google Scholar
• Zullo JM, Demarco IA, Piqué-Regi R, et al. DNA sequence-dependent compartmentalization and silencing of chromatin at the nuclear lamina. Cell. 2012;149(7):1474–1487.
   PubMed Web of Science ®Google Scholar
• Kumaran RI, Muralikrishna B, Parnaik VK. Lamin A/C speckles mediate spatial organization of splicing factor compartments and RNA polymerase II transcription. J Cell Biol. 2002;159(5):783–793.
   Web of Science ®Google Scholar
• Moir RD, Spann TP, Herrmann H, Goldman RD. Disruption of nuclear lamin organization blocks the elongation phase of DNA replication. J Cell Biol. 2000;149(6):1179–1192.
   PubMed Web of Science ®Google Scholar
• Singh M, Hunt CR, Pandita RK, et al. Lamin A/C depletion enhances DNA damage-induced stalled replication fork arrest. Mol Cell Biol. 2013;33(6):1210–1222.
   PubMed Web of Science ®Google Scholar
• Lei K, Zhu X, Xu R, et al. Inner nuclear envelope proteins SUN1 and SUN2 play a prominent role in the DNA damage response. Curr Biol. 2012;22(17):1609–1615.
   Web of Science ®Google Scholar
• Alberts BJA, Lewis J, et al. Molecular Biology of the Cell. 4th ed. New York: Garland Science; 2002.
   Google Scholar
• Wang N, Tytell JD, Ingber DE. Mechanotransduction at a distance: mechanically coupling the extracellular matrix with the nucleus. Nat Rev Mol Cell Biol. 2009;10(1):75–82.
   PubMed Web of Science ®Google Scholar
• Chambliss AB, Khatau SB, Erdenberger N, et al. The LINC-anchored actin cap connects the extracellular milieu to the nucleus for ultrafast mechanotransduction. Sci Rep. 2013;3(1087):18.
   Google Scholar
• Ho CY, Jaalouk DE, Vartiainen MK, Lammerding J. Lamin A/C and emerin regulate MKL1-SRF activity by modulating actin dynamics. Nature. 2013;497(7450):507–511.
   PubMed Web of Science ®Google Scholar
• Markiewicz E, Tilgner K, Barker N, et al. The inner nuclear membrane protein emerin regulates beta-catenin activity by restricting its accumulation in the nucleus. EMBO J. 2006;25(14):3275–3285.
   Web of Science ®Google Scholar
• Pan D, Estévez-Salmerón LD, Stroschein SL, et al. The integral inner nuclear membrane protein MAN1 physically interacts with the R-Smad proteins to repress signaling by the transforming growth factor-{beta} superfamily of cytokines. J Biol Chem. 2005;280(16):15992–16001.
   Web of Science ®Google Scholar
• Osada S, Ohmori SY, Taira M. XMAN1, an inner nuclear membrane protein, antagonizes BMP signaling by interacting with Smad1 in Xenopus embryos. Development. 2003;130(9):1783–1794.
   Google Scholar
• Muchir A, Pavlidis P, Bonne G, Hayashi YK, Worman HJ. Activation of MAPK in hearts of EMD null mice: similarities between mouse models of X-linked and autosomal dominant Emery Dreifuss muscular dystrophy. Hum Mol Genet. 2007;16(15):1884–1895.
   PubMed Web of Science ®Google Scholar
• Muchir A, Wu W, Worman HJ. Reduced expression of A-type lamins and emerin activates extracellular signal-regulated kinase in cultured cells. Biochim Biophys Acta. 2009;1:75–81.
   Google Scholar
• Worman HJ. Nuclear lamins and laminopathies. J Pathol. 2012;226(2):316–325.
   PubMed Web of Science ®Google Scholar
• Hutchison CJ, Alvarez-Reyes M, Vaughan OA. Lamins in disease: why do ubiquitously expressed nuclear envelope proteins give rise to tissue-specific disease phenotypes? J Cell Sci. 2001;114(pt 1):9–19.
   Web of Science ®Google Scholar
• Hutchison CJ, Worman HJ. A-type lamins: guardians of the soma? Nat Cell Biol. 2004;6(11):1062–1067.
   Web of Science ®Google Scholar
• Bonne G, Di Barletta MR, Varnous S, et al. Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy. Nat Genet. 1999;21(3):285–288.
   PubMed Web of Science ®Google Scholar
• Muchir A, Bonne G, van der Kooi AJ, et al. Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B). Hum Mol Genet. 2000;9(9):1453–1459.
   PubMed Web of Science ®Google Scholar
• Quijano-Roy S, Mbieleu B, Bönnemann CG, et al. De novo LMNA mutations cause a new form of congenital muscular dystrophy. Ann Neurol. 2008;64(2):177–186.
   PubMed Web of Science ®Google Scholar
• De Sandre-Giovannoli A, Chaouch M, Kozlov S, et al. Homozygous defects in LMNA, encoding lamin A/C nuclear-envelope proteins, cause autosomal recessive axonal neuropathy in human (Charcot-Marie-Tooth disorder type 2) and mouse. Am J Hum Genet. 2002;70(3):726–736.
   PubMed Web of Science ®Google Scholar
• Navarro CL, De Sandre-Giovannoli A, Bernard R, et al. Lamin A and ZMPSTE24 (FACE-1) defects cause nuclear disorganization and identify restrictive dermopathy as a lethal neonatal laminopathy. Hum Mol Genet. 2004;13(20):2493–2503.
   Web of Science ®Google Scholar
• Cao H, Hegele RA. Nuclear lamin A/C R482Q mutation in Canadian kindreds with Dunnigan-type familial partial lipodystrophy. Hum Mol Genet. 2000;9(1):109–112.
   PubMed Web of Science ®Google Scholar
• Shackleton S, Lloyd DJ, Jackson SN, et al. LMNA, encoding lamin A/C, is mutated in partial lipodystrophy. Nat Genet. 2000;24(2):153–156.
   PubMed Web of Science ®Google Scholar
• Emery AE, Dreifuss FE. Unusual type of benign x-linked muscular dystrophy. J Neurol Neurosurg Psychiatry. 1966;29(4):338–342.
   Web of Science ®Google Scholar
• Bacon PA, Smith B. Familial muscular dystrophy of late onset. J Neurol Neurosurg Psychiatry. 1971;34(1):93–97.
   Web of Science ®Google Scholar
• Levitas A, Muhammad E, Harel G, et al. Familial neonatal isolated cardiomyopathy caused by a mutation in the flavoprotein subunit of succinate dehydrogenase. Eur J Hum Genet. 2010;18(10):1160–1165.
   PubMed Web of Science ®Google Scholar
• Schirmer EC, Foisner R. Proteins that associate with lamins: many faces, many functions. Exp Cell Res. 2007;313(10):2167–2179.
   PubMed Web of Science ®Google Scholar
• Meinke P, Mattioli E, Haque F, et al. Muscular dystrophy-associated SUN1 and SUN2 variants disrupt nuclear-cytoskeletal connections and myonuclear organization. PLoS Genet. 2014;10(9):e1004605.
   PubMed Web of Science ®Google Scholar
• Liang WC, Mitsuhashi H, Keduka E, et al. TMEM43 mutations in Emery-Dreifuss muscular dystrophy-related myopathy. Ann Neurol. 2011;69(6):1005–1013.
   PubMed Web of Science ®Google Scholar
• Bione S, Maestrini E, Rivella S, et al. Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy. Nat Genet. 1994;8(4):323–327.
   PubMed Web of Science ®Google Scholar
• Zhang Q, Bethmann C, Worth NF, et al. Nesprin-1 and -2 are involved in the pathogenesis of Emery Dreifuss muscular dystrophy and are critical for nuclear envelope integrity. Hum Mol Genet. 2007;16(23):2816–2833.
   PubMed Web of Science ®Google Scholar
• Clements L, Manilal S, Love DR, Morris GE. Direct interaction between emerin and lamin A. Biochem Biophys Res Commun. 2000;267(3):709–714.
   Web of Science ®Google Scholar
• Wiesel N, Mattout A, Melcer S, et al. Laminopathic mutations interfere with the assembly, localization, and dynamics of nuclear lamins. Proc Natl Acad Sci U S A. 2008;105(1):180–185.
   PubMed Web of Science ®Google Scholar
• Melcon G, Kozlov S, Cutler DA, et al. Loss of emerin at the nuclear envelope disrupts the Rb1/E2F and MyoD pathways during muscle regeneration. Hum Mol Genet. 2006;15(4):637–651.
   Web of Science ®Google Scholar
• Mattout A, Pike BL, Towbin BD, et al. An EDMD mutation in C. elegans lamin blocks muscle-specific gene relocation and compromises muscle integrity. Curr Biol. 2011;21(19):1603–1614.
   PubMed Web of Science ®Google Scholar
• Li P, Meinke P, Huong Le TT, Wehnert M, Noegel AA. Contribution of SUN1 mutations to the pathomechanism in muscular dystrophies. Hum Mutat. 2014;35(4):452–461.
   Web of Science ®Google Scholar
• Taranum S, Vaylann E, Meinke P, et al. LINC complex alterations in DMD and EDMD/CMT fibroblasts. Eur J Cell Biol. 2012;91(8):614–628.
   Web of Science ®Google Scholar
• Muntoni F, Bonne G, Goldfarb LG, et al. Disease severity in dominant Emery Dreifuss is increased by mutations in both emerin and desmin proteins. Brain. 2006;129(pt 5):1260–1268.
   Google Scholar
• Gundesli H, Talim B, Korkusuz P, et al. Mutation in exon 1f of PLEC, leading to disruption of plectin isoform 1f, causes autosomal-recessive limb-girdle muscular dystrophy. Am J Hum Genet. 2010;87(6):834–841.
   PubMed Web of Science ®Google Scholar
• Cetin N, Balci-Hayta B, Gundesli H, et al. A novel desmin mutation leading to autosomal recessive limb-girdle muscular dystrophy: distinct histopathological outcomes compared with desminopathies. J Med Genet. 2013;50(7):437–443.
   Web of Science ®Google Scholar
• Hackman P, Vihola A, Haravuori H, et al. Tibial muscular dystrophy is a titinopathy caused by mutations in TTN, the gene encoding the giant skeletal-muscle protein titin. Am J Hum Genet. 2002;71(3):492–500.
   Web of Science ®Google Scholar
• Hayashi YK, Chou FL, Engvall E, et al. Mutations in the integrin alpha7 gene cause congenital myopathy. Nat Genet. 1998;19(1):94–97.
   Web of Science ®Google Scholar
• Hoffmann K, Dreger CK, Olins AL, et al. Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger-Huet anomaly). Nat Genet. 2002;31(4):410–414.
   PubMed Web of Science ®Google Scholar
• Olins AL, Hoang TV, Zwerger M, et al. The LINC-less granulocyte nucleus. Eur J Cell Biol. 2009;88(4):203–214.
   Web of Science ®Google Scholar
• Horn HF, Brownstein Z, Lenz DR, et al. The LINC complex is essential for hearing. J Clin Invest. 2013;123(2):740–750.
   Web of Science ®Google Scholar
• Muchir A, Shan J, Bonne G, Lehnart SE, Worman HJ. Inhibition of extracellular signal-regulated kinase signaling to prevent cardiomyopathy caused by mutation in the gene encoding A-type lamins. Hum Mol Genet. 2009;18(2):241–247.
   PubMed Web of Science ®Google Scholar
• Muchir A, Pavlidis P, Decostre V, et al. Activation of MAPK pathways links LMNA mutations to cardiomyopathy in Emery-Dreifuss muscular dystrophy. J Clin Invest. 2007;117(5):1282–1293.
   PubMed Web of Science ®Google Scholar
• Eriksson M, Brown WT, Gordon LB, et al. Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome. Nature. 2003;423(6937):293–298.
   PubMed Web of Science ®Google Scholar
• De Sandre-Giovannoli A, Bernard R, Cau P, et al. Lamin a truncation in Hutchinson-Gilford progeria. Science. 2003;300(5628):17.
   Web of Science ®Google Scholar
• Agarwal AK, Fryns JP, Auchus RJ, Garg A. Zinc metalloproteinase, ZMPSTE24, is mutated in mandibuloacral dysplasia. Hum Mol Genet. 2003;12(16):1995–2001.
   PubMed Web of Science ®Google Scholar
• Hennekam RC. Hutchinson-Gilford progeria syndrome: review of the phenotype. Am J Med Genet A. 2006;140(23):2603–2624.
   PubMed Web of Science ®Google Scholar
• Liu B, Wang J, Chan KM, et al. Genomic instability in laminopathy-based premature aging. Nat Med. 2005;11(7):780–785.
   PubMed Web of Science ®Google Scholar
• Musich PR, Zou Y. Genomic instability and DNA damage responses in progeria arising from defective maturation of prelamin A. Aging (Albany N Y). 2009;1(1):28–37.
   Google Scholar
• Gonzalez-Suarez I, Redwood AB, Perkins SM, et al. Novel roles for A-type lamins in telomere biology and the DNA damage response pathway. EMBO J. 2009;28(16):2414–2427.
   PubMed Web of Science ®Google Scholar
• Puente XS, Quesada V, Osorio FG, et al. Exome sequencing and functional analysis identifies BANF1 mutation as the cause of a hereditary progeroid syndrome. Am J Hum Genet. 2011;88(5):650–656.
   PubMed Web of Science ®Google Scholar
• Madej-Pilarczyk A, Kmieć T, Fidziańska A, et al. Progeria caused by a rare LMNA mutation p.S143F associated with mild myopathy and atrial fibrillation. Eur J Paediatr Neurol. 2008;12(5):427–430.
   Web of Science ®Google Scholar
• Starke S, Meinke P, Camozzi D, et al. Progeroid laminopathy with restrictive dermopathy-like features caused by an isodisomic LMNA mutation p.R435C. Aging. 2013;5(6):445–459.
   Google Scholar
• Padiath QS, Saigoh K, Schiffmann R, et al. Lamin B1 duplications cause autosomal dominant leukodystrophy. Nat Genet. 2006;38(10):1114–1123.
   PubMed Web of Science ®Google Scholar
• Hegele RA, Cao H, Liu DM, et al. Sequencing of the reannotated LMNB2 gene reveals novel mutations in patients with acquired partial lipodystrophy. Am J Hum Genet. 2006;79(2):383–389.
   Web of Science ®Google Scholar
• Kuzmina SN, Buldyaeva TV, Akopov SB, Zbarsky IB. Protein patterns of the nuclear matrix in differently proliferating and malignant cells. Mol Cell Biochem. 1984;58(1–2):183–186.
   Web of Science ®Google Scholar
• Broers JL, Ramaekers FC. The role of the nuclear lamina in cancer and apoptosis. Adv Exp Med Biol. 2014;773:27–48.
   PubMed Web of Science ®Google Scholar
• Neumann S, Noegel AA. Nesprins in cell stability and migration. Adv Exp Med Biol. 2014;773:491–504.
   Web of Science ®Google Scholar
• Hutchison CJ. Do lamins influence disease progression in cancer? Adv Exp Med Biol. 2014;773:593–604.
   Web of Science ®Google Scholar
• Daniele N, Richard I, Bartoli M. Ins and outs of therapy in limb girdle muscular dystrophies. Int J Biochem Cell Biol. 2007;39(9):1608–1624.
   Web of Science ®Google Scholar
• Scharner J, Gnocchi VF, Ellis JA, Zammit PS. Genotype-phenotype correlations in laminopathies: how does fate translate? Biochem Soc Trans. 2010;38(pt 1):257–262.
   PubMed Web of Science ®Google Scholar
• Wu W, Muchir A, Shan J, Bonne G, Worman HJ. Mitogen-activated protein kinase inhibitors improve heart function and prevent fibrosis in cardiomyopathy caused by mutation in lamin A/C gene. Circulation. 2011;123(1):53–61.
   PubMed Web of Science ®Google Scholar
• Muchir A, Kim YJ, Reilly SA, Wu W, Choi JC, Worman HJ. Inhibition of extracellular signal-regulated kinase 1/2 signaling has beneficial effects on skeletal muscle in a mouse model of Emery-Dreifuss muscular dystrophy caused by lamin A/C gene mutation. Skelet Muscle. 2013;3(1):17.
   Google Scholar
• Gordon LB, Kleinman ME, Miller DT, et al. Clinical trial of a farnesyltransferase inhibitor in children with Hutchinson-Gilford progeria syndrome. Proc Natl Acad Sci U S A. 2012;109(41):16666–16671.
   PubMed Web of Science ®Google Scholar
• Larrieu D, Britton S, Demir M, Rodriguez R, Jackson SP. Chemical inhibition of NAT10 corrects defects of laminopathic cells. Science. 2014;344(6183):527–532.
   PubMed Web of Science ®Google Scholar
• Swift J, Ivanovska IL, Buxboim A, et al. Nuclear lamin-A scales with tissue stiffness and enhances matrix-directed differentiation. Science. 2013;341(6149):1240104.
   PubMed Web of Science ®Google Scholar
• Raffaele Di Barletta M, Ricci E, Galluzzi G, et al. Different mutations in the LMNA gene cause autosomal dominant and autosomal recessive Emery-Dreifuss muscular dystrophy. Am J Hum Genet. 2000;66(4):1407–1412.
   Web of Science ®Google Scholar
• Fatkin D, MacRae C, Sasaki T, et al. Missense mutations in the rod domain of the lamin A/C gene as causes of dilated cardiomyopathy and conduction-system disease. N Engl J Med. 1999;341(23):1715–1724.
   PubMed Web of Science ®Google Scholar
• Renou L, Stora S, Yaou RB, et al. Heart-hand syndrome of Slovenian type: a new kind of laminopathy. J Med Genet. 2008;45(10):666–671.
   PubMed Web of Science ®Google Scholar
• Chen L, Lee L, Kudlow BA, et al. LMNA mutations in atypical Werner’s syndrome. Lancet. 2003;362(9382):440–445.
   PubMed Web of Science ®Google Scholar
• Novelli G, Muchir A, Sangiuolo F, et al. Mandibuloacral dysplasia is caused by a mutation in LMNA-encoding lamin A/C. Am J Hum Genet. 2002;71(2):426–431.
   PubMed Web of Science ®Google Scholar
• Waterham HR, Koster J, Mooyer P, et al. Autosomal recessive HEM/Greenberg skeletal dysplasia is caused by 3 beta-hydroxysterol delta 14-reductase deficiency due to mutations in the lamin B receptor gene. Am J Hum Genet. 2003;72(4):1013–1017.
   PubMed Web of Science ®Google Scholar
• Gros-Louis F, Dupré N, Dion P, et al. Mutations in SYNE1 lead to a newly discovered form of autosomal recessive cerebellar ataxia. Nat Genet. 2007;39(1):80–85.
   PubMed Web of Science ®Google Scholar
• Hellemans J, Preobrazhenska O, Willaert A, et al. Loss-of-function mutations in LEMD3 result in osteopoikilosis, Buschke-Ollendorff syndrome and melorheostosis. Nat Genet. 2004;36(11):1213–1218.
   PubMed Web of Science ®Google Scholar
• Debeer P, Pykels E, Lammens J, Devriendt K, Fryns JP. Melorheostosis in a family with autosomal dominant osteopoikilosis: report of a third family. Am J Med Genet A. 2003;1(2):188–193.
   Google Scholar
• Merner ND, Hodgkinson KA, Haywood AF, et al. Arrhythmogenic right ventricular cardiomyopathy type 5 is a fully penetrant, lethal arrhythmic disorder caused by a missense mutation in the TMEM43 gene. Am J Hum Genet. 2008;82(4):809–821.
   PubMed Web of Science ®Google Scholar
• Kayman-Kurekci G, Talim B, Korkusuz P, et al. Mutation in TOR1AIP1 encoding LAP1B in a form of muscular dystrophy: a novel gene related to nuclear envelopathies. Neuromuscul Disord. 2014;24(7):624–633.
   PubMed Web of Science ®Google Scholar
• Taylor MR, Slavov D, Gajewski A, et al; Familial Cardiomyopathy Registry Research Group. Thymopoietin (lamina-associated polypeptide 2) gene mutation associated with dilated cardiomyopathy. Hum Mutat. 2005;26(6):566–574.
   PubMed Web of Science ®Google Scholar
• Ichida F, Tsubata S, Bowles KR, et al. Novel gene mutations in patients with left ventricular noncompaction or Barth syndrome. Circulation. 2001;103(9):1256–1263.
   PubMed Web of Science ®Google Scholar