Abstract
Double-membrane-bound nucleus is the major organelle of every metazoan cell, which controls various nuclear processes like chromatin maintenance, DNA replication, transcription and nucleoskeleton-cytoskeleton coupling. Nuclear homeostasis depends on the integrity of nuclear membrane and associated proteins. Lamins, underlying the inner nuclear membrane (INM), play a crucial role in maintaining nuclear homeostasis. In this review, we have focussed on the disruption of nuclear homeostasis due to lamin A/C mutation which produces a plethora of diseases, termed as laminopathies.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Al-Haboubi T, Shumaker DK, Koser J, Wehnert M, Fahrenkrog B (2011) Distinct association of the nuclear pore protein Nup153 with A- and B-type lamins. Nucleus 2:500–509
Clayton P, Fischer B, Mann A, Mansour S, Rossier E, Veen M, Lang C, Baasanjav S, Kieslich M, Brossuleit K et al (2010) Mutations causing Greenberg dysplasia but not Pelger anomaly uncouple enzymatic from structural functions of a nuclear membrane protein. Nucleus 1:354–366
Daigle N, Beaudouin J, Hartnell L, Imreh G, Hallberg E, Lippincott-Schwartz J, Ellenberg J (2001) Nuclear pore complexes form immobile networks and have a very low turnover in live mammalian cells. J Cell Biol 154:71–84
Davies BS, Barnes RH 2nd, 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
Davies BS, Coffinier C, Yang SH, Barnes RH 2nd, Jung HJ, Young SG, Fong LG (2011) Investigating the purpose of prelamin A processing. Nucleus 2:4–9
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
Eibauer M, Pellanda M, Turgay Y, Dubrovsky A, Wild A, Medalia O (2015) Structure and gating of the nuclear pore complex. Nat Commun 6:7532
Fidzianska A, Bilinska ZT, Tesson F, Wagner T, Walski M, Grzybowski J, Ruzyllo W, Hausmanowa-Petrusewicz I (2008) Obliteration of cardiomyocyte nuclear architecture in a patient with LMNA gene mutation. J Neurol Sci 271:91–96
Gaines P, Tien CW, Olins AL, Olins DE, Shultz LD, Carney L, Berliner N (2008) Mouse neutrophils lacking Lamin B-receptor expression exhibit aberrant development and lack critical functional responses. Exp Hematol 36:965–976
Goldman RD, Shumaker DK, Erdos MR, Eriksson M, Goldman AE, Gordon LB, Gruenbaum Y, Khuon S, Mendez M, Varga R et al (2004) Accumulation of mutant Lamin A causes progressive changes in nuclear architecture in Hutchinson-Gilford progeria syndrome. Proc Natl Acad Sci USA 101:8963–8968
Grady RM, Starr DA, Ackerman GL, Sanes JR, Han M (2005) Syne proteins anchor muscle nuclei at the neuromuscular junction. Proc Natl Acad Sci USA 102:4359–4364
Gupta P, Bilinska ZT, Sylvius N, Boudreau E, Veinot JP, Labib S, Bolongo PM, Hamza A, Jackson T, Ploski R et al (2010) Genetic and ultrastructural studies in dilated cardiomyopathy patients: a large deletion in the Lamin A/C gene is associated with cardiomyocyte nuclear envelope disruption. Basic Res Cardiol 105:365–377
Hawryluk-Gara LA, Shibuya EK, Wozniak RW (2005) Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex. Mol Biol Cell 16:2382–2394
Hegele RA, Cao H, Liu DM, Costain GA, Charlton-Menys V, Rodger NW, Durrington PN (2006) Sequencing of the reannotated LMNB2 gene reveals novel mutations in patients with acquired partial lipodystrophy. Am J Hum Genet 79:383–389
Hennekes H, Nigg EA (1994) The role of isoprenylation in membrane attachment of nuclear lamins. A single point mutation prevents proteolytic cleavage of the Lamin A precursor and confers membrane binding properties. J Cell Sci 107(Pt 4):1019–1029
Hoffmann K, Dreger CK, Olins AL, Olins DE, Shultz LD, Lucke B, Karl H, Kaps R, Muller D, Vaya A et al (2002) Mutations in the gene encoding the Lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger-Huet anomaly). Nat Genet 31:410–414
Holmer L, Pezhman A, Worman HJ (1998) The human Lamin B receptor/sterol reductase multigene family. Genomics 54:469–476
Houben F, Ramaekers FC, Snoeckx LH, Broers JL (2007) Role of nuclear lamina-cytoskeleton interactions in the maintenance of cellular strength. Biochim Biophys Acta 1773:675–686
Kelley K, Knockenhauer KE, Kabachinski G, Schwartz TU (2015) Atomic structure of the Y complex of the nuclear pore. Nat Struct Mol Biol 22:425–431
Lammerding J, Hsiao J, Schulze PC, Kozlov S, Stewart CL, Lee RT (2005) Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells. J Cell Biol 170:781–791
Luke Y, Zaim H, Karakesisoglou I, Jaeger VM, Sellin L, Lu W, Schneider M, Neumann S, Beijer A, Munck M et al (2008) Nesprin-2 Giant (NUANCE) maintains nuclear envelope architecture and composition in skin. J Cell Sci 121:1887–1898
Lussi YC, Hugi I, Laurell E, Kutay U, Fahrenkrog B (2011) The nucleoporin Nup88 is interacting with nuclear Lamin A. Mol Biol Cell 22:1080–1090
Nikolakaki E, Meier J, Simos G, Georgatos SD, Giannakouros T (1997) Mitotic phosphorylation of the Lamin B receptor by a serine/arginine kinase and p34(cdc2). J Biol Chem 272:6208–6213
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
Pan Y, Garg A, Agarwal AK (2007) Mislocalization of prelamin A Tyr646Phe mutant to the nuclear pore complex in human embryonic kidney 293 cells. Biochem Biophys Res Commun 355:78–84
Rober 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
Rowat AC, Lammerding J, Ipsen JH (2006) Mechanical properties of the cell nucleus and the effect of emerin deficiency. Biophys J 91:4649–4664
Rusinol AE, Sinensky MS (2006) Farnesylated lamins, progeroid syndromes and farnesyl transferase inhibitors. J Cell Sci 119:3265–3272
Smythe C, Jenkins HE, Hutchison CJ (2000) Incorporation of the nuclear pore basket protein nup153 into nuclear pore structures is dependent upon lamina assembly: evidence from cell-free extracts of Xenopus eggs. EMBO J 19:3918–3931
Solovei I, Wang AS, Thanisch K, Schmidt CS, Krebs S, Zwerger M, Cohen TV, Devys D, Foisner R, Peichl L et al (2013) LBR and Lamin A/C sequentially tether peripheral heterochromatin and inversely regulate differentiation. Cell 152:584–598
Stegh AH, Herrmann H, Lampel S, Weisenberger D, Andra K, Seper M, Wiche G, Krammer PH, Peter ME (2000) Identification of the cytolinker plectin as a major early in vivo substrate for caspase 8 during CD95- and tumor necrosis factor receptor-mediated apoptosis. Mol Cell Biol 20:5665–5679
Stewart CL, Kozlov S, Fong LG, Young SG (2007) Mouse models of the laminopathies. Exp Cell Res 313:2144–2156
Suh Y, Kennedy BK (2012) Dialing down SUN1 for laminopathies. Cell 149:509–510
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 147:913–920
Talamas JA, Hetzer MW (2011) POM121 and Sun1 play a role in early steps of interphase NPC assembly. J Cell Biol 194:27–37
Tapley EC, Starr DA (2013) Connecting the nucleus to the cytoskeleton by SUN-KASH bridges across the nuclear envelope. Curr Opin Cell Biol 25:57–62
Ulbert S, Antonin W, Platani M, Mattaj IW (2006) The inner nuclear membrane protein Lem2 is critical for normal nuclear envelope morphology. FEBS Lett 580:6435–6441
Vargas JD, Hatch EM, Anderson DJ, Hetzer MW (2012) Transient nuclear envelope rupturing during interphase in human cancer cells. Nucleus 3:88–100
Vaughan A, Alvarez-Reyes M, Bridger JM, Broers JL, Ramaekers FC, Wehnert M, Morris GE, Whitfield WGF, Hutchison CJ (2001) Both emerin and Lamin C depend on Lamin A for localization at the nuclear envelope. J Cell Sci 114:2577–2590
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 USA 101:10428–10433
Vigouroux C, Auclair M, Dubosclard E, Pouchelet M, Capeau J, Courvalin JC, Buendia B (2001) Nuclear envelope disorganization in fibroblasts from lipodystrophic patients with heterozygous R482Q/W mutations in the Lamin A/C gene. J Cell Sci 114:4459–4468
Yewdell WT, Colombi P, Makhnevych T, Lusk CP (2011) Lumenal interactions in nuclear pore complex assembly and stability. Mol Biol Cell 22:1375–1388
Zhang Q, Bethmann C, Worth NF, Davies JD, Wasner C, Feuer A, Ragnauth CD, Yi Q, Mellad JA, Warren DT et al (2007a) Nesprin-1 and -2 are involved in the pathogenesis of Emery Dreifuss muscular dystrophy and are critical for nuclear envelope integrity. Hum Mol Genet 16:2816–2833
Zhang X, Xu R, Zhu B, Yang X, Ding X, Duan S, Xu T, Zhuang Y, Han M (2007b) Syne-1 and Syne-2 play crucial roles in myonuclear anchorage and motor neuron innervation. Development 134:901–908
Zhou Z, Du X, Cai Z, Song X, Zhang H, Mizuno T, Suzuki E, Yee MR, Berezov A, Murali R et al (2012) Structure of Sad1-UNC84 homology (SUN) domain defines features of molecular bridge in nuclear envelope. J Biol Chem 287:5317–5326
Zwerger M, Herrmann H, Gaines P, Olins AL, Olins DE (2008) Granulocytic nuclear differentiation of Lamin B receptor-deficient mouse EPRO cells. Exp Hematol 36:977–987
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2018 Springer Nature Singapore Pte Ltd.
About this chapter
Cite this chapter
Dutta, S., Bhattacharyya, M., Sengupta, K. (2018). Changes in the Nuclear Envelope in Laminopathies. In: Chattopadhyay, K., Basu, S. (eds) Biochemical and Biophysical Roles of Cell Surface Molecules. Advances in Experimental Medicine and Biology, vol 1112. Springer, Singapore. https://doi.org/10.1007/978-981-13-3065-0_3
Download citation
DOI: https://doi.org/10.1007/978-981-13-3065-0_3
Published:
Publisher Name: Springer, Singapore
Print ISBN: 978-981-13-3064-3
Online ISBN: 978-981-13-3065-0
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)