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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
MeSH Review

Nuclear Lamina

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Disease relevance of Nuclear Lamina


High impact information on Nuclear Lamina

  • These alterations are similar to those developed by mice deficient in A-type lamin, a major component of the nuclear lamina, and phenocopy most defects observed in humans with diverse congenital laminopathies [6].
  • This region contains the lamin A/C gene (LMNA), a candidate gene encoding two proteins of the nuclear lamina, lamins A and C, produced by alternative splicing [7].
  • Lamin A is a major component of the nuclear lamina and nuclear skeleton [8].
  • The mammalian nuclear lamina protein lamin B1 is posttranslationally modified by farnesylation, endoproteolysis, and carboxymethylation at a carboxyl-terminal CAAX motif [9].
  • Nup153 is a peripheral NPC component that has been implicated in protein and RNP transport and in the interaction of NPCs with the nuclear lamina [10].

Biological context of Nuclear Lamina


Anatomical context of Nuclear Lamina


Associations of Nuclear Lamina with chemical compounds


Gene context of Nuclear Lamina

  • Here we describe the derivation of mice carrying an autosomal recessive mutation in the lamin A gene (Lmna) encoding A-type lamins, major components of the nuclear lamina [25].
  • Zmpste24 is a metalloproteinase required for the processing of prelamin A to lamin A, a structural component of the nuclear lamina [26].
  • In contrast, lamin B1 was absent from cardiomyocyte nuclei, showing that lamin B1 is not essential for localization of emerin to the nuclear lamina [27].
  • Our results suggest that interactions with lamin might mediate or stabilize the localization of otefin and YA in the nuclear lamina [28].
  • Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex [29].

Analytical, diagnostic and therapeutic context of Nuclear Lamina


  1. Cellular p32 recruits cytomegalovirus kinase pUL97 to redistribute the nuclear lamina. Marschall, M., Marzi, A., aus dem Siepen, P., Jochmann, R., Kalmer, M., Auerochs, S., Lischka, P., Leis, M., Stamminger, T. J. Biol. Chem. (2005) [Pubmed]
  2. Nuclear envelope defects associated with LMNA mutations cause dilated cardiomyopathy and Emery-Dreifuss muscular dystrophy. Raharjo, W.H., Enarson, P., Sullivan, T., Stewart, C.L., Burke, B. J. Cell. Sci. (2001) [Pubmed]
  3. Induction of nuclear lamins A/C during in vitro-induced differentiation of F9 and P19 embryonal carcinoma cells. Mattia, E., Hoff, W.D., den Blaauwen, J., Meijne, A.M., Stuurman, N., van Renswoude, J. Exp. Cell Res. (1992) [Pubmed]
  4. Autoantibodies to lamins A and C in sera of patients showing peripheral fluorescent antinuclear antibody pattern on HEP-2 cells. Konstantinov, K.N., Galcheva-Gargova, Z., Høier-Madsen, M., Wiik, A., Ullman, S., Halberg, P., Vejlsgaard, G.L. J. Invest. Dermatol. (1990) [Pubmed]
  5. Cytomegalovirus recruitment of cellular kinases to dissolve the nuclear lamina. Muranyi, W., Haas, J., Wagner, M., Krohne, G., Koszinowski, U.H. Science (2002) [Pubmed]
  6. Defective prelamin A processing and muscular and adipocyte alterations in Zmpste24 metalloproteinase-deficient mice. Pendás, A.M., Zhou, Z., Cadiñanos, J., Freije, J.M., Wang, J., Hultenby, K., Astudillo, A., Wernerson, A., Rodríguez, F., Tryggvason, K., López-Otín, C. Nat. Genet. (2002) [Pubmed]
  7. Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy. Bonne, G., Di Barletta, M.R., Varnous, S., Bécane, H.M., Hammouda, E.H., Merlini, L., Muntoni, F., Greenberg, C.R., Gary, F., Urtizberea, J.A., Duboc, D., Fardeau, M., Toniolo, D., Schwartz, K. Nat. Genet. (1999) [Pubmed]
  8. 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., Pei, D., Pendas, A.M., Cadiñanos, J., López-Otín, C., Tse, H.F., Hutchison, C., Chen, J., Cao, Y., Cheah, K.S., Tryggvason, K., Zhou, Z. Nat. Med. (2005) [Pubmed]
  9. A carboxyl-terminal interaction of lamin B1 is dependent on the CAAX endoprotease Rce1 and carboxymethylation. Maske, C.P., Hollinshead, M.S., Higbee, N.C., Bergo, M.O., Young, S.G., Vaux, D.J. J. Cell Biol. (2003) [Pubmed]
  10. The nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins. Walther, T.C., Fornerod, M., Pickersgill, H., Goldberg, M., Allen, T.D., Mattaj, I.W. EMBO J. (2001) [Pubmed]
  11. NuMA: an unusually long coiled-coil related protein in the mammalian nucleus. Yang, C.H., Lambie, E.J., Snyder, M. J. Cell Biol. (1992) [Pubmed]
  12. Human cyclins A and B1 are differentially located in the cell and undergo cell cycle-dependent nuclear transport. Pines, J., Hunter, T. J. Cell Biol. (1991) [Pubmed]
  13. Barrier-to-autointegration factor is required to segregate and enclose chromosomes within the nuclear envelope and assemble the nuclear lamina. Margalit, A., Segura-Totten, M., Gruenbaum, Y., Wilson, K.L. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  14. betaII protein kinase C is required for the G2/M phase transition of cell cycle. Thompson, L.J., Fields, A.P. J. Biol. Chem. (1996) [Pubmed]
  15. Identification of a major polypeptide of the nuclear pore complex. Gerace, L., Ottaviano, Y., Kondor-Koch, C. J. Cell Biol. (1982) [Pubmed]
  16. Expression of an LMNA-N195K variant of A-type lamins results in cardiac conduction defects and death in mice. Mounkes, L.C., Kozlov, S.V., Rottman, J.N., Stewart, C.L. Hum. Mol. Genet. (2005) [Pubmed]
  17. Localization of 4q35.2 to the nuclear periphery: is FSHD a nuclear envelope disease? Masny, P.S., Bengtsson, U., Chung, S.A., Martin, J.H., van Engelen, B., van der Maarel, S.M., Winokur, S.T. Hum. Mol. Genet. (2004) [Pubmed]
  18. unc-83 encodes a novel component of the nuclear envelope and is essential for proper nuclear migration. Starr, D.A., Hermann, G.J., Malone, C.J., Fixsen, W., Priess, J.R., Horvitz, H.R., Han, M. Development (2001) [Pubmed]
  19. Synchronization of interphase events depends neither on mitosis nor on cdk1. Laronne, A., Rotkopf, S., Hellman, A., Gruenbaum, Y., Porter, A.C., Brandeis, M. Mol. Biol. Cell (2003) [Pubmed]
  20. Isoprenylation is required for the processing of the lamin A precursor. Beck, L.A., Hosick, T.J., Sinensky, M. J. Cell Biol. (1990) [Pubmed]
  21. Protein kinase activity associated with the nuclear lamina. Dessev, G., Iovcheva, C., Tasheva, B., Goldman, R. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  22. The Drosophila nuclear lamina protein YA binds to DNA and histone H2B with four domains. Yu, J., Wolfner, M.F. Mol. Biol. Cell (2002) [Pubmed]
  23. Lamin A precursor is localized to intranuclear foci. Sasseville, A.M., Raymond, Y. J. Cell. Sci. (1995) [Pubmed]
  24. In vivo crosslinking of nuclear proteins to DNA by cis-diamminedichloroplatinum (II) in differentiating rat myoblasts. Wedrychowski, A., Bhorjee, J.S., Briggs, R.C. Exp. Cell Res. (1989) [Pubmed]
  25. A progeroid syndrome in mice is caused by defects in A-type lamins. Mounkes, L.C., Kozlov, S., Hernandez, L., Sullivan, T., Stewart, C.L. Nature (2003) [Pubmed]
  26. Heterozygosity for Lmna deficiency eliminates the progeria-like phenotypes in Zmpste24-deficient mice. Fong, L.G., Ng, J.K., Meta, M., Coté, N., Yang, S.H., Stewart, C.L., Sullivan, T., Burghardt, A., Majumdar, S., Reue, K., Bergo, M.O., Young, S.G. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  27. Distribution of emerin and lamins in the heart and implications for Emery-Dreifuss muscular dystrophy. Manilal, S., Sewry, C.A., Pereboev, A., Man, N., Gobbi, P., Hawkes, S., Love, D.R., Morris, G.E. Hum. Mol. Genet. (1999) [Pubmed]
  28. Interactions among Drosophila nuclear envelope proteins lamin, otefin, and YA. Goldberg, M., Lu, H., Stuurman, N., Ashery-Padan, R., Weiss, A.M., Yu, J., Bhattacharyya, D., Fisher, P.A., Gruenbaum, Y., Wolfner, M.F. Mol. Cell. Biol. (1998) [Pubmed]
  29. Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex. Hawryluk-Gara, L.A., Shibuya, E.K., Wozniak, R.W. Mol. Biol. Cell (2005) [Pubmed]
  30. Atypical antineutrophil cytoplasmic antibodies with perinuclear fluorescence in chronic inflammatory bowel diseases and hepatobiliary disorders colocalize with nuclear lamina proteins. Terjung, B., Herzog, V., Worman, H.J., Gestmann, I., Bauer, C., Sauerbruch, T., Spengler, U. Hepatology (1998) [Pubmed]
  31. Isolation and characterization of subnuclear compartments from Trypanosoma brucei. Identification of a major repetitive nuclear lamina component. Rout, M.P., Field, M.C. J. Biol. Chem. (2001) [Pubmed]
  32. Vimentin and CP49/filensin form distinct networks in the lens which are independently modulated during lens fibre cell differentiation. Sandilands, A., Prescott, A.R., Carter, J.M., Hutcheson, A.M., Quinlan, R.A., Richards, J., FitzGerald, P.G. J. Cell. Sci. (1995) [Pubmed]
  33. Association of DNA with the nuclear lamina in Ehrlich ascites tumor cells. Krachmarov, C., Iovcheva, C., Hancock, R., Dessev, G. J. Cell. Biochem. (1986) [Pubmed]
  34. Visualization of the nuclear lamina in mouse anterior pituitary cells and immunocytochemical detection of lamin A/C by quick-freeze freeze-substitution electron microscopy. Senda, T., Iizuka-Kogo, A., Shimomura, A. J. Histochem. Cytochem. (2005) [Pubmed]
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