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Volumn 24, Issue 6, 2012, Pages 775-783

Outfits for different occasions: Tissue-specific roles of Nuclear Envelope proteins

Author keywords

[No Author keywords available]

Indexed keywords

EMERIN; ENVELOPE PROTEIN; LAMIN A; LAMIN C; NUCLEOPORIN;

EID: 84871929542     PISSN: 09550674     EISSN: 18790410     Source Type: Journal    
DOI: 10.1016/j.ceb.2012.08.008     Document Type: Review
Times cited : (35)

References (85)
  • 1
    • 71549117899 scopus 로고    scopus 로고
    • The nuclear envelope as a signaling node in development and disease
    • Dauer W.T., Worman H.J. The nuclear envelope as a signaling node in development and disease. Dev Cell 2009, 17:626-638. 10.1016/j.devcel.2009.10.016.
    • (2009) Dev Cell , vol.17 , pp. 626-638
    • Dauer, W.T.1    Worman, H.J.2
  • 2
    • 67650147960 scopus 로고    scopus 로고
    • The role of nuclear pores in gene regulation, development and disease
    • Capelson M., Hetzer M.W. The role of nuclear pores in gene regulation, development and disease. EMBO Rep 2009, 10:697-705. 10.1038/embor.2009.147.
    • (2009) EMBO Rep , vol.10 , pp. 697-705
    • Capelson, M.1    Hetzer, M.W.2
  • 3
    • 77951616674 scopus 로고    scopus 로고
    • The nuclear envelope in genome organization, expression and stability
    • Mekhail K., Moazed D. The nuclear envelope in genome organization, expression and stability. Nat Rev Mol Cell Biol 2010, 11:317-328. 10.1038/nrm2894.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 317-328
    • Mekhail, K.1    Moazed, D.2
  • 4
    • 0013187463 scopus 로고
    • Studies on the physical properties of protoplasm
    • Kite G. Studies on the physical properties of protoplasm. Am J Physiol 1913, 146.
    • (1913) Am J Physiol , vol.146
    • Kite, G.1
  • 5
    • 0040419373 scopus 로고
    • Experimental studies on amphibian oocyte nuclei. I. Investigation of the structure of the nuclear membrane by means of the electron microscope
    • Callan H.G., Tomlin S.G. Experimental studies on amphibian oocyte nuclei. I. Investigation of the structure of the nuclear membrane by means of the electron microscope. Proc R Soc Lond B Biol Sci 1950, 137:367-378.
    • (1950) Proc R Soc Lond B Biol Sci , vol.137 , pp. 367-378
    • Callan, H.G.1    Tomlin, S.G.2
  • 6
    • 70449301952 scopus 로고
    • Further observations on the nuclear envelope of the animal cell
    • Watson M.L. Further observations on the nuclear envelope of the animal cell. J Biophys Biochem Cytol 1959, 6:147-156.
    • (1959) J Biophys Biochem Cytol , vol.6 , pp. 147-156
    • Watson, M.L.1
  • 7
    • 3242807744 scopus 로고
    • The nuclear envelope; its structure and relation to cytoplasmic membranes
    • Watson M.L. The nuclear envelope; its structure and relation to cytoplasmic membranes. J Biophys Biochem Cytol 1955, 1:257-270.
    • (1955) J Biophys Biochem Cytol , vol.1 , pp. 257-270
    • Watson, M.L.1
  • 8
    • 0019842267 scopus 로고
    • The nuclear envelope and the architecture of the nuclear periphery
    • Franke W.W., Scheer U., Krohne G., Jarasch E.D. The nuclear envelope and the architecture of the nuclear periphery. J Cell Biol 1981, 91(3 Pt 2):39s-50s.
    • (1981) J Cell Biol , vol.91 , Issue.3 PART 2
    • Franke, W.W.1    Scheer, U.2    Krohne, G.3    Jarasch, E.D.4
  • 9
    • 32044433784 scopus 로고    scopus 로고
    • The role of the nuclear envelope in cellular organization
    • D'Angelo M.A., Hetzer M.W. The role of the nuclear envelope in cellular organization. Cell Mol Life Sci 2006, 63:316-332. 10.1007/s00018-005-5361-3.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 316-332
    • D'Angelo, M.A.1    Hetzer, M.W.2
  • 10
    • 36749031152 scopus 로고    scopus 로고
    • Blurring the boundary: the nuclear envelope extends its reach
    • Stewart C.L., Roux K.J., Burke B. Blurring the boundary: the nuclear envelope extends its reach. Science (New York, NY) 2007, 318:1408-1412. 10.1126/science.1142034.
    • (2007) Science (New York, NY) , vol.318 , pp. 1408-1412
    • Stewart, C.L.1    Roux, K.J.2    Burke, B.3
  • 11
    • 0036429266 scopus 로고    scopus 로고
    • The nesprins are giant actin-binding proteins, orthologous to drosophila melanogaster muscle protein MSP-300
    • Zhang Q., Ragnauth C., Greener M.J., Shanahan C.M., Roberts R.G. The nesprins are giant actin-binding proteins, orthologous to drosophila melanogaster muscle protein MSP-300. Genomics 2002, 80:473-481.
    • (2002) Genomics , vol.80 , pp. 473-481
    • Zhang, Q.1    Ragnauth, C.2    Greener, M.J.3    Shanahan, C.M.4    Roberts, R.G.5
  • 13
    • 33646555082 scopus 로고    scopus 로고
    • SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton
    • Haque F., Lloyd D.J., Smallwood D.T., Dent C.L., Shanahan C.M., Fry A.M., Shackleton S. SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton. Mol Cell Biol 2006, 26:3738-3751. 10.1128/MCB.26.10.3738-3751.2006.
    • (2006) Mol Cell Biol , vol.26 , pp. 3738-3751
    • Haque, F.1    Lloyd, D.J.2    Smallwood, D.T.3    Dent, C.L.4    Shanahan, C.M.5    Fry, A.M.6    Shackleton, S.7
  • 14
    • 34249313304 scopus 로고    scopus 로고
    • SUN1 is required for telomere attachment to nuclear envelope and gametogenesis in mice
    • Ding X., Xu R., Yu J., Xu T., Zhuang Y., Han M. SUN1 is required for telomere attachment to nuclear envelope and gametogenesis in mice. Dev Cell 2007, 12:863-872.
    • (2007) Dev Cell , vol.12 , pp. 863-872
    • Ding, X.1    Xu, R.2    Yu, J.3    Xu, T.4    Zhuang, Y.5    Han, M.6
  • 15
    • 7944236264 scopus 로고    scopus 로고
    • Mapping the dynamic organization of the nuclear pore complex inside single living cells
    • Rabut G., Doye V., Ellenberg J. Mapping the dynamic organization of the nuclear pore complex inside single living cells. Nat Cell Biol 2004, 6:1114-1121. 10.1038/ncb1184.
    • (2004) Nat Cell Biol , vol.6 , pp. 1114-1121
    • Rabut, G.1    Doye, V.2    Ellenberg, J.3
  • 16
    • 77953577950 scopus 로고    scopus 로고
    • The nuclear envelope at a glance
    • Wilson K.L., Berk J.M. The nuclear envelope at a glance. J Cell Sci 2010, 123(Pt 12):1973-1978. 10.1242/jcs.019042.
    • (2010) J Cell Sci , vol.123 , Issue.PART 12 , pp. 1973-1978
    • Wilson, K.L.1    Berk, J.M.2
  • 17
    • 84859728172 scopus 로고    scopus 로고
    • Inner nuclear membrane proteins: impact on human disease
    • Mendez-Lopez I., Worman H.J. Inner nuclear membrane proteins: impact on human disease. Chromosoma 2012, 121:153-167. http://dx.doi.org/10.1007/s00412-012-0360-2;
    • (2012) Chromosoma , vol.121 , pp. 153-167
    • Mendez-Lopez, I.1    Worman, H.J.2
  • 18
    • 0042691509 scopus 로고    scopus 로고
    • Nuclear membrane proteins with potential disease links found by subtractive proteomics
    • Schirmer E.C., Florens L., Guan T., Yates J.R., Gerace L. Nuclear membrane proteins with potential disease links found by subtractive proteomics. Science (New York, NY) 2003, 301:1380-1382. 10.1126/science.1088176.
    • (2003) Science (New York, NY) , vol.301 , pp. 1380-1382
    • Schirmer, E.C.1    Florens, L.2    Guan, T.3    Yates, J.R.4    Gerace, L.5
  • 19
    • 78650089607 scopus 로고    scopus 로고
    • The leukocyte nuclear envelope proteome varies with cell activation and contains novel transmembrane proteins that affect genome architecture
    • Korfali N., Wilkie G.S., Swanson S.K., Srsen V., Batrakou D.G., Fairley E.A., Schirmer E.C. The leukocyte nuclear envelope proteome varies with cell activation and contains novel transmembrane proteins that affect genome architecture. Mol Cell Proteomics 2010, 9:2571-2585. 10.1074/mcp.M110.002915.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 2571-2585
    • Korfali, N.1    Wilkie, G.S.2    Swanson, S.K.3    Srsen, V.4    Batrakou, D.G.5    Fairley, E.A.6    Schirmer, E.C.7
  • 20
    • 78651112186 scopus 로고    scopus 로고
    • Several novel nuclear envelope transmembrane proteins identified in skeletal muscle have cytoskeletal associations
    • Wilkie G.S., Korfali N., Swanson S.K., Malik P., Srsen V., Batrakou D.G., Schirmer E.C. Several novel nuclear envelope transmembrane proteins identified in skeletal muscle have cytoskeletal associations. Mol Cell Proteomics 2011, 10:M110. 10.1074/mcp.M110.003129.003129.
    • (2011) Mol Cell Proteomics , vol.10
    • Wilkie, G.S.1    Korfali, N.2    Swanson, S.K.3    Malik, P.4    Srsen, V.5    Batrakou, D.G.6    Schirmer, E.C.7
  • 21
    • 0029874852 scopus 로고    scopus 로고
    • Emerin deficiency at the nuclear membrane in patients with emery-dreifuss muscular dystrophy
    • Nagano A., Koga R., Ogawa M., Kurano Y., Kawada J., Okada R., Arahata K. Emerin deficiency at the nuclear membrane in patients with emery-dreifuss muscular dystrophy. Nat Genet 1996, 12:254-259. 10.1038/ng0396-254.
    • (1996) Nat Genet , vol.12 , pp. 254-259
    • Nagano, A.1    Koga, R.2    Ogawa, M.3    Kurano, Y.4    Kawada, J.5    Okada, R.6    Arahata, K.7
  • 22
    • 13544274478 scopus 로고    scopus 로고
    • Loss-of-function mutations in LEMD3 result in osteopoikilosis, buschke-ollendorff syndrome and melorheostosis
    • Hellemans J., Preobrazhenska O., Willaert A., Debeer P., Verdonk P.C., Costa T., Mortier G.R. Loss-of-function mutations in LEMD3 result in osteopoikilosis, buschke-ollendorff syndrome and melorheostosis. Nat Genet 2004, 36:1213-1218. 10.1038/ng1453.
    • (2004) Nat Genet , vol.36 , pp. 1213-1218
    • Hellemans, J.1    Preobrazhenska, O.2    Willaert, A.3    Debeer, P.4    Verdonk, P.C.5    Costa, T.6    Mortier, G.R.7
  • 24
    • 84855388549 scopus 로고    scopus 로고
    • Lamin B receptor regulates the growth and maturation of myeloid progenitors via its sterol reductase domain: implications for cholesterol biosynthesis in regulating myelopoiesis
    • Subramanian G., Chaudhury P., Malu K., Fowler S., Manmode R., Gotur D., Zwerger M., Ryan D., Roberti R., Gaines P. Lamin B receptor regulates the growth and maturation of myeloid progenitors via its sterol reductase domain: implications for cholesterol biosynthesis in regulating myelopoiesis. J Immunol (Baltimore, MD: 1950) 2012, 188:85-102.
    • (2012) J Immunol (Baltimore, MD: 1950) , vol.188 , pp. 85-102
    • Subramanian, G.1    Chaudhury, P.2    Malu, K.3    Fowler, S.4    Manmode, R.5    Gotur, D.6    Zwerger, M.7    Ryan, D.8    Roberti, R.9    Gaines, P.10
  • 25
    • 12244285280 scopus 로고    scopus 로고
    • Mutations at the mouse ichthyosis locus are within the lamin B receptor gene: a single gene model for human pelger-huet anomaly
    • Shultz L.D., Lyons B.L., Burzenski L.M., Gott B., Samuels R., Schweitzer P.A., Hoffmann K. Mutations at the mouse ichthyosis locus are within the lamin B receptor gene: a single gene model for human pelger-huet anomaly. Hum Mol Genet 2003, 12:61-69.
    • (2003) Hum Mol Genet , vol.12 , pp. 61-69
    • Shultz, L.D.1    Lyons, B.L.2    Burzenski, L.M.3    Gott, B.4    Samuels, R.5    Schweitzer, P.A.6    Hoffmann, K.7
  • 26
    • 33750429896 scopus 로고    scopus 로고
    • Man1, an inner nuclear membrane protein, regulates vascular remodeling by modulating transforming growth factor beta signaling
    • Ishimura A., Ng J.K., Taira M., Young S.G., Osada S. Man1, an inner nuclear membrane protein, regulates vascular remodeling by modulating transforming growth factor beta signaling. Development (Cambridge, England) 2006, 133:3919-3928. 10.1242/dev.02538.
    • (2006) Development (Cambridge, England) , vol.133 , pp. 3919-3928
    • Ishimura, A.1    Ng, J.K.2    Taira, M.3    Young, S.G.4    Osada, S.5
  • 27
    • 34248154716 scopus 로고    scopus 로고
    • The nuclear envelope protein MAN1 regulates TGFbeta signaling and vasculogenesis in the embryonic yolk sac
    • Cohen T.V., Kosti O., Stewart C.L. The nuclear envelope protein MAN1 regulates TGFbeta signaling and vasculogenesis in the embryonic yolk sac. Development (Cambridge, England) 2007, 134:1385-1395. 10.1242/dev.02816.
    • (2007) Development (Cambridge, England) , vol.134 , pp. 1385-1395
    • Cohen, T.V.1    Kosti, O.2    Stewart, C.L.3
  • 28
    • 13544264752 scopus 로고    scopus 로고
    • MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-beta signaling
    • Lin F., Morrison J.M., Wu W., Worman H.J. MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-beta signaling. Hum Mol Genet 2005, 14:437-445. 10.1093/hmg/ddi040.
    • (2005) Hum Mol Genet , vol.14 , pp. 437-445
    • Lin, F.1    Morrison, J.M.2    Wu, W.3    Worman, H.J.4
  • 29
    • 18144411595 scopus 로고    scopus 로고
    • 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
    • Pan D., Estevez-Salmeron L.D., Stroschein S.L., Zhu X., He J., Zhou S., Luo K. 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, 280:15992-16001. 10.1074/jbc.M411234200.
    • (2005) J Biol Chem , vol.280 , pp. 15992-16001
    • Pan, D.1    Estevez-Salmeron, L.D.2    Stroschein, S.L.3    Zhu, X.4    He, J.5    Zhou, S.6    Luo, K.7
  • 30
    • 77956600811 scopus 로고    scopus 로고
    • Structural analysis of the Smad2-MAN1 interaction that regulates transforming growth factor-beta signaling at the inner nuclear membrane
    • Konde E., Bourgeois B., Tellier-Lebegue C., Wu W., Perez J., Caputo S., Zinn-Justin S. Structural analysis of the Smad2-MAN1 interaction that regulates transforming growth factor-beta signaling at the inner nuclear membrane. Biochemistry 2010, 49:8020-8032. 10.1021/bi101153w.
    • (2010) Biochemistry , vol.49 , pp. 8020-8032
    • Konde, E.1    Bourgeois, B.2    Tellier-Lebegue, C.3    Wu, W.4    Perez, J.5    Caputo, S.6    Zinn-Justin, S.7
  • 31
    • 0023654060 scopus 로고
    • Cartilage-inducing factor-B is a unique protein structurally and functionally related to transforming growth factor-beta
    • Seyedin S.M., Segarini P.R., Rosen D.M., Thompson A.Y., Bentz H., Graycar J. Cartilage-inducing factor-B is a unique protein structurally and functionally related to transforming growth factor-beta. J Biol Chem 1987, 262:1946-1949.
    • (1987) J Biol Chem , vol.262 , pp. 1946-1949
    • Seyedin, S.M.1    Segarini, P.R.2    Rosen, D.M.3    Thompson, A.Y.4    Bentz, H.5    Graycar, J.6
  • 32
    • 34250019537 scopus 로고
    • Bone: formation by autoinduction
    • Urist M.R. Bone: formation by autoinduction. Science (New York, NY) 1965, 150:893-899.
    • (1965) Science (New York, NY) , vol.150 , pp. 893-899
    • Urist, M.R.1
  • 34
    • 0034777991 scopus 로고    scopus 로고
    • Nuclear membrane protein LAP2beta mediates transcriptional repression alone and together with its binding partner GCL (germ-cell-less)
    • Nili E., Cojocaru G.S., Kalma Y., Ginsberg D., Copeland N.G., Gilbert D.J., Rechavi G. 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.
    • (2001) J Cell Sci , vol.114 , Issue.PART 18 , pp. 3297-3307
    • Nili, E.1    Cojocaru, G.S.2    Kalma, Y.3    Ginsberg, D.4    Copeland, N.G.5    Gilbert, D.J.6    Rechavi, G.7
  • 35
    • 33746500691 scopus 로고    scopus 로고
    • The inner nuclear membrane protein emerin regulates beta-catenin activity by restricting its accumulation in the nucleus
    • Markiewicz E., Tilgner K., Barker N., van de Wetering M., Clevers H., Dorobek M., Hutchison C.J. The inner nuclear membrane protein emerin regulates beta-catenin activity by restricting its accumulation in the nucleus. EMBO J 2006, 25:3275-3285. 10.1038/sj.emboj.7601230.
    • (2006) EMBO J , vol.25 , pp. 3275-3285
    • Markiewicz, E.1    Tilgner, K.2    Barker, N.3    van de Wetering, M.4    Clevers, H.5    Dorobek, M.6    Hutchison, C.J.7
  • 36
    • 70350524986 scopus 로고    scopus 로고
    • Overlapping functions of nuclear envelope proteins NET25 (Lem2) and emerin in regulation of extracellular signal-regulated kinase signaling in myoblast differentiation
    • Huber M.D., Guan T., Gerace L. Overlapping functions of nuclear envelope proteins NET25 (Lem2) and emerin in regulation of extracellular signal-regulated kinase signaling in myoblast differentiation. Mol Cell Biol 2009, 29:5718-5728. 10.1128/MCB.00270-09.
    • (2009) Mol Cell Biol , vol.29 , pp. 5718-5728
    • Huber, M.D.1    Guan, T.2    Gerace, L.3
  • 37
    • 34547851806 scopus 로고    scopus 로고
    • Activation of MAPK in hearts of EMD null mice: similarities between mouse models of X-linked and autosomal dominant emery dreifuss muscular dystrophy
    • Muchir A., Pavlidis P., Bonne G., Hayashi Y.K., Worman H.J. 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, 16:1884-1895. 10.1093/hmg/ddm137.
    • (2007) Hum Mol Genet , vol.16 , pp. 1884-1895
    • Muchir, A.1    Pavlidis, P.2    Bonne, G.3    Hayashi, Y.K.4    Worman, H.J.5
  • 38
    • 57849157294 scopus 로고    scopus 로고
    • Reduced expression of A-type lamins and emerin activates extracellular signal-regulated kinase in cultured cells
    • Muchir A., Wu W., Worman H.J. Reduced expression of A-type lamins and emerin activates extracellular signal-regulated kinase in cultured cells. Biochim Biophys Acta 2009, 1792:75-81. 10.1016/j.bbadis.2008.10.012.
    • (2009) Biochim Biophys Acta , vol.1792 , pp. 75-81
    • Muchir, A.1    Wu, W.2    Worman, H.J.3
  • 40
    • 77949887190 scopus 로고    scopus 로고
    • Identification of an emerin-beta-catenin complex in the heart important for intercalated disc architecture and beta-catenin localisation
    • Wheeler M.A., Warley A., Roberts R.G., Ehler E., Ellis J.A. Identification of an emerin-beta-catenin complex in the heart important for intercalated disc architecture and beta-catenin localisation. Cell Mol Life Sci 2010, 67:781-796. 10.1007/s00018-009-0219-8.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 781-796
    • Wheeler, M.A.1    Warley, A.2    Roberts, R.G.3    Ehler, E.4    Ellis, J.A.5
  • 41
    • 70350543572 scopus 로고    scopus 로고
    • Regulation of myoblast differentiation by the nuclear envelope protein NET39
    • Liu G.H., Guan T., Datta K., Coppinger J., Yates J., Gerace L. Regulation of myoblast differentiation by the nuclear envelope protein NET39. Mol Cell Biol 2009, 29:5800-5812. 10.1128/MCB.00684-09.
    • (2009) Mol Cell Biol , vol.29 , pp. 5800-5812
    • Liu, G.H.1    Guan, T.2    Datta, K.3    Coppinger, J.4    Yates, J.5    Gerace, L.6
  • 42
    • 70350367846 scopus 로고    scopus 로고
    • NET37, a nuclear envelope transmembrane protein with glycosidase homology, is involved in myoblast differentiation
    • Datta K., Guan T., Gerace L. NET37, a nuclear envelope transmembrane protein with glycosidase homology, is involved in myoblast differentiation. J Biol Chem 2009, 284:29666-29676. 10.1074/jbc.M109.034041.
    • (2009) J Biol Chem , vol.284 , pp. 29666-29676
    • Datta, K.1    Guan, T.2    Gerace, L.3
  • 43
    • 33751359975 scopus 로고    scopus 로고
    • Lmo7 is an emerin-binding protein that regulates the transcription of emerin and many other muscle-relevant genes
    • Holaska J.M., Rais-Bahrami S., Wilson K.L. Lmo7 is an emerin-binding protein that regulates the transcription of emerin and many other muscle-relevant genes. Hum Mol Genet 2006, 15:3459-3472. 10.1093/hmg/ddl423.
    • (2006) Hum Mol Genet , vol.15 , pp. 3459-3472
    • Holaska, J.M.1    Rais-Bahrami, S.2    Wilson, K.L.3
  • 44
    • 34547642520 scopus 로고    scopus 로고
    • An emerin " proteome" : purification of distinct emerin-containing complexes from HeLa cells suggests molecular basis for diverse roles including gene regulation, mRNA splicing, signaling, mechanosensing, and nuclear architecture
    • Holaska J.M., Wilson K.L. An emerin " proteome" : purification of distinct emerin-containing complexes from HeLa cells suggests molecular basis for diverse roles including gene regulation, mRNA splicing, signaling, mechanosensing, and nuclear architecture. Biochemistry 2007, 46:8897-8908. 10.1021/bi602636m.
    • (2007) Biochemistry , vol.46 , pp. 8897-8908
    • Holaska, J.M.1    Wilson, K.L.2
  • 45
    • 48049085684 scopus 로고    scopus 로고
    • Emerin and the nuclear lamina in muscle and cardiac disease
    • Holaska J.M. Emerin and the nuclear lamina in muscle and cardiac disease. Circ Res 2008, 103:16-23. 10.1161/CIRCRESAHA.108.172197.
    • (2008) Circ Res , vol.103 , pp. 16-23
    • Holaska, J.M.1
  • 46
    • 34250777112 scopus 로고    scopus 로고
    • The nuclear envelope and transcriptional control
    • Akhtar A., Gasser S.M. The nuclear envelope and transcriptional control. Nat Rev Genet 2007, 8:507-517. 10.1038/nrg2122.
    • (2007) Nat Rev Genet , vol.8 , pp. 507-517
    • Akhtar, A.1    Gasser, S.M.2
  • 47
    • 34047262162 scopus 로고    scopus 로고
    • Transcriptional regulation at the nuclear pore complex
    • Brown C.R., Silver P.A. Transcriptional regulation at the nuclear pore complex. Curr Opin Genet Dev 2007, 17:100-106. 10.1016/j.gde.2007.02.005.
    • (2007) Curr Opin Genet Dev , vol.17 , pp. 100-106
    • Brown, C.R.1    Silver, P.A.2
  • 48
    • 79951555476 scopus 로고    scopus 로고
    • Functional interactions between nucleoporins and chromatin
    • Liang Y., Hetzer M.W. Functional interactions between nucleoporins and chromatin. Curr Opin Cell Biol 2011, 23:65-70. 10.1016/j.ceb.2010.09.008.
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 65-70
    • Liang, Y.1    Hetzer, M.W.2
  • 49
    • 9044241254 scopus 로고    scopus 로고
    • Fusion of the nucleoporin gene NUP98 to HOXA9 by the chromosome translocation t(7;11)(p15;p15) in human myeloid leukaemia
    • Nakamura T., Largaespada D.A., Lee M.P., Johnson L.A., Ohyashiki K., Toyama K., Shaughnessy J.D. Fusion of the nucleoporin gene NUP98 to HOXA9 by the chromosome translocation t(7;11)(p15;p15) in human myeloid leukaemia. Nat Genet 1996, 12:154-158. 10.1038/ng0296-154.
    • (1996) Nat Genet , vol.12 , pp. 154-158
    • Nakamura, T.1    Largaespada, D.A.2    Lee, M.P.3    Johnson, L.A.4    Ohyashiki, K.5    Toyama, K.6    Shaughnessy, J.D.7
  • 50
    • 57349179985 scopus 로고    scopus 로고
    • Mutation in nuclear pore component NUP155 leads to atrial fibrillation and early sudden cardiac death
    • Zhang X., Chen S., Yoo S., Chakrabarti S., Zhang T., Ke T., Wang Q.K. Mutation in nuclear pore component NUP155 leads to atrial fibrillation and early sudden cardiac death. Cell 2008, 135:1017-1027. 10.1016/j.cell.2008.10.022.
    • (2008) Cell , vol.135 , pp. 1017-1027
    • Zhang, X.1    Chen, S.2    Yoo, S.3    Chakrabarti, S.4    Zhang, T.5    Ke, T.6    Wang, Q.K.7
  • 51
    • 44449129923 scopus 로고    scopus 로고
    • Nuclear pore composition regulates neural stem/progenitor cell differentiation in the mouse embryo
    • Lupu F., Alves A., Anderson K., Doye V., Lacy E. Nuclear pore composition regulates neural stem/progenitor cell differentiation in the mouse embryo. Dev Cell 2008, 14:831-842. 10.1016/j.devcel.2008.03.011.
    • (2008) Dev Cell , vol.14 , pp. 831-842
    • Lupu, F.1    Alves, A.2    Anderson, K.3    Doye, V.4    Lacy, E.5
  • 53
    • 33745160393 scopus 로고    scopus 로고
    • Deletion of the inducible 70-kDa heat shock protein genes in mice impairs cardiac contractile function and calcium handling associated with hypertrophy
    • Kim Y.K., Suarez J., Hu Y., McDonough P.M., Boer C., Dix D.J., Dillmann W.H. Deletion of the inducible 70-kDa heat shock protein genes in mice impairs cardiac contractile function and calcium handling associated with hypertrophy. Circulation 2006, 113:2589-2597. 10.1161/CIRCULATIONAHA.105.598409.
    • (2006) Circulation , vol.113 , pp. 2589-2597
    • Kim, Y.K.1    Suarez, J.2    Hu, Y.3    McDonough, P.M.4    Boer, C.5    Dix, D.J.6    Dillmann, W.H.7
  • 54
    • 41749119125 scopus 로고    scopus 로고
    • Association of Met439Thr substitution in heat shock protein 70 gene with postoperative atrial fibrillation and serum HSP70 protein levels
    • Afzal A.R., Mandal K., Nyamweya S., Foteinos G., Poloniecki J., Camm A.J., Xu Q. Association of Met439Thr substitution in heat shock protein 70 gene with postoperative atrial fibrillation and serum HSP70 protein levels. Cardiology 2008, 110:45-52. 10.1159/000109406.
    • (2008) Cardiology , vol.110 , pp. 45-52
    • Afzal, A.R.1    Mandal, K.2    Nyamweya, S.3    Foteinos, G.4    Poloniecki, J.5    Camm, A.J.6    Xu, Q.7
  • 55
    • 79955515703 scopus 로고    scopus 로고
    • Modulation of chromatin position and gene expression by HDAC4 interaction with nucleoporins
    • Kehat I., Accornero F., Aronow B.J., Molkentin J.D. Modulation of chromatin position and gene expression by HDAC4 interaction with nucleoporins. J Cell Biol 2011, 193:21-29. 10.1083/jcb.201101046.
    • (2011) J Cell Biol , vol.193 , pp. 21-29
    • Kehat, I.1    Accornero, F.2    Aronow, B.J.3    Molkentin, J.D.4
  • 56
    • 58249089343 scopus 로고    scopus 로고
    • Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells
    • D'Angelo M.A., Raices M., Panowski S.H., Hetzer M.W. Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells. Cell 2009, 136:284-295. 10.1016/j.cell.2008.11.037.
    • (2009) Cell , vol.136 , pp. 284-295
    • D'Angelo, M.A.1    Raices, M.2    Panowski, S.H.3    Hetzer, M.W.4
  • 58
    • 0020399177 scopus 로고
    • Identification of a major polypeptide of the nuclear pore complex
    • Gerace L., Ottaviano Y., Kondor-Koch C. Identification of a major polypeptide of the nuclear pore complex. J Cell Biol 1982, 95:826-837.
    • (1982) J Cell Biol , vol.95 , pp. 826-837
    • Gerace, L.1    Ottaviano, Y.2    Kondor-Koch, C.3
  • 59
    • 0024360678 scopus 로고
    • Primary structure analysis of an integral membrane glycoprotein of the nuclear pore
    • Wozniak R.W., Bartnik E., Blobel G. Primary structure analysis of an integral membrane glycoprotein of the nuclear pore. J Cell Biol 1989, 108:2083-2092.
    • (1989) J Cell Biol , vol.108 , pp. 2083-2092
    • Wozniak, R.W.1    Bartnik, E.2    Blobel, G.3
  • 60
    • 0032874218 scopus 로고    scopus 로고
    • CDNA cloning and embryonic expression of mouse nuclear pore membrane glycoprotein 210 mRNA
    • Olsson M., Ekblom M., Fecker L., Kurkinen M., Ekblom P. cDNA cloning and embryonic expression of mouse nuclear pore membrane glycoprotein 210 mRNA. Kidney Int 1999, 56:827-838. 10.1046/j.1523-1755.1999.00618.x.
    • (1999) Kidney Int , vol.56 , pp. 827-838
    • Olsson, M.1    Ekblom, M.2    Fecker, L.3    Kurkinen, M.4    Ekblom, P.5
  • 61
    • 0346992146 scopus 로고    scopus 로고
    • Limited expression of nuclear pore membrane glycoprotein 210 in cell lines and tissues suggests cell-type specific nuclear pores in metazoans
    • Olsson M., Scheele S., Ekblom P. Limited expression of nuclear pore membrane glycoprotein 210 in cell lines and tissues suggests cell-type specific nuclear pores in metazoans. Exp Cell Res 2004, 292:359-370.
    • (2004) Exp Cell Res , vol.292 , pp. 359-370
    • Olsson, M.1    Scheele, S.2    Ekblom, P.3
  • 62
    • 84857031394 scopus 로고    scopus 로고
    • A change in nuclear pore complex composition regulates cell differentiation
    • D'Angelo M.A., Gomez-Cavazos J.S., Mei A., Lackner D.H., Hetzer M.W. A change in nuclear pore complex composition regulates cell differentiation. Dev Cell 2012, 22:446-458. 10.1016/j.devcel.2011.11.021.
    • (2012) Dev Cell , vol.22 , pp. 446-458
    • D'Angelo, M.A.1    Gomez-Cavazos, J.S.2    Mei, A.3    Lackner, D.H.4    Hetzer, M.W.5
  • 63
    • 0037123357 scopus 로고    scopus 로고
    • Genomic organization, transcript variants and comparative analysis of the human nucleoporin 155 (NUP155) gene
    • Zhang X., Yang H., Yu J., Chen C., Zhang G., Bao J., Bolund L. Genomic organization, transcript variants and comparative analysis of the human nucleoporin 155 (NUP155) gene. Gene 2002, 288:9-18.
    • (2002) Gene , vol.288 , pp. 9-18
    • Zhang, X.1    Yang, H.2    Yu, J.3    Chen, C.4    Zhang, G.5    Bao, J.6    Bolund, L.7
  • 64
    • 0036357721 scopus 로고    scopus 로고
    • Characterization and potential function of a novel testis-specific nucleoporin BS-63
    • Cai Y., Gao Y., Sheng Q., Miao S., Cui X., Wang L., Koide S.S. Characterization and potential function of a novel testis-specific nucleoporin BS-63. Mol Reprod Dev 2002, 61:126-134. 10.1002/mrd.1139.
    • (2002) Mol Reprod Dev , vol.61 , pp. 126-134
    • Cai, Y.1    Gao, Y.2    Sheng, Q.3    Miao, S.4    Cui, X.5    Wang, L.6    Koide, S.S.7
  • 65
    • 2342501365 scopus 로고    scopus 로고
    • Genome-wide localization of the nuclear transport machinery couples transcriptional status and nuclear organization
    • Casolari J.M., Brown C.R., Komili S., West J., Hieronymus H., Silver P.A. Genome-wide localization of the nuclear transport machinery couples transcriptional status and nuclear organization. Cell 2004, 117:427-439.
    • (2004) Cell , vol.117 , pp. 427-439
    • Casolari, J.M.1    Brown, C.R.2    Komili, S.3    West, J.4    Hieronymus, H.5    Silver, P.A.6
  • 66
    • 31544471808 scopus 로고    scopus 로고
    • Nup-PI: the nucleopore-promoter interaction of genes in yeast
    • Schmid M., Arib G., Laemmli C., Nishikawa J., Durussel T., Laemmli U.K. Nup-PI: the nucleopore-promoter interaction of genes in yeast. Mol Cell 2006, 21:379-391. 10.1016/j.molcel.2005.12.012.
    • (2006) Mol Cell , vol.21 , pp. 379-391
    • Schmid, M.1    Arib, G.2    Laemmli, C.3    Nishikawa, J.4    Durussel, T.5    Laemmli, U.K.6
  • 67
    • 33744977019 scopus 로고    scopus 로고
    • Nuclear pore association confers optimal expression levels for an inducible yeast gene
    • Taddei A., Van Houwe G., Hediger F., Kalck V., Cubizolles F., Schober H., Gasser S.M. Nuclear pore association confers optimal expression levels for an inducible yeast gene. Nature 2006, 441:774-778. 10.1038/nature04845.
    • (2006) Nature , vol.441 , pp. 774-778
    • Taddei, A.1    Van Houwe, G.2    Hediger, F.3    Kalck, V.4    Cubizolles, F.5    Schober, H.6    Gasser, S.M.7
  • 68
    • 75749103380 scopus 로고    scopus 로고
    • Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes
    • Capelson M., Liang Y., Schulte R., Mair W., Wagner U., Hetzer M.W. Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes. Cell 2010, 140:372-383. 10.1016/j.cell.2009.12.054.
    • (2010) Cell , vol.140 , pp. 372-383
    • Capelson, M.1    Liang, Y.2    Schulte, R.3    Mair, W.4    Wagner, U.5    Hetzer, M.W.6
  • 69
    • 75749117571 scopus 로고    scopus 로고
    • Nucleoporins directly stimulate expression of developmental and cell-cycle genes inside the nucleoplasm
    • Kalverda B., Pickersgill H., Shloma V.V., Fornerod M. Nucleoporins directly stimulate expression of developmental and cell-cycle genes inside the nucleoplasm. Cell 2010, 140:360-371. 10.1016/j.cell.2010.01.011.
    • (2010) Cell , vol.140 , pp. 360-371
    • Kalverda, B.1    Pickersgill, H.2    Shloma, V.V.3    Fornerod, M.4
  • 70
    • 77649210955 scopus 로고    scopus 로고
    • Nuclear pore proteins nup153 and megator define transcriptionally active regions in the drosophila genome
    • Vaquerizas J.M., Suyama R., Kind J., Miura K., Luscombe N.M., Akhtar A. Nuclear pore proteins nup153 and megator define transcriptionally active regions in the drosophila genome. PLoS Genet 2010, 6:e1000846. 10.1371/journal.pgen.1000846.
    • (2010) PLoS Genet , vol.6
    • Vaquerizas, J.M.1    Suyama, R.2    Kind, J.3    Miura, K.4    Luscombe, N.M.5    Akhtar, A.6
  • 71
    • 0033912083 scopus 로고    scopus 로고
    • Characterization and targeted disruption of murine Nup50, a p27(Kip1)-interacting component of the nuclear pore complex
    • Smitherman M., Lee K., Swanger J., Kapur R., Clurman B.E. Characterization and targeted disruption of murine Nup50, a p27(Kip1)-interacting component of the nuclear pore complex. Mol Cell Biol 2000, 20:5631-5642.
    • (2000) Mol Cell Biol , vol.20 , pp. 5631-5642
    • Smitherman, M.1    Lee, K.2    Swanger, J.3    Kapur, R.4    Clurman, B.E.5
  • 72
  • 73
    • 0037673950 scopus 로고    scopus 로고
    • Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome
    • Eriksson M., Brown W.T., Gordon L.B., Glynn M.W., Singer J., Scott L., Collins F.S. Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome. Nature 2003, 423:293-298. 10.1038/nature01629.
    • (2003) Nature , vol.423 , pp. 293-298
    • Eriksson, M.1    Brown, W.T.2    Gordon, L.B.3    Glynn, M.W.4    Singer, J.5    Scott, L.6    Collins, F.S.7
  • 74
    • 0032771080 scopus 로고    scopus 로고
    • The emery-dreifuss muscular dystrophy phenotype arises from aberrant targeting and binding of emerin at the inner nuclear membrane
    • Fairley E.A., Kendrick-Jones J., Ellis J.A. The emery-dreifuss muscular dystrophy phenotype arises from aberrant targeting and binding of emerin at the inner nuclear membrane. J Cell Sci 1999, 112(Pt 15):2571-2582.
    • (1999) J Cell Sci , vol.112 , Issue.PART 15 , pp. 2571-2582
    • Fairley, E.A.1    Kendrick-Jones, J.2    Ellis, J.A.3
  • 76
    • 84860327128 scopus 로고    scopus 로고
    • Accumulation of the inner nuclear envelope protein Sun1 is pathogenic in progeric and dystrophic laminopathies
    • Chen C.Y., Chi Y.H., Mutalif R.A., Starost M.F., Myers T.G., Anderson S.A., Jeang K.T. Accumulation of the inner nuclear envelope protein Sun1 is pathogenic in progeric and dystrophic laminopathies. Cell 2012, 149:565-577. 10.1016/j.cell.2012.01.059.
    • (2012) Cell , vol.149 , pp. 565-577
    • Chen, C.Y.1    Chi, Y.H.2    Mutalif, R.A.3    Starost, M.F.4    Myers, T.G.5    Anderson, S.A.6    Jeang, K.T.7
  • 77
    • 0033615969 scopus 로고    scopus 로고
    • Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy
    • Sullivan T., Escalante-Alcalde D., Bhatt H., Anver M., Bhat N., Nagashima K., Burke B. Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy. J Cell Biol 1999, 147:913-920.
    • (1999) J Cell Biol , vol.147 , pp. 913-920
    • Sullivan, T.1    Escalante-Alcalde, D.2    Bhatt, H.3    Anver, M.4    Bhat, N.5    Nagashima, K.6    Burke, B.7
  • 78
    • 0035034047 scopus 로고    scopus 로고
    • A mutation in the X-linked emery-dreifuss muscular dystrophy gene in a patient affected with conduction cardiomyopathy
    • Vohanka S., Vytopil M., Bednarik J., Lukas Z., Kadanka Z., Schildberger J., Toniolo D. A mutation in the X-linked emery-dreifuss muscular dystrophy gene in a patient affected with conduction cardiomyopathy. Neuromuscul Disord 2001, 11:411-413.
    • (2001) Neuromuscul Disord , vol.11 , pp. 411-413
    • Vohanka, S.1    Vytopil, M.2    Bednarik, J.3    Lukas, Z.4    Kadanka, Z.5    Schildberger, J.6    Toniolo, D.7
  • 79
    • 80053966315 scopus 로고    scopus 로고
    • Repetitive disruptions of the nuclear envelope invoke temporary loss of cellular compartmentalization in laminopathies
    • De Vos W.H., Houben F., Kamps M., Malhas A., Verheyen F., Cox J., Broers J.L. Repetitive disruptions of the nuclear envelope invoke temporary loss of cellular compartmentalization in laminopathies. Hum Mol Genet 2011, 20:4175-4186. 10.1093/hmg/ddr344.
    • (2011) Hum Mol Genet , vol.20 , pp. 4175-4186
    • De Vos, W.H.1    Houben, F.2    Kamps, M.3    Malhas, A.4    Verheyen, F.5    Cox, J.6    Broers, J.L.7
  • 80
    • 84860122715 scopus 로고    scopus 로고
    • Transient nuclear envelope rupturing during interphase in human cancer cells
    • Vargas J.D., Hatch E.M., Anderson D.J., Hetzer M.W. Transient nuclear envelope rupturing during interphase in human cancer cells. Nucleus (Austin, Tex) 2012, 3:88-100. 10.4161/nucl.18954.
    • (2012) Nucleus (Austin, Tex) , vol.3 , pp. 88-100
    • Vargas, J.D.1    Hatch, E.M.2    Anderson, D.J.3    Hetzer, M.W.4
  • 81
    • 8544264593 scopus 로고    scopus 로고
    • Intranuclear rodlets in the substantia nigra: interactions with marinesco bodies, ubiquitin, and promyelocytic leukemia protein
    • Woulfe J., Gray D., Prichett-Pejic W., Munoz D.G., Chretien M. Intranuclear rodlets in the substantia nigra: interactions with marinesco bodies, ubiquitin, and promyelocytic leukemia protein. J Neuropathol Exp Neurol 2004, 63:1200-1207.
    • (2004) J Neuropathol Exp Neurol , vol.63 , pp. 1200-1207
    • Woulfe, J.1    Gray, D.2    Prichett-Pejic, W.3    Munoz, D.G.4    Chretien, M.5
  • 82
    • 33846262456 scopus 로고    scopus 로고
    • Abnormalities of the nucleus and nuclear inclusions in neurodegenerative disease: a work in progress
    • Woulfe J.M. Abnormalities of the nucleus and nuclear inclusions in neurodegenerative disease: a work in progress. Neuropathol Appl Neurobiol 2007, 33:2-42. 10.1111/j.1365-2990.2006.00819.x.
    • (2007) Neuropathol Appl Neurobiol , vol.33 , pp. 2-42
    • Woulfe, J.M.1
  • 83
    • 0027985787 scopus 로고
    • Identification of a novel X-linked gene responsible for emery-dreifuss muscular dystrophy
    • Bione S., Maestrini E., Rivella S., Mancini M., Regis S., Romeo G., Toniolo D. Identification of a novel X-linked gene responsible for emery-dreifuss muscular dystrophy. Nat Genet 1994, 8:323-327. 10.1038/ng1294-323.
    • (1994) Nat Genet , vol.8 , pp. 323-327
    • Bione, S.1    Maestrini, E.2    Rivella, S.3    Mancini, M.4    Regis, S.5    Romeo, G.6    Toniolo, D.7
  • 84
    • 80052100421 scopus 로고    scopus 로고
    • Generation of induced pluripotent stem cell lines from 3 distinct laminopathies bearing heterogeneous mutations in lamin A/C
    • Ho J.C., Zhou T., Lai W.H., Huang Y., Chan Y.C., Li X., Esteban M.A. Generation of induced pluripotent stem cell lines from 3 distinct laminopathies bearing heterogeneous mutations in lamin A/C. Aging (Milano) 2011, 3:380-390.
    • (2011) Aging (Milano) , vol.3 , pp. 380-390
    • Ho, J.C.1    Zhou, T.2    Lai, W.H.3    Huang, Y.4    Chan, Y.C.5    Li, X.6    Esteban, M.A.7
  • 85
    • 79954626173 scopus 로고    scopus 로고
    • Recapitulation of premature ageing with iPSCs from Hutchinson-Gilford progeria syndrome
    • Liu G.H., Barkho B.Z., Ruiz S., Diep D., Qu J., Yang S.L., Izpisua Belmonte J.C. Recapitulation of premature ageing with iPSCs from Hutchinson-Gilford progeria syndrome. Nature 2011, 472:221-225. 10.1038/nature09879.
    • (2011) Nature , vol.472 , pp. 221-225
    • Liu, G.H.1    Barkho, B.Z.2    Ruiz, S.3    Diep, D.4    Qu, J.5    Yang, S.L.6    Izpisua Belmonte, J.C.7


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