메뉴 건너뛰기




Volumn 24, Issue 4, 2014, Pages 221-229

Destination: Inner nuclear membrane

Author keywords

Inner nuclear membrane; LEM domain; NPC; Nuclear transport; SUN protein

Indexed keywords

CELL RECEPTOR; CIS ACTING ELEMENT; INNER NUCLEAR MEMBRANE PROTEIN; KARYOPHERIN; LAMIN B RECEPTOR; LAMINA ASSOCIATED POLYPEPTIDE 2 BETA; LEM DOMAIN CONTAINING PROTEIN 3; LEM PROTEIN; MEMBRANE PROTEIN; NUCLEAR PROTEIN; OUTER NUCLEAR MEMBRANE PROTEIN; RAN PROTEIN; RNA; SEC61 TRANSLOCON; SUN PROTEIN; TRANS ACTING FACTOR; TRANSLOCON; UNCLASSIFIED DRUG; WNT PROTEIN; NUCLEOPORIN; PROTEIN BINDING;

EID: 84897049480     PISSN: 09628924     EISSN: 18793088     Source Type: Journal    
DOI: 10.1016/j.tcb.2013.10.006     Document Type: Review
Times cited : (87)

References (88)
  • 1
    • 84858176255 scopus 로고    scopus 로고
    • The yeast nuclear pore complex and transport through it
    • Aitchison J.D., Rout M.P. The yeast nuclear pore complex and transport through it. Genetics 2012, 190:855-883.
    • (2012) Genetics , vol.190 , pp. 855-883
    • Aitchison, J.D.1    Rout, M.P.2
  • 2
    • 84861384878 scopus 로고    scopus 로고
    • Functional architecture of the nuclear pore complex
    • Grossman E., et al. Functional architecture of the nuclear pore complex. Annu. Rev. Biophys. 2012, 41:557-584.
    • (2012) Annu. Rev. Biophys. , vol.41 , pp. 557-584
    • Grossman, E.1
  • 3
    • 73349134975 scopus 로고    scopus 로고
    • Flexible gates: dynamic topologies and functions for FG nucleoporins in nucleocytoplasmic transport
    • Terry L.J., Wente S.R. Flexible gates: dynamic topologies and functions for FG nucleoporins in nucleocytoplasmic transport. Eukaryot. Cell 2009, 8:1814-1827.
    • (2009) Eukaryot. Cell , vol.8 , pp. 1814-1827
    • Terry, L.J.1    Wente, S.R.2
  • 4
    • 36749088906 scopus 로고    scopus 로고
    • Determining the architectures of macromolecular assemblies
    • Alber F., et al. Determining the architectures of macromolecular assemblies. Nature 2007, 450:683-694.
    • (2007) Nature , vol.450 , pp. 683-694
    • Alber, F.1
  • 5
    • 36749045172 scopus 로고    scopus 로고
    • The molecular architecture of the nuclear pore complex
    • Alber F., et al. The molecular architecture of the nuclear pore complex. Nature 2007, 450:695-701.
    • (2007) Nature , vol.450 , pp. 695-701
    • Alber, F.1
  • 6
    • 84861966443 scopus 로고    scopus 로고
    • The human nuclear pore complex as revealed by cryo-electron tomography
    • Maimon T., et al. The human nuclear pore complex as revealed by cryo-electron tomography. Structure 2012, 20:998-1006.
    • (2012) Structure , vol.20 , pp. 998-1006
    • Maimon, T.1
  • 7
    • 25144491496 scopus 로고    scopus 로고
    • The nuclear membrane proteome: extending the envelope
    • Schirmer E.C., Gerace L. The nuclear membrane proteome: extending the envelope. Trends Biochem. Sci. 2005, 30:551-558.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 551-558
    • Schirmer, E.C.1    Gerace, L.2
  • 8
    • 84872483388 scopus 로고    scopus 로고
    • The nuclear envelope proteome differs notably between tissues
    • Korfali N., et al. The nuclear envelope proteome differs notably between tissues. Nucleus 2012, 3:552-564.
    • (2012) Nucleus , vol.3 , pp. 552-564
    • Korfali, N.1
  • 9
    • 78049394356 scopus 로고    scopus 로고
    • Interactions between nuclei and the cytoskeleton are mediated by SUN-KASH nuclear-envelope bridges
    • Starr D.A., Fridolfsson H.N. Interactions between nuclei and the cytoskeleton are mediated by SUN-KASH nuclear-envelope bridges. Annu. Rev. Cell Dev. Biol. 2010, 26:421-444.
    • (2010) Annu. Rev. Cell Dev. Biol. , vol.26 , pp. 421-444
    • Starr, D.A.1    Fridolfsson, H.N.2
  • 10
    • 84885846858 scopus 로고    scopus 로고
    • The diverse functional LINCs of the nuclear envelope to the cytoskeleton and chromatin
    • Rothballer A., Kutay U. The diverse functional LINCs of the nuclear envelope to the cytoskeleton and chromatin. Chromosoma 2013, 122:415-429.
    • (2013) Chromosoma , vol.122 , pp. 415-429
    • Rothballer, A.1    Kutay, U.2
  • 11
    • 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.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 317-328
    • Mekhail, K.1    Moazed, D.2
  • 12
    • 84877825124 scopus 로고    scopus 로고
    • Building silent compartments at the nuclear periphery: a recurrent theme
    • Meister P., Taddei A. Building silent compartments at the nuclear periphery: a recurrent theme. Curr. Opin. Genet. Dev. 2013, 23:96-103.
    • (2013) Curr. Opin. Genet. Dev. , vol.23 , pp. 96-103
    • Meister, P.1    Taddei, A.2
  • 13
    • 84866109279 scopus 로고    scopus 로고
    • Structure and function in the budding yeast nucleus
    • Taddei A., Gasser S.M. Structure and function in the budding yeast nucleus. Genetics 2012, 192:107-129.
    • (2012) Genetics , vol.192 , pp. 107-129
    • Taddei, A.1    Gasser, S.M.2
  • 14
    • 84887476450 scopus 로고    scopus 로고
    • Transcriptional regulation at the yeast nuclear envelope
    • Steglich B., et al. Transcriptional regulation at the yeast nuclear envelope. Nucleus 2013, 4:379-389.
    • (2013) Nucleus , vol.4 , pp. 379-389
    • Steglich, B.1
  • 16
    • 36749031152 scopus 로고    scopus 로고
    • Blurring the boundary: the nuclear envelope extends its reach
    • Stewart C.L., et al. Blurring the boundary: the nuclear envelope extends its reach. Science 2007, 318:1408-1412.
    • (2007) Science , vol.318 , pp. 1408-1412
    • Stewart, C.L.1
  • 17
    • 80054902318 scopus 로고    scopus 로고
    • The nucleoskeleton as a genome-associated dynamic 'network of networks'
    • Simon D.N., Wilson K.L. The nucleoskeleton as a genome-associated dynamic 'network of networks'. Nat. Rev. Mol. Cell Biol. 2011, 12:695-708.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 695-708
    • Simon, D.N.1    Wilson, K.L.2
  • 18
    • 84876499240 scopus 로고    scopus 로고
    • Partners and post-translational modifications of nuclear lamins
    • Simon D.N., Wilson K.L. Partners and post-translational modifications of nuclear lamins. Chromosoma 2013, 122:13-31.
    • (2013) Chromosoma , vol.122 , pp. 13-31
    • Simon, D.N.1    Wilson, K.L.2
  • 19
    • 84875175486 scopus 로고    scopus 로고
    • When lamins go bad: nuclear structure and disease
    • Schreiber K.H., Kennedy B.K. When lamins go bad: nuclear structure and disease. Cell 2013, 152:1365-1375.
    • (2013) Cell , vol.152 , pp. 1365-1375
    • Schreiber, K.H.1    Kennedy, B.K.2
  • 20
    • 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.
    • (2009) Dev. Cell , vol.17 , pp. 626-638
    • Dauer, W.T.1    Worman, H.J.2
  • 21
    • 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.
    • (2012) Chromosoma , vol.121 , pp. 153-167
    • Mendez-Lopez, I.1    Worman, H.J.2
  • 22
    • 0031969698 scopus 로고    scopus 로고
    • Aberrant intracellular targeting and cell cycle-dependent phosphorylation of emerin contribute to the Emery-Dreifuss muscular dystrophy phenotype
    • Ellis J.A., et al. Aberrant intracellular targeting and cell cycle-dependent phosphorylation of emerin contribute to the Emery-Dreifuss muscular dystrophy phenotype. J. Cell Sci. 1998, 111:781-792.
    • (1998) J. Cell Sci. , vol.111 , pp. 781-792
    • Ellis, J.A.1
  • 23
    • 0036193442 scopus 로고    scopus 로고
    • Lamin-dependent localization of UNC-84, a protein required for nuclear migration in Caenorhabditis elegans
    • Lee K.K., et al. Lamin-dependent localization of UNC-84, a protein required for nuclear migration in Caenorhabditis elegans. Mol. Biol. Cell 2002, 13:892-901.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 892-901
    • Lee, K.K.1
  • 24
    • 78651103909 scopus 로고    scopus 로고
    • Lamin A variants that cause striated muscle disease are defective in anchoring transmembrane actin-associated nuclear lines for nuclear movement
    • Folker E.S., et al. Lamin A variants that cause striated muscle disease are defective in anchoring transmembrane actin-associated nuclear lines for nuclear movement. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:131-136.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 131-136
    • Folker, E.S.1
  • 25
    • 0033615969 scopus 로고    scopus 로고
    • Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy
    • Sullivan T., et al. 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
  • 26
    • 0037081564 scopus 로고    scopus 로고
    • The cell cycle dependent mislocalisation of emerin may contribute to the Emery-Dreifuss muscular dystrophy phenotype
    • Fairley E.A., et al. The cell cycle dependent mislocalisation of emerin may contribute to the Emery-Dreifuss muscular dystrophy phenotype. J. Cell Sci. 2002, 115:341-354.
    • (2002) J. Cell Sci. , vol.115 , pp. 341-354
    • Fairley, E.A.1
  • 27
    • 77449109551 scopus 로고    scopus 로고
    • Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes
    • Haque F., et al. Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes. J. Biol. Chem. 2010, 285:3487-3498.
    • (2010) J. Biol. Chem. , vol.285 , pp. 3487-3498
    • Haque, F.1
  • 28
    • 80052230265 scopus 로고    scopus 로고
    • Ran-dependent nuclear export mediators: a structural perspective
    • Guttler T., Gorlich D. Ran-dependent nuclear export mediators: a structural perspective. EMBO J. 2011, 30:3457-3474.
    • (2011) EMBO J. , vol.30 , pp. 3457-3474
    • Guttler, T.1    Gorlich, D.2
  • 29
    • 78649650714 scopus 로고    scopus 로고
    • Recognition of nuclear targeting signals by Karyopherin-beta proteins
    • Xu D., et al. Recognition of nuclear targeting signals by Karyopherin-beta proteins. Curr. Opin. Struct. Biol. 2010, 20:782-790.
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 782-790
    • Xu, D.1
  • 30
    • 84880964277 scopus 로고    scopus 로고
    • Postage for the messenger: designating routes for nuclear mRNA export
    • Natalizio B.J., Wente S.R. Postage for the messenger: designating routes for nuclear mRNA export. Trends Cell Biol. 2013, 23:365-373.
    • (2013) Trends Cell Biol. , vol.23 , pp. 365-373
    • Natalizio, B.J.1    Wente, S.R.2
  • 31
    • 84861361690 scopus 로고    scopus 로고
    • Mechanisms of Sec61/SecY-mediated protein translocation across membranes
    • Park E., Rapoport T.A. Mechanisms of Sec61/SecY-mediated protein translocation across membranes. Annu. Rev. Biophys. 2012, 41:21-40.
    • (2012) Annu. Rev. Biophys. , vol.41 , pp. 21-40
    • Park, E.1    Rapoport, T.A.2
  • 32
    • 4644356464 scopus 로고    scopus 로고
    • Membrane-protein integration and the role of the translocation channel
    • Rapoport T.A., et al. Membrane-protein integration and the role of the translocation channel. Trends Cell Biol. 2004, 14:568-575.
    • (2004) Trends Cell Biol. , vol.14 , pp. 568-575
    • Rapoport, T.A.1
  • 33
    • 0033021606 scopus 로고    scopus 로고
    • Intracellular trafficking of emerin, the Emery-Dreifuss muscular dystrophy protein
    • Ostlund C., et al. Intracellular trafficking of emerin, the Emery-Dreifuss muscular dystrophy protein. J. Cell Sci. 1999, 112:1709-1719.
    • (1999) J. Cell Sci. , vol.112 , pp. 1709-1719
    • Ostlund, C.1
  • 34
    • 0030763228 scopus 로고    scopus 로고
    • Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase and mitosis
    • Ellenberg J., et al. Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase and mitosis. J. Cell Biol. 1997, 138:1193-1206.
    • (1997) J. Cell Biol. , vol.138 , pp. 1193-1206
    • Ellenberg, J.1
  • 35
    • 0036538599 scopus 로고    scopus 로고
    • Intracellular trafficking of MAN1, an integral protein of the nuclear envelope inner membrane
    • Wu W., et al. Intracellular trafficking of MAN1, an integral protein of the nuclear envelope inner membrane. J. Cell Sci. 2002, 115:1361-1371.
    • (2002) J. Cell Sci. , vol.115 , pp. 1361-1371
    • Wu, W.1
  • 36
    • 1842578717 scopus 로고    scopus 로고
    • Dynamic interaction between BAF and emerin revealed by FRAP, FLIP, and FRET analyese in living HeLa cells
    • Shimi T., et al. Dynamic interaction between BAF and emerin revealed by FRAP, FLIP, and FRET analyese in living HeLa cells. J. Struct. Biol. 2004, 147:31-41.
    • (2004) J. Struct. Biol. , vol.147 , pp. 31-41
    • Shimi, T.1
  • 37
    • 11244316478 scopus 로고    scopus 로고
    • Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore
    • Ohba T., et al. Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore. J. Cell Biol. 2004, 167:1051-1062.
    • (2004) J. Cell Biol. , vol.167 , pp. 1051-1062
    • Ohba, T.1
  • 38
    • 0025247954 scopus 로고
    • Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components
    • Reichelt R., et al. Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components. J. Cell Biol. 1990, 110:883-894.
    • (1990) J. Cell Biol. , vol.110 , pp. 883-894
    • Reichelt, R.1
  • 39
    • 0026776959 scopus 로고
    • Architecture and design of the nuclear pore complex
    • Hindshaw J.E., et al. Architecture and design of the nuclear pore complex. Cell 1992, 69:1133-1141.
    • (1992) Cell , vol.69 , pp. 1133-1141
    • Hindshaw, J.E.1
  • 40
    • 0027500249 scopus 로고
    • The amino-terminal domain of the lamin B receptor is a nuclear envelope targeting signal
    • Soullam B., Worman H.J. The amino-terminal domain of the lamin B receptor is a nuclear envelope targeting signal. J. Cell Biol. 1993, 120:1093-1100.
    • (1993) J. Cell Biol. , vol.120 , pp. 1093-1100
    • Soullam, B.1    Worman, H.J.2
  • 41
    • 0029069183 scopus 로고
    • Signals and structural features involved in integral membrane protein targeting to the inner nuclear membrane
    • Soullam B., Worman H.J. Signals and structural features involved in integral membrane protein targeting to the inner nuclear membrane. J. Cell Biol. 1995, 130:15-27.
    • (1995) J. Cell Biol. , vol.130 , pp. 15-27
    • Soullam, B.1    Worman, H.J.2
  • 42
    • 0032512832 scopus 로고    scopus 로고
    • The major nuclear envelope targeting domain of LAP2 coincides with its lamin binding region but is distinct from its chromatin interaction domain
    • Furukawa K., et al. The major nuclear envelope targeting domain of LAP2 coincides with its lamin binding region but is distinct from its chromatin interaction domain. J. Biol. Chem. 1998, 273:4213-4219.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4213-4219
    • Furukawa, K.1
  • 43
    • 79955502505 scopus 로고    scopus 로고
    • System analysis shows distinct mechanisms and common principles of nuclear envelope protein dynamics
    • Zuleger N., et al. System analysis shows distinct mechanisms and common principles of nuclear envelope protein dynamics. J. Cell Biol. 2011, 193:109-123.
    • (2011) J. Cell Biol. , vol.193 , pp. 109-123
    • Zuleger, N.1
  • 44
    • 79955966597 scopus 로고    scopus 로고
    • Multiple mechanisms actively target the SUN protein UNC-84 to the inner nuclear membrane
    • Tapley E.C., et al. Multiple mechanisms actively target the SUN protein UNC-84 to the inner nuclear membrane. Mol. Biol. Cell 2011, 22:1739-1752.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 1739-1752
    • Tapley, E.C.1
  • 45
    • 0028989340 scopus 로고
    • Cloning of a cDNA for lamina-associated polypeptide 2 (LAP2) and identification of regions that specify targeting to the nuclear envelope
    • Furukawa K., et al. Cloning of a cDNA for lamina-associated polypeptide 2 (LAP2) and identification of regions that specify targeting to the nuclear envelope. EMBO J. 1995, 14:1626-1636.
    • (1995) EMBO J. , vol.14 , pp. 1626-1636
    • Furukawa, K.1
  • 46
    • 31344435644 scopus 로고    scopus 로고
    • The Drosophila melanogaster LEM-domain protein MAN1
    • Wagner N., et al. The Drosophila melanogaster LEM-domain protein MAN1. Eur. J. Cell Biol. 2006, 85:91-105.
    • (2006) Eur. J. Cell Biol. , vol.85 , pp. 91-105
    • Wagner, N.1
  • 47
    • 56049115622 scopus 로고    scopus 로고
    • Tissue-specific defects are caused by loss of the Drosophila MAN1 LEM domain protein
    • Pinto B.S., et al. Tissue-specific defects are caused by loss of the Drosophila MAN1 LEM domain protein. Genetics 2008, 180:133-145.
    • (2008) Genetics , vol.180 , pp. 133-145
    • Pinto, B.S.1
  • 48
    • 33748310680 scopus 로고    scopus 로고
    • Karyopherin-mediated import of integral inner nuclear membrane proteins
    • King M.C., et al. Karyopherin-mediated import of integral inner nuclear membrane proteins. Nature 2006, 442:1003-1007.
    • (2006) Nature , vol.442 , pp. 1003-1007
    • King, M.C.1
  • 49
    • 34247364639 scopus 로고    scopus 로고
    • Highway to the inner nuclear membrane: rules for the road
    • Lusk C.P., et al. Highway to the inner nuclear membrane: rules for the road. Nat. Rev. Mol. Cell Biol. 2007, 8:414-420.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 414-420
    • Lusk, C.P.1
  • 50
    • 76449106819 scopus 로고    scopus 로고
    • Transport of inner nuclear membrane proteins
    • Landes Bioscience, R.H. Kehlenbach (Ed.)
    • Malik P., et al. Transport of inner nuclear membrane proteins. Nuclear Transport 2009, 133-145. Landes Bioscience. R.H. Kehlenbach (Ed.).
    • (2009) Nuclear Transport , pp. 133-145
    • Malik, P.1
  • 51
    • 33750349837 scopus 로고    scopus 로고
    • Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase
    • Deng M., Hochstrasser M. Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase. Nature 2006, 443:827-831.
    • (2006) Nature , vol.443 , pp. 827-831
    • Deng, M.1    Hochstrasser, M.2
  • 52
    • 79959846745 scopus 로고    scopus 로고
    • Long unfolded linkers facilitate membrane protein import through the nuclear pore complex
    • Meinema A.C., et al. Long unfolded linkers facilitate membrane protein import through the nuclear pore complex. Science 2011, 333:90-93.
    • (2011) Science , vol.333 , pp. 90-93
    • Meinema, A.C.1
  • 53
    • 52049084405 scopus 로고    scopus 로고
    • The anchor-away technique: rapid, conditional establishment of yeast mutant phenotypes
    • Haruki H., et al. The anchor-away technique: rapid, conditional establishment of yeast mutant phenotypes. Mol. Cell 2008, 31:925-932.
    • (2008) Mol. Cell , vol.31 , pp. 925-932
    • Haruki, H.1
  • 54
    • 84876124126 scopus 로고    scopus 로고
    • Quantitative analysis of membrane protein transport across the nuclear pore complex
    • Meinema A.C., et al. Quantitative analysis of membrane protein transport across the nuclear pore complex. Traffic 2013, 14:487-501.
    • (2013) Traffic , vol.14 , pp. 487-501
    • Meinema, A.C.1
  • 55
    • 77954886484 scopus 로고    scopus 로고
    • A classical NLS and the SUN domain contribute to the targeting of SUN2 to the inner nuclear membrane
    • Turgay Y., et al. A classical NLS and the SUN domain contribute to the targeting of SUN2 to the inner nuclear membrane. EMBO J. 2010, 29:2262-2275.
    • (2010) EMBO J. , vol.29 , pp. 2262-2275
    • Turgay, Y.1
  • 56
    • 2942614889 scopus 로고    scopus 로고
    • Trafficking of ODV-E66 is mediated via a sorting motif and other viral proteins: facilitated trafficking to the inner nuclear membrane
    • Braunagel S.C., et al. Trafficking of ODV-E66 is mediated via a sorting motif and other viral proteins: facilitated trafficking to the inner nuclear membrane. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:8372-8377.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 8372-8377
    • Braunagel, S.C.1
  • 57
    • 4344645948 scopus 로고    scopus 로고
    • Cotranslational integration and initial sorting at the endoplasmic reticulum translocon of proteins destined for the inner nuclear membrane
    • Saksena S., et al. Cotranslational integration and initial sorting at the endoplasmic reticulum translocon of proteins destined for the inner nuclear membrane. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:12537-12542.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 12537-12542
    • Saksena, S.1
  • 58
    • 84884411179 scopus 로고    scopus 로고
    • Anchors aweigh: protein localization and transport mediated by transmembrane domains
    • Cosson P., et al. Anchors aweigh: protein localization and transport mediated by transmembrane domains. Trends Cell Biol. 2013, 23:511-517.
    • (2013) Trends Cell Biol. , vol.23 , pp. 511-517
    • Cosson, P.1
  • 59
    • 33744915536 scopus 로고    scopus 로고
    • Importin-alpha-16 is a translocon-associated protein involved in sorting membrane proteins to the nuclear envelope
    • Saksena S., et al. Importin-alpha-16 is a translocon-associated protein involved in sorting membrane proteins to the nuclear envelope. Nat. Struct. Mol. Biol. 2006, 13:500-508.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 500-508
    • Saksena, S.1
  • 60
    • 34547229757 scopus 로고    scopus 로고
    • Early sorting of inner nuclear membrane proteins is conserved
    • Braunagel S.C., et al. Early sorting of inner nuclear membrane proteins is conserved. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:9307-9312.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 9307-9312
    • Braunagel, S.C.1
  • 61
    • 33744950130 scopus 로고    scopus 로고
    • A sorting importin on Sec61
    • Rexach M.F. A sorting importin on Sec61. Nat. Struct. Mol. Biol. 2006, 13:476-478.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 476-478
    • Rexach, M.F.1
  • 62
    • 0034725636 scopus 로고    scopus 로고
    • Truncated form of importin alpha identified in breast cancer cell inhibits nuclear import of p53
    • Kim I.S., et al. Truncated form of importin alpha identified in breast cancer cell inhibits nuclear import of p53. J. Biol. Chem. 2000, 275:23139-23145.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23139-23145
    • Kim, I.S.1
  • 63
    • 78349279170 scopus 로고    scopus 로고
    • Truncated isoforms of Kap60 facilitate trafficking of Heh2 to the nuclear envelope
    • Liu D., et al. Truncated isoforms of Kap60 facilitate trafficking of Heh2 to the nuclear envelope. Traffic 2010, 11:1506-1518.
    • (2010) Traffic , vol.11 , pp. 1506-1518
    • Liu, D.1
  • 64
    • 59749094731 scopus 로고    scopus 로고
    • Baculovirus data suggest a common but multifaceted pathway for sorting proteins to the inner nuclear membrane
    • Braunagel S.C., et al. Baculovirus data suggest a common but multifaceted pathway for sorting proteins to the inner nuclear membrane. J. Virol. 2009, 83:1280-1288.
    • (2009) J. Virol. , vol.83 , pp. 1280-1288
    • Braunagel, S.C.1
  • 65
    • 27744577638 scopus 로고    scopus 로고
    • Nup50/Npap60 function in nuclear protein import complex disassembly and importin recycling
    • Matsuura Y., Stewart M. Nup50/Npap60 function in nuclear protein import complex disassembly and importin recycling. EMBO J. 2005, 24:3681-3689.
    • (2005) EMBO J. , vol.24 , pp. 3681-3689
    • Matsuura, Y.1    Stewart, M.2
  • 66
    • 4444291705 scopus 로고    scopus 로고
    • Importin alpha: a multipurpose nuclear-transport receptor
    • Goldfarb D.S., et al. Importin alpha: a multipurpose nuclear-transport receptor. Trends Cell Biol. 2004, 14:505-514.
    • (2004) Trends Cell Biol. , vol.14 , pp. 505-514
    • Goldfarb, D.S.1
  • 67
    • 0345803001 scopus 로고    scopus 로고
    • Molecular basis for the rapid dissociation of nuclear localization signals from karyopherin alpha in the nucleoplasm
    • Gilchrist D., Rexach M. Molecular basis for the rapid dissociation of nuclear localization signals from karyopherin alpha in the nucleoplasm. J. Biol. Chem. 2003, 278:51937-51949.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51937-51949
    • Gilchrist, D.1    Rexach, M.2
  • 68
    • 2942533937 scopus 로고    scopus 로고
    • Sun2 is a novel mammalian inner nuclear membrane protein
    • Hodzic D.M., et al. Sun2 is a novel mammalian inner nuclear membrane protein. J. Biol. Chem. 2004, 279:25805-25812.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25805-25812
    • Hodzic, D.M.1
  • 69
    • 79956226201 scopus 로고    scopus 로고
    • Targeting of the SUN protein Mps3 to the inner nuclear membrane by the histone variant H2A.Z
    • Gardner J.M., et al. Targeting of the SUN protein Mps3 to the inner nuclear membrane by the histone variant H2A.Z. J. Cell Biol. 2011, 193:489-507.
    • (2011) J. Cell Biol. , vol.193 , pp. 489-507
    • Gardner, J.M.1
  • 70
    • 84863511126 scopus 로고    scopus 로고
    • Acetylation of the SUN protein Mps3 by Eco1 regulates its function in nuclear organization
    • Ghosh S., et al. Acetylation of the SUN protein Mps3 by Eco1 regulates its function in nuclear organization. Mol. Biol. Cell 2012, 23:2546-2559.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 2546-2559
    • Ghosh, S.1
  • 71
    • 36849008181 scopus 로고    scopus 로고
    • Telomere anchoring at the nuclear periphery requires the budding yeast Sad1-UNC-84 domain protein Mps3
    • Bupp J.M., et al. Telomere anchoring at the nuclear periphery requires the budding yeast Sad1-UNC-84 domain protein Mps3. J. Cell Biol. 2007, 179:845-854.
    • (2007) J. Cell Biol. , vol.179 , pp. 845-854
    • Bupp, J.M.1
  • 72
    • 30944461855 scopus 로고    scopus 로고
    • Hide and run. Arginine-based endoplasmic-reticulum-sorting motifs in the assembly of heteromultimeric membrane proteins
    • Michelsen K., et al. Hide and run. Arginine-based endoplasmic-reticulum-sorting motifs in the assembly of heteromultimeric membrane proteins. EMBO Rep. 2005, 6:717-722.
    • (2005) EMBO Rep. , vol.6 , pp. 717-722
    • Michelsen, K.1
  • 73
    • 84878253184 scopus 로고    scopus 로고
    • Organization of the ER-Golgi interface for membrane traffic control
    • Brandizzi F., Barlowe C. Organization of the ER-Golgi interface for membrane traffic control. Nat. Rev. Mol. Cell Biol. 2013, 14:382-392.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 382-392
    • Brandizzi, F.1    Barlowe, C.2
  • 74
    • 84860852545 scopus 로고    scopus 로고
    • Nuclear envelope budding enables large ribonucleoprotein particle export during synaptic Wnt signaling
    • Speese S.D., et al. Nuclear envelope budding enables large ribonucleoprotein particle export during synaptic Wnt signaling. Cell 2012, 149:832-846.
    • (2012) Cell , vol.149 , pp. 832-846
    • Speese, S.D.1
  • 75
    • 84872616937 scopus 로고    scopus 로고
    • The way out: what we know and do not know about herpesvirus nuclear egress
    • Mettenleiter T.C., et al. The way out: what we know and do not know about herpesvirus nuclear egress. Cell. Microbiol. 2013, 15:170-178.
    • (2013) Cell. Microbiol. , vol.15 , pp. 170-178
    • Mettenleiter, T.C.1
  • 76
    • 79954599465 scopus 로고    scopus 로고
    • Herpesviruses remodel host membranes for virus egress
    • Johnson D.C., Baines J.D. Herpesviruses remodel host membranes for virus egress. Nat. Rev. Microbiol. 2011, 9:382-394.
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 382-394
    • Johnson, D.C.1    Baines, J.D.2
  • 77
    • 44449165125 scopus 로고    scopus 로고
    • Nuclear translocation of Gln3 in response to nutrient signals requires Golgi-to-endosome trafficking in Saccharomyces cerevisiae
    • Puria R., et al. Nuclear translocation of Gln3 in response to nutrient signals requires Golgi-to-endosome trafficking in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:7194-7199.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 7194-7199
    • Puria, R.1
  • 78
    • 84876447241 scopus 로고    scopus 로고
    • Vps factors are required for efficient transcription elongation in budding yeast
    • Gaur N.A., et al. Vps factors are required for efficient transcription elongation in budding yeast. Genetics 2013, 193:829-851.
    • (2013) Genetics , vol.193 , pp. 829-851
    • Gaur, N.A.1
  • 79
    • 79955703186 scopus 로고    scopus 로고
    • Phosphoinositide [PI(3,5)P2] lipid-dependent regulation of the general transcriptional regulator Tup1
    • Han B.K., Emr S.D. Phosphoinositide [PI(3,5)P2] lipid-dependent regulation of the general transcriptional regulator Tup1. Genes Dev. 2011, 25:984-995.
    • (2011) Genes Dev. , vol.25 , pp. 984-995
    • Han, B.K.1    Emr, S.D.2
  • 80
    • 84862902975 scopus 로고    scopus 로고
    • Many mechanisms, one entrance: membrane protein translocation into the nucleus
    • Zuleger N., et al. Many mechanisms, one entrance: membrane protein translocation into the nucleus. Cell. Mol. Life Sci. 2012, 69:2205-2216.
    • (2012) Cell. Mol. Life Sci. , vol.69 , pp. 2205-2216
    • Zuleger, N.1
  • 81
    • 68749112707 scopus 로고    scopus 로고
    • Importing mitochondrial proteins: machineries and mechanisms
    • Chacinska A., et al. Importing mitochondrial proteins: machineries and mechanisms. Cell 2009, 138:628-644.
    • (2009) Cell , vol.138 , pp. 628-644
    • Chacinska, A.1
  • 82
    • 77954759289 scopus 로고    scopus 로고
    • Nuclear trafficking of the epidermal growth factor receptor family membrane proteins
    • Wang Y.N., et al. Nuclear trafficking of the epidermal growth factor receptor family membrane proteins. Oncogene 2010, 29:3997-4006.
    • (2010) Oncogene , vol.29 , pp. 3997-4006
    • Wang, Y.N.1
  • 83
    • 78649681031 scopus 로고    scopus 로고
    • The translocon Sec61beta localized in the inner nuclear membrane transports membrane-embedded EGF receptor to the nucleus
    • Wang Y.N., et al. The translocon Sec61beta localized in the inner nuclear membrane transports membrane-embedded EGF receptor to the nucleus. J. Biol. Chem. 2010, 285:38720-38729.
    • (2010) J. Biol. Chem. , vol.285 , pp. 38720-38729
    • Wang, Y.N.1
  • 84
    • 79953323939 scopus 로고    scopus 로고
    • Traversing the NPC along the pore membrane: targeting of membrane proteins to the INM
    • Antonin W., et al. Traversing the NPC along the pore membrane: targeting of membrane proteins to the INM. Nucleus 2011, 2:87-91.
    • (2011) Nucleus , vol.2 , pp. 87-91
    • Antonin, W.1
  • 85
    • 78049508819 scopus 로고    scopus 로고
    • Pom121 links two essential subcomplexes of the nuclear pore complex core to the membrane
    • Mitchell J.M., et al. Pom121 links two essential subcomplexes of the nuclear pore complex core to the membrane. J. Cell Biol. 2010, 191:505-521.
    • (2010) J. Cell Biol. , vol.191 , pp. 505-521
    • Mitchell, J.M.1
  • 86
    • 32344452653 scopus 로고    scopus 로고
    • Nuclear envelope localization of human UNC84A does not require nuclear lamins
    • Hasan S., et al. Nuclear envelope localization of human UNC84A does not require nuclear lamins. FEBS Lett. 2006, 580:1263-1268.
    • (2006) FEBS Lett. , vol.580 , pp. 1263-1268
    • Hasan, S.1
  • 87
    • 34548320825 scopus 로고    scopus 로고
    • Functional association of Sun1 with nuclear pore complexes
    • Liu Q., et al. Functional association of Sun1 with nuclear pore complexes. J. Cell Biol. 2007, 178:785-798.
    • (2007) J. Cell Biol. , vol.178 , pp. 785-798
    • Liu, Q.1
  • 88
    • 84863816293 scopus 로고    scopus 로고
    • The transport of integral membrane proteins across the nuclear pore complex
    • Meinema A.C., et al. The transport of integral membrane proteins across the nuclear pore complex. Nucleus 2012, 3:322-329.
    • (2012) Nucleus , vol.3 , pp. 322-329
    • Meinema, A.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.