메뉴 건너뛰기




Volumn 1843, Issue 11, 2014, Pages 2784-2795

Macromolecular transport between the nucleus and the cytoplasm: Advances in mechanism and emerging links to disease

Author keywords

Karyopherin importin exportin; Nuclear pore; Nucleocytoplasmic transport; Protein import; RNA export; RNA processing

Indexed keywords

LAMIN; MESSENGER RNA; PROTEIN;

EID: 84907570608     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2014.08.003     Document Type: Review
Times cited : (80)

References (145)
  • 1
    • 84867786612 scopus 로고    scopus 로고
    • Nuclear pore complex composition: a new regulator of tissue-specific and developmental functions
    • Raices M., D'Angelo M.A. Nuclear pore complex composition: a new regulator of tissue-specific and developmental functions. Nat. Rev. Mol. Cell Biol. 2012, 13:687-699.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 687-699
    • Raices, M.1    D'Angelo, M.A.2
  • 2
    • 84861384878 scopus 로고    scopus 로고
    • Functional architecture of the nuclear pore complex
    • Grossman E., Medalia O., Zwerger M. 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    Medalia, O.2    Zwerger, M.3
  • 4
    • 84857689254 scopus 로고    scopus 로고
    • A jumbo problem: mapping the structure and functions of the nuclear pore complex
    • Fernandez-Martinez J., Rout M.P. A jumbo problem: mapping the structure and functions of the nuclear pore complex. Curr. Opin. Cell Biol. 2012, 24:92-99.
    • (2012) Curr. Opin. Cell Biol. , vol.24 , pp. 92-99
    • Fernandez-Martinez, J.1    Rout, M.P.2
  • 8
    • 0030031968 scopus 로고    scopus 로고
    • A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores
    • Siniossoglou S., Wimmer C., Rieger M., Doye V., Tekotte H., Weise C., Emig S., Segref A., Hurt E.C. A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores. Cell 1996, 84:265-275.
    • (1996) Cell , vol.84 , pp. 265-275
    • Siniossoglou, S.1    Wimmer, C.2    Rieger, M.3    Doye, V.4    Tekotte, H.5    Weise, C.6    Emig, S.7    Segref, A.8    Hurt, E.C.9
  • 11
    • 84894309215 scopus 로고    scopus 로고
    • Evidence for an evolutionary relationship between the large adaptor nucleoporin Nup192 and karyopherins
    • Stuwe T., Lina D.H., Collins L.N., Hurt E., Hoelz A. Evidence for an evolutionary relationship between the large adaptor nucleoporin Nup192 and karyopherins. Proc. Natl. Acad. Sci. U. S. A. 2014, 111:2530-2535.
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. 2530-2535
    • Stuwe, T.1    Lina, D.H.2    Collins, L.N.3    Hurt, E.4    Hoelz, A.5
  • 14
    • 33646482468 scopus 로고    scopus 로고
    • Karyopherin flexibility in nucleocytoplasmic transport
    • Conti E., Muller C.W., Stewart M. Karyopherin flexibility in nucleocytoplasmic transport. Curr. Opin. Struct. Biol. 2006, 16:237-244.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 237-244
    • Conti, E.1    Muller, C.W.2    Stewart, M.3
  • 15
    • 0032563246 scopus 로고    scopus 로고
    • Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha
    • Conti E., Uy M., Leighton L., Blobel G., Kuriyan J. Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha. Cell 1998, 94:193-204.
    • (1998) Cell , vol.94 , pp. 193-204
    • Conti, E.1    Uy, M.2    Leighton, L.3    Blobel, G.4    Kuriyan, J.5
  • 16
    • 0033612390 scopus 로고    scopus 로고
    • Structural view of the Ran-Importin beta interaction at 2.3A resolution
    • Vetter I.R., Arndt A., Kutay U., Gorlich D., Wittinghofer A. Structural view of the Ran-Importin beta interaction at 2.3A resolution. Cell 1999, 97:635-646.
    • (1999) Cell , vol.97 , pp. 635-646
    • Vetter, I.R.1    Arndt, A.2    Kutay, U.3    Gorlich, D.4    Wittinghofer, A.5
  • 17
    • 0033587167 scopus 로고    scopus 로고
    • Structure of importin-beta bound to the IBB domain of importin-alpha
    • Cingolani G., Petosa C., Weis K., Muller C.W. Structure of importin-beta bound to the IBB domain of importin-alpha. Nature 1999, 399:221-229.
    • (1999) Nature , vol.399 , pp. 221-229
    • Cingolani, G.1    Petosa, C.2    Weis, K.3    Muller, C.W.4
  • 18
    • 84875141193 scopus 로고    scopus 로고
    • Uncovering nuclear pore complexity with innovation
    • Adams R.L., Wente S.R. Uncovering nuclear pore complexity with innovation. Cell 2013, 152:1218-1221.
    • (2013) Cell , vol.152 , pp. 1218-1221
    • Adams, R.L.1    Wente, S.R.2
  • 20
    • 34948891095 scopus 로고    scopus 로고
    • Snapshots of nuclear pore complexes in action captured by cryo-electron tomography
    • Beck M., Lucic V., Forster F., Baumeister W., Medalia O. Snapshots of nuclear pore complexes in action captured by cryo-electron tomography. Nature 2007, 449:611-615.
    • (2007) Nature , vol.449 , pp. 611-615
    • Beck, M.1    Lucic, V.2    Forster, F.3    Baumeister, W.4    Medalia, O.5
  • 21
    • 77955884087 scopus 로고    scopus 로고
    • Relationships at the nuclear envelope: lamins and nuclear pore complexes in animals and plants
    • Fiserova J., Goldberg M.W. Relationships at the nuclear envelope: lamins and nuclear pore complexes in animals and plants. Biochem. Soc. Trans. 2010, 38:829-831.
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 829-831
    • Fiserova, J.1    Goldberg, M.W.2
  • 22
    • 84900520197 scopus 로고    scopus 로고
    • Toward understanding the structure of the vertebrate nuclear pore complex
    • Beck M., Glavy J.S. Toward understanding the structure of the vertebrate nuclear pore complex. Nucleus 2014, 5.
    • (2014) Nucleus , vol.5
    • Beck, M.1    Glavy, J.S.2
  • 23
    • 78649650714 scopus 로고    scopus 로고
    • Recognition of nuclear targeting signals by Karyopherin-beta proteins
    • Xu D., Farmer A., Chook Y.M. 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    Farmer, A.2    Chook, Y.M.3
  • 24
    • 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
  • 25
    • 34247135913 scopus 로고    scopus 로고
    • Classical nuclear localization signals: definition, function, and interaction with importin alpha
    • Lange A., Mills R.E., Lange C.J., Stewart M., Devine S.E., Corbett A.H. Classical nuclear localization signals: definition, function, and interaction with importin alpha. J. Biol. Chem. 2007, 282:5101-5105.
    • (2007) J. Biol. Chem. , vol.282 , pp. 5101-5105
    • Lange, A.1    Mills, R.E.2    Lange, C.J.3    Stewart, M.4    Devine, S.E.5    Corbett, A.H.6
  • 26
    • 14744301997 scopus 로고    scopus 로고
    • Leucine-rich nuclear-export signals: born to be weak
    • Kutay U., Guttinger S. Leucine-rich nuclear-export signals: born to be weak. Trends Cell Biol. 2005, 15:121-124.
    • (2005) Trends Cell Biol. , vol.15 , pp. 121-124
    • Kutay, U.1    Guttinger, S.2
  • 27
    • 20444468112 scopus 로고    scopus 로고
    • Structural basis for nuclear import complex dissociation by RanGTP
    • Lee S.J., Matsuura Y., Liu S.M., Stewart M. Structural basis for nuclear import complex dissociation by RanGTP. Nature 2005, 435:693-696.
    • (2005) Nature , vol.435 , pp. 693-696
    • Lee, S.J.1    Matsuura, Y.2    Liu, S.M.3    Stewart, M.4
  • 28
    • 0030748907 scopus 로고    scopus 로고
    • Evidence for a role of CRM1 in signal-mediated nuclear protein export
    • Ossareh-Nazari B., Bachelerie F., Dargemont C. Evidence for a role of CRM1 in signal-mediated nuclear protein export. Science 1997, 278:141-144.
    • (1997) Science , vol.278 , pp. 141-144
    • Ossareh-Nazari, B.1    Bachelerie, F.2    Dargemont, C.3
  • 29
    • 0030985459 scopus 로고    scopus 로고
    • Exportin 1 (Crm1p) is an essential nuclear export factor
    • Stade K., Ford C.S., Guthrie C., Weis K. Exportin 1 (Crm1p) is an essential nuclear export factor. Cell 1997, 90:1041-1050.
    • (1997) Cell , vol.90 , pp. 1041-1050
    • Stade, K.1    Ford, C.S.2    Guthrie, C.3    Weis, K.4
  • 30
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod M., Ohno M., Yoshida M., Mattaj I.W. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 1997, 90:1051-1060.
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 31
    • 0038699131 scopus 로고    scopus 로고
    • The small GTPase Ran: interpreting the signs
    • Quimby B.B., Dasso M. The small GTPase Ran: interpreting the signs. Curr. Opin. Cell Biol. 2003, 15:338-344.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 338-344
    • Quimby, B.B.1    Dasso, M.2
  • 33
    • 33746776838 scopus 로고    scopus 로고
    • Rules for nuclear localization sequence recognition by karyopherin beta 2
    • Lee B.J., Cansizoglu A.E., Suel K.E., Louis T.H., Zhang Z., Chook Y.M. Rules for nuclear localization sequence recognition by karyopherin beta 2. Cell 2006, 126:543-558.
    • (2006) Cell , vol.126 , pp. 543-558
    • Lee, B.J.1    Cansizoglu, A.E.2    Suel, K.E.3    Louis, T.H.4    Zhang, Z.5    Chook, Y.M.6
  • 34
    • 45849096845 scopus 로고    scopus 로고
    • Modular organization and combinatorial energetics of proline-tyrosine nuclear localization signals
    • Suel K.E., Gu H., Chook Y.M. Modular organization and combinatorial energetics of proline-tyrosine nuclear localization signals. PLoS Biol. 2008, 6:e137.
    • (2008) PLoS Biol. , vol.6
    • Suel, K.E.1    Gu, H.2    Chook, Y.M.3
  • 35
    • 69849093363 scopus 로고    scopus 로고
    • Characterisation of the passive permeability barrier of nuclear pore complexes
    • Mohr D., Frey S., Fischer T., Guttler T., Gorlich D. Characterisation of the passive permeability barrier of nuclear pore complexes. EMBO J. 2009, 28:2541-2553.
    • (2009) EMBO J. , vol.28 , pp. 2541-2553
    • Mohr, D.1    Frey, S.2    Fischer, T.3    Guttler, T.4    Gorlich, D.5
  • 36
    • 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
  • 37
    • 33947727395 scopus 로고    scopus 로고
    • Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex
    • Patel S.S., Belmont B.J., Sante J.M., Rexach M.F. Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex. Cell 2007, 129:83-96.
    • (2007) Cell , vol.129 , pp. 83-96
    • Patel, S.S.1    Belmont, B.J.2    Sante, J.M.3    Rexach, M.F.4
  • 38
    • 0037418190 scopus 로고    scopus 로고
    • Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded
    • Denning D.P., Patel S.S., Uversky V., Fink A.L., Rexach M. Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:2450-2455.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 2450-2455
    • Denning, D.P.1    Patel, S.S.2    Uversky, V.3    Fink, A.L.4    Rexach, M.5
  • 39
    • 33750701489 scopus 로고    scopus 로고
    • FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties
    • Frey S., Richter R.P., Gorlich D. FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties. Science 2006, 314:815-817.
    • (2006) Science , vol.314 , pp. 815-817
    • Frey, S.1    Richter, R.P.2    Gorlich, D.3
  • 40
    • 84890571104 scopus 로고    scopus 로고
    • Large cargo transport by nuclear pores: implications for the spatial organization of FG-nucleoporins
    • Tu L.C., Fu G., Zilman A., Musser S.M. Large cargo transport by nuclear pores: implications for the spatial organization of FG-nucleoporins. EMBO J. 2013, 32:3220-3230.
    • (2013) EMBO J. , vol.32 , pp. 3220-3230
    • Tu, L.C.1    Fu, G.2    Zilman, A.3    Musser, S.M.4
  • 41
    • 84861127061 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: a role for nonspecific competition in karyopherin-nucleoporin interactions
    • Tetenbaum-Novatt J., Hough L.E., Mironska R., McKenney A.S., Rout M.P. Nucleocytoplasmic transport: a role for nonspecific competition in karyopherin-nucleoporin interactions. Mol. Cell. Proteomics 2012, 11:31-46.
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 31-46
    • Tetenbaum-Novatt, J.1    Hough, L.E.2    Mironska, R.3    McKenney, A.S.4    Rout, M.P.5
  • 42
    • 84865260520 scopus 로고    scopus 로고
    • The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model
    • Hulsmann B.B., Labokha A.A., Gorlich D. The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model. Cell 2012, 150:738-751.
    • (2012) Cell , vol.150 , pp. 738-751
    • Hulsmann, B.B.1    Labokha, A.A.2    Gorlich, D.3
  • 43
    • 79959840108 scopus 로고    scopus 로고
    • Brownian dynamics simulation of nucleocytoplasmic transport: a coarse-grained model for the functional state of the nuclear pore complex
    • Moussavi-Baygi R., Jamali Y., Karimi R., Mofrad M.R. Brownian dynamics simulation of nucleocytoplasmic transport: a coarse-grained model for the functional state of the nuclear pore complex. PLoS Comput. Biol. 2011, 7:e1002049.
    • (2011) PLoS Comput. Biol. , vol.7
    • Moussavi-Baygi, R.1    Jamali, Y.2    Karimi, R.3    Mofrad, M.R.4
  • 44
    • 34547595082 scopus 로고    scopus 로고
    • The nuclear pore complex: oily spaghetti or gummy bear?
    • Weis K. The nuclear pore complex: oily spaghetti or gummy bear?. Cell 2007, 130:405-407.
    • (2007) Cell , vol.130 , pp. 405-407
    • Weis, K.1
  • 45
    • 0035869022 scopus 로고    scopus 로고
    • Kinetic analysis of translocation through nuclear pore complexes
    • Ribbeck K., Gorlich D. Kinetic analysis of translocation through nuclear pore complexes. EMBO J. 2001, 20:1320-1330.
    • (2001) EMBO J. , vol.20 , pp. 1320-1330
    • Ribbeck, K.1    Gorlich, D.2
  • 46
    • 0037013954 scopus 로고    scopus 로고
    • The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion
    • Ribbeck K., Gorlich D. The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion. EMBO J. 2002, 21:2664-2671.
    • (2002) EMBO J. , vol.21 , pp. 2664-2671
    • Ribbeck, K.1    Gorlich, D.2
  • 48
    • 84867627425 scopus 로고    scopus 로고
    • Nuclear transport receptor binding avidity triggers a self-healing collapse transition in FG-nucleoporin molecular brushes
    • Schoch R.L., Kapinos L.E., Lim R.Y. Nuclear transport receptor binding avidity triggers a self-healing collapse transition in FG-nucleoporin molecular brushes. Proc. Natl. Acad. Sci. U. S. A. 2012, 109:16911-16916.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 16911-16916
    • Schoch, R.L.1    Kapinos, L.E.2    Lim, R.Y.3
  • 49
    • 84898866295 scopus 로고    scopus 로고
    • Karyopherin-centric control of nuclear pores based on molecular occupancy and kinetic analysis of multivalent binding with FG nucleoporins
    • Kapinos L.E., Schoch R.L., Wagner R.S., Schleicher K.D., Lim R.Y. Karyopherin-centric control of nuclear pores based on molecular occupancy and kinetic analysis of multivalent binding with FG nucleoporins. Biophys. J. 2014, 106:1751-1762.
    • (2014) Biophys. J. , vol.106 , pp. 1751-1762
    • Kapinos, L.E.1    Schoch, R.L.2    Wagner, R.S.3    Schleicher, K.D.4    Lim, R.Y.5
  • 51
    • 78049296915 scopus 로고    scopus 로고
    • Nuclear export of mRNA
    • Stewart M. Nuclear export of mRNA. Trends Biochem. Sci. 2010, 35:609-617.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 609-617
    • Stewart, M.1
  • 52
    • 84895555644 scopus 로고    scopus 로고
    • Continuous throughput and long-term observation of single-molecule FRET without immobilization
    • Tyagi S., Vandelinder V., Banterle N., Fuertes G., Milles S., Agez M., Lemke E.A. Continuous throughput and long-term observation of single-molecule FRET without immobilization. Nat. Methods 2014, 11:297-300.
    • (2014) Nat. Methods , vol.11 , pp. 297-300
    • Tyagi, S.1    Vandelinder, V.2    Banterle, N.3    Fuertes, G.4    Milles, S.5    Agez, M.6    Lemke, E.A.7
  • 53
    • 0031454975 scopus 로고    scopus 로고
    • The location of the transport gate in the nuclear pore complex
    • Feldherr C.M., Akin D. The location of the transport gate in the nuclear pore complex. J. Cell Sci. 1997, 110(Pt 24):3065-3070.
    • (1997) J. Cell Sci. , vol.110 , Issue.PT 24 , pp. 3065-3070
    • Feldherr, C.M.1    Akin, D.2
  • 54
    • 79959929587 scopus 로고    scopus 로고
    • Tetrahymena thermophila, a unicellular eukaryote with separate germline and somatic genomes
    • Orias E., Cervantes M.D., Hamilton E.P. Tetrahymena thermophila, a unicellular eukaryote with separate germline and somatic genomes. Res. Microbiol. 2011, 162:578-586.
    • (2011) Res. Microbiol. , vol.162 , pp. 578-586
    • Orias, E.1    Cervantes, M.D.2    Hamilton, E.P.3
  • 55
    • 66249136180 scopus 로고    scopus 로고
    • Two distinct repeat sequences of Nup98 nucleoporins characterize dual nuclei in the binucleated ciliate Tetrahymena
    • Iwamoto M., Mori C., Kojidani T., Bunai F., Hori T., Fukagawa T., Hiraoka Y., Haraguchi T. Two distinct repeat sequences of Nup98 nucleoporins characterize dual nuclei in the binucleated ciliate Tetrahymena. Curr. Biol. 2009, 19:843-847.
    • (2009) Curr. Biol. , vol.19 , pp. 843-847
    • Iwamoto, M.1    Mori, C.2    Kojidani, T.3    Bunai, F.4    Hori, T.5    Fukagawa, T.6    Hiraoka, Y.7    Haraguchi, T.8
  • 56
    • 77954161165 scopus 로고    scopus 로고
    • Nucleoporin Nup98: a gatekeeper in the eukaryotic kingdoms
    • Iwamoto M., Asakawa H., Hiraoka Y., Haraguchi T. Nucleoporin Nup98: a gatekeeper in the eukaryotic kingdoms. Genes Cells 2010, 15:661-669.
    • (2010) Genes Cells , vol.15 , pp. 661-669
    • Iwamoto, M.1    Asakawa, H.2    Hiraoka, Y.3    Haraguchi, T.4
  • 57
    • 84874677693 scopus 로고    scopus 로고
    • Assessing the function of the plant nuclear pore complex and the search for specificity
    • Parry G. Assessing the function of the plant nuclear pore complex and the search for specificity. J. Exp. Bot. 2013, 64:833-845.
    • (2013) J. Exp. Bot. , vol.64 , pp. 833-845
    • Parry, G.1
  • 59
    • 84905234491 scopus 로고    scopus 로고
    • The alpha-importome of mammalian germ cell maturation provides novel insights for importin biology
    • Arjomand A., Baker M.A., Li C., Buckle A.M., Jans D.A., Loveland K.L., Miyamoto Y. The alpha-importome of mammalian germ cell maturation provides novel insights for importin biology. FASEB J. 2014, 28(8):3480-3493.
    • (2014) FASEB J. , vol.28 , Issue.8 , pp. 3480-3493
    • Arjomand, A.1    Baker, M.A.2    Li, C.3    Buckle, A.M.4    Jans, D.A.5    Loveland, K.L.6    Miyamoto, Y.7
  • 60
    • 0026309494 scopus 로고
    • In vitro nuclear protein import using permeabilized mammalian cells
    • Adam S.A., Sterne-Marr R., Gerace L. In vitro nuclear protein import using permeabilized mammalian cells. Methods Cell Biol. 1991, 35:469-482.
    • (1991) Methods Cell Biol. , vol.35 , pp. 469-482
    • Adam, S.A.1    Sterne-Marr, R.2    Gerace, L.3
  • 61
    • 79953323939 scopus 로고    scopus 로고
    • Traversing the NPC along the pore membrane: targeting of membrane proteins to the INM
    • Antonin W., Ungricht R., Kutay U. 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    Ungricht, R.2    Kutay, U.3
  • 63
    • 33748310680 scopus 로고    scopus 로고
    • Karyopherin-mediated import of integral inner nuclear membrane proteins
    • King M.C., Lusk C.P., Blobel G. 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    Lusk, C.P.2    Blobel, G.3
  • 65
    • 79960234802 scopus 로고    scopus 로고
    • TAN lines: a novel nuclear envelope structure involved in nuclear positioning
    • Luxton G.W., Gomes E.R., Folker E.S., Worman H.J., Gundersen G.G. TAN lines: a novel nuclear envelope structure involved in nuclear positioning. Nucleus 2011, 2:173-181.
    • (2011) Nucleus , vol.2 , pp. 173-181
    • Luxton, G.W.1    Gomes, E.R.2    Folker, E.S.3    Worman, H.J.4    Gundersen, G.G.5
  • 66
    • 0013925189 scopus 로고
    • On the occurrence of a fibrous lamina on the inner aspect of the nuclear envelope in certain cells of vertebrates
    • Fawcett D.W. On the occurrence of a fibrous lamina on the inner aspect of the nuclear envelope in certain cells of vertebrates. Am. J. Anat. 1966, 119:129-145.
    • (1966) Am. J. Anat. , vol.119 , pp. 129-145
    • Fawcett, D.W.1
  • 67
    • 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
  • 68
    • 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.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 5718-5728
    • Huber, M.D.1    Guan, T.2    Gerace, L.3
  • 70
    • 67349217986 scopus 로고    scopus 로고
    • Molecular mechanisms of mTOR-mediated translational control
    • Ma X.M., Blenis J. Molecular mechanisms of mTOR-mediated translational control. Nat. Rev. Mol. Cell Biol. 2009, 10:307-318.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 307-318
    • Ma, X.M.1    Blenis, J.2
  • 71
    • 84861543038 scopus 로고    scopus 로고
    • LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins
    • Sosa B.A., Rothballer A., Kutay U., Schwartz T.U. LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins. Cell 2012, 149:1035-1047.
    • (2012) Cell , vol.149 , pp. 1035-1047
    • Sosa, B.A.1    Rothballer, A.2    Kutay, U.3    Schwartz, T.U.4
  • 72
    • 84873539589 scopus 로고    scopus 로고
    • LINCing complex functions at the nuclear envelope: what the molecular architecture of the LINC complex can reveal about its function
    • Rothballer A., Schwartz T.U., Kutay U. LINCing complex functions at the nuclear envelope: what the molecular architecture of the LINC complex can reveal about its function. Nucleus 2013, 4:29-36.
    • (2013) Nucleus , vol.4 , pp. 29-36
    • Rothballer, A.1    Schwartz, T.U.2    Kutay, U.3
  • 73
    • 84892662840 scopus 로고    scopus 로고
    • How plants LINC the SUN to KASH
    • Zhou X., Meier I. How plants LINC the SUN to KASH. Nucleus 2013, 4:206-215.
    • (2013) Nucleus , vol.4 , pp. 206-215
    • Zhou, X.1    Meier, I.2
  • 74
    • 84863027078 scopus 로고    scopus 로고
    • Novel plant SUN-KASH bridges are involved in RanGAP anchoring and nuclear shape determination
    • Zhou X., Graumann K., Evans D.E., Meier I. Novel plant SUN-KASH bridges are involved in RanGAP anchoring and nuclear shape determination. J. Cell Biol. 2012, 196:203-211.
    • (2012) J. Cell Biol. , vol.196 , pp. 203-211
    • Zhou, X.1    Graumann, K.2    Evans, D.E.3    Meier, I.4
  • 75
    • 84905976925 scopus 로고    scopus 로고
    • Efficient plant male fertility depends on vegetative nuclear movement mediated by two families of plant outer nuclear membrane proteins
    • (published ahead of print July 29, 2014)
    • Zhao Y., Meier I. Efficient plant male fertility depends on vegetative nuclear movement mediated by two families of plant outer nuclear membrane proteins. Proc. Natl. Acad. Sci. U. S. A. 2014, (published ahead of print July 29, 2014). 10.1073/pnas.1323104111.
    • (2014) Proc. Natl. Acad. Sci. U. S. A.
    • Zhao, Y.1    Meier, I.2
  • 76
    • 84897511498 scopus 로고    scopus 로고
    • The missing LINC: a mammalian KASH-domain protein coupling meiotic chromosomes to the cytoskeleton
    • Stewart C.L., Burke B. The missing LINC: a mammalian KASH-domain protein coupling meiotic chromosomes to the cytoskeleton. Nucleus 2014, 5:3-10.
    • (2014) Nucleus , vol.5 , pp. 3-10
    • Stewart, C.L.1    Burke, B.2
  • 77
    • 42149178405 scopus 로고    scopus 로고
    • Splicing promotes rapid and efficient mRNA export in mammalian cells
    • Valencia P., Dias A.P., Reed R. Splicing promotes rapid and efficient mRNA export in mammalian cells. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:3386-3391.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 3386-3391
    • Valencia, P.1    Dias, A.P.2    Reed, R.3
  • 78
    • 33845626622 scopus 로고    scopus 로고
    • Human mRNA export machinery recruited to the 5' end of mRNA
    • Cheng H., Dufu K., Lee C.S., Hsu J.L., Dias A., Reed R. Human mRNA export machinery recruited to the 5' end of mRNA. Cell 2006, 127:1389-1400.
    • (2006) Cell , vol.127 , pp. 1389-1400
    • Cheng, H.1    Dufu, K.2    Lee, C.S.3    Hsu, J.L.4    Dias, A.5    Reed, R.6
  • 79
    • 84876359822 scopus 로고    scopus 로고
    • Evidence that a consensus element found in naturally intronless mRNAs promotes mRNA export
    • Lei H., Zhai B., Yin S., Gygi S., Reed R. Evidence that a consensus element found in naturally intronless mRNAs promotes mRNA export. Nucleic Acids Res. 2013, 41:2517-2525.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 2517-2525
    • Lei, H.1    Zhai, B.2    Yin, S.3    Gygi, S.4    Reed, R.5
  • 80
    • 60149110358 scopus 로고    scopus 로고
    • Pre-mRNA processing reaches back to transcription and ahead to translation
    • Moore M.J., Proudfoot N.J. Pre-mRNA processing reaches back to transcription and ahead to translation. Cell 2009, 136:688-700.
    • (2009) Cell , vol.136 , pp. 688-700
    • Moore, M.J.1    Proudfoot, N.J.2
  • 82
    • 70349306459 scopus 로고    scopus 로고
    • Assembly of an export-competent mRNP is needed for efficient release of the 3'-end processing complex after polyadenylation
    • Qu X., Lykke-Andersen S., Nasser T., Saguez C., Bertrand E., Jensen T.H., Moore C. Assembly of an export-competent mRNP is needed for efficient release of the 3'-end processing complex after polyadenylation. Mol. Cell. Biol. 2009, 29:5327-5338.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 5327-5338
    • Qu, X.1    Lykke-Andersen, S.2    Nasser, T.3    Saguez, C.4    Bertrand, E.5    Jensen, T.H.6    Moore, C.7
  • 84
    • 0141469976 scopus 로고    scopus 로고
    • Yra1p, a conserved nuclear RNA-binding protein, interacts directly with Mex67p and is required for mRNA export
    • Strasser K., Hurt E. Yra1p, a conserved nuclear RNA-binding protein, interacts directly with Mex67p and is required for mRNA export. EMBO J. 2000, 19:410-420.
    • (2000) EMBO J. , vol.19 , pp. 410-420
    • Strasser, K.1    Hurt, E.2
  • 85
    • 0034699472 scopus 로고    scopus 로고
    • The protein Aly links pre-messenger-RNA splicing to nuclear export in metazoans
    • Zhou Z., Luo M.J., Straesser K., Katahira J., Hurt E., Reed R. The protein Aly links pre-messenger-RNA splicing to nuclear export in metazoans. Nature 2000, 407:401-405.
    • (2000) Nature , vol.407 , pp. 401-405
    • Zhou, Z.1    Luo, M.J.2    Straesser, K.3    Katahira, J.4    Hurt, E.5    Reed, R.6
  • 86
    • 0029994329 scopus 로고    scopus 로고
    • A protein that shuttles between the nucleus and the cytoplasm is an important mediator of RNA export
    • Lee M.S., Henry M., Silver P.A. A protein that shuttles between the nucleus and the cytoplasm is an important mediator of RNA export. Genes Dev. 1996, 10:1233-1246.
    • (1996) Genes Dev. , vol.10 , pp. 1233-1246
    • Lee, M.S.1    Henry, M.2    Silver, P.A.3
  • 87
    • 27944474017 scopus 로고    scopus 로고
    • The DEAD-box protein Dbp5p is required to dissociate Mex67p from exported mRNPs at the nuclear rim
    • Lund M.K., Guthrie C. The DEAD-box protein Dbp5p is required to dissociate Mex67p from exported mRNPs at the nuclear rim. Mol. Cell 2005, 20:645-651.
    • (2005) Mol. Cell , vol.20 , pp. 645-651
    • Lund, M.K.1    Guthrie, C.2
  • 89
    • 36749016233 scopus 로고    scopus 로고
    • The DEAD-box protein Dbp5 controls mRNA export by triggering specific RNA:protein remodeling events
    • Tran E.J., Zhou Y., Corbett A.H., Wente S.R. The DEAD-box protein Dbp5 controls mRNA export by triggering specific RNA:protein remodeling events. Mol. Cell 2007, 28:850-859.
    • (2007) Mol. Cell , vol.28 , pp. 850-859
    • Tran, E.J.1    Zhou, Y.2    Corbett, A.H.3    Wente, S.R.4
  • 91
    • 84856218082 scopus 로고    scopus 로고
    • Nuclear quality control of RNA polymerase II transcripts
    • Schmid M., Jensen T.H. Nuclear quality control of RNA polymerase II transcripts. Wiley Interdiscip. Rev. RNA 2010, 1:474-485.
    • (2010) Wiley Interdiscip. Rev. RNA , vol.1 , pp. 474-485
    • Schmid, M.1    Jensen, T.H.2
  • 92
    • 22444435897 scopus 로고    scopus 로고
    • Process or perish: quality control in mRNA biogenesis
    • Fasken M.B., Corbett A.H. Process or perish: quality control in mRNA biogenesis. Nat. Struct. Mol. Biol. 2005, 12:482-488.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 482-488
    • Fasken, M.B.1    Corbett, A.H.2
  • 93
    • 0034698683 scopus 로고    scopus 로고
    • Binding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG, and FG repeat nucleoporins is essential for nuclear mRNA export
    • Strasser K., Bassler J., Hurt E. Binding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG, and FG repeat nucleoporins is essential for nuclear mRNA export. J. Cell Biol. 2000, 150:695-706.
    • (2000) J. Cell Biol. , vol.150 , pp. 695-706
    • Strasser, K.1    Bassler, J.2    Hurt, E.3
  • 94
    • 84864387173 scopus 로고    scopus 로고
    • The DEAD-box RNA helicase Dbp2 connects RNA quality control with repression of aberrant transcription
    • Cloutier S.C., Ma W.K., Nguyen L.T., Tran E.J. The DEAD-box RNA helicase Dbp2 connects RNA quality control with repression of aberrant transcription. J. Biol. Chem. 2012, 287:26155-26166.
    • (2012) J. Biol. Chem. , vol.287 , pp. 26155-26166
    • Cloutier, S.C.1    Ma, W.K.2    Nguyen, L.T.3    Tran, E.J.4
  • 95
    • 84885172341 scopus 로고    scopus 로고
    • The DEAD-box protein Dbp2 functions with the RNA-binding protein Yra1 to promote mRNP assembly
    • Ma W.K., Cloutier S.C., Tran E.J. The DEAD-box protein Dbp2 functions with the RNA-binding protein Yra1 to promote mRNP assembly. J. Mol. Biol. 2013, 425:3824-3838.
    • (2013) J. Mol. Biol. , vol.425 , pp. 3824-3838
    • Ma, W.K.1    Cloutier, S.C.2    Tran, E.J.3
  • 96
    • 84856117990 scopus 로고    scopus 로고
    • Ubiquitylation of the nuclear pore complex controls nuclear migration during mitosis in S. cerevisiae
    • Hayakawa A., Babour A., Sengmanivong L., Dargemont C. Ubiquitylation of the nuclear pore complex controls nuclear migration during mitosis in S. cerevisiae. J. Cell Biol. 2012, 196:19-27.
    • (2012) J. Cell Biol. , vol.196 , pp. 19-27
    • Hayakawa, A.1    Babour, A.2    Sengmanivong, L.3    Dargemont, C.4
  • 97
    • 84889039636 scopus 로고    scopus 로고
    • Mapping ubiquitin modifications reveals new functions for the yeast nuclear pore complex
    • Nino C.A., Hayakawa A., Dargemont C., Babour A. Mapping ubiquitin modifications reveals new functions for the yeast nuclear pore complex. Cell Logist. 2012, 2:43-45.
    • (2012) Cell Logist. , vol.2 , pp. 43-45
    • Nino, C.A.1    Hayakawa, A.2    Dargemont, C.3    Babour, A.4
  • 98
    • 84885870186 scopus 로고    scopus 로고
    • Multiple crosstalks between mRNA biogenesis and SUMO
    • Rouviere J.O., Geoffroy M.C., Palancade B. Multiple crosstalks between mRNA biogenesis and SUMO. Chromosoma 2013, 122:387-399.
    • (2013) Chromosoma , vol.122 , pp. 387-399
    • Rouviere, J.O.1    Geoffroy, M.C.2    Palancade, B.3
  • 99
    • 79960959180 scopus 로고    scopus 로고
    • RNA mimics of green fluorescent protein
    • Paige J.S., Wu K.Y., Jaffrey S.R. RNA mimics of green fluorescent protein. Science 2011, 333:642-646.
    • (2011) Science , vol.333 , pp. 642-646
    • Paige, J.S.1    Wu, K.Y.2    Jaffrey, S.R.3
  • 100
    • 0033580444 scopus 로고    scopus 로고
    • A new protease required for cell-cycle progression in yeast
    • Li S.J., Hochstrasser M. A new protease required for cell-cycle progression in yeast. Nature 1999, 398:246-251.
    • (1999) Nature , vol.398 , pp. 246-251
    • Li, S.J.1    Hochstrasser, M.2
  • 102
    • 79960631283 scopus 로고    scopus 로고
    • Nuclear export dynamics of RNA-protein complexes
    • Grunwald D., Singer R.H., Rout M. Nuclear export dynamics of RNA-protein complexes. Nature 2011, 475:333-341.
    • (2011) Nature , vol.475 , pp. 333-341
    • Grunwald, D.1    Singer, R.H.2    Rout, M.3
  • 103
    • 77953107225 scopus 로고    scopus 로고
    • Dynamics of single mRNP nucleocytoplasmic transport and export through the nuclear pore in living cells
    • Mor A., Suliman S., Ben-Yishay R., Yunger S., Brody Y., Shav-Tal Y. Dynamics of single mRNP nucleocytoplasmic transport and export through the nuclear pore in living cells. Nat. Cell Biol. 2010, 12:543-552.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 543-552
    • Mor, A.1    Suliman, S.2    Ben-Yishay, R.3    Yunger, S.4    Brody, Y.5    Shav-Tal, Y.6
  • 104
    • 0032080030 scopus 로고    scopus 로고
    • Dbp5p/Rat8p is a yeast nuclear pore-associated DEAD-box protein essential for RNA export
    • Snay-Hodge C.A., Colot H.V., Goldstein A.L., Cole C.N. Dbp5p/Rat8p is a yeast nuclear pore-associated DEAD-box protein essential for RNA export. EMBO J. 1998, 17:2663-2676.
    • (1998) EMBO J. , vol.17 , pp. 2663-2676
    • Snay-Hodge, C.A.1    Colot, H.V.2    Goldstein, A.L.3    Cole, C.N.4
  • 105
    • 0029028762 scopus 로고
    • The essential yeast nucleoporin NUP159 is located on the cytoplasmic side of the nuclear pore complex and serves in karyopherin-mediated binding of transport substrate
    • Kraemer D.M., Strambio-de-Castillia C., Blobel G., Rout M.P. The essential yeast nucleoporin NUP159 is located on the cytoplasmic side of the nuclear pore complex and serves in karyopherin-mediated binding of transport substrate. J. Biol. Chem. 1995, 270:19017-19021.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19017-19021
    • Kraemer, D.M.1    Strambio-de-Castillia, C.2    Blobel, G.3    Rout, M.P.4
  • 106
    • 0030911425 scopus 로고    scopus 로고
    • Mex67p, a novel factor for nuclear mRNA export, binds to both poly(A)+RNA and nuclear pores
    • Segref A., Sharma K., Doye V., Hellwig A., Huber J., Luhrmann R., Hurt E. Mex67p, a novel factor for nuclear mRNA export, binds to both poly(A)+RNA and nuclear pores. EMBO J. 1997, 16:3256-3271.
    • (1997) EMBO J. , vol.16 , pp. 3256-3271
    • Segref, A.1    Sharma, K.2    Doye, V.3    Hellwig, A.4    Huber, J.5    Luhrmann, R.6    Hurt, E.7
  • 109
    • 84901330247 scopus 로고    scopus 로고
    • From hypothesis to mechanism: uncovering nuclear pore complex links to gene expression
    • Wente S.R., Burns L. From hypothesis to mechanism: uncovering nuclear pore complex links to gene expression. Mol. Biol. Cell 2014, 34(12):2114-2120.
    • (2014) Mol. Biol. Cell , vol.34 , Issue.12 , pp. 2114-2120
    • Wente, S.R.1    Burns, L.2
  • 110
    • 84884550965 scopus 로고    scopus 로고
    • The nuclear pore regulates GAL1 gene transcription by controlling the localization of the SUMO protease Ulp1
    • Texari L., Dieppois G., Vinciguerra P., Contreras M.P., Groner A., Letourneau A., Stutz F. The nuclear pore regulates GAL1 gene transcription by controlling the localization of the SUMO protease Ulp1. Mol. Cell 2013, 51:807-818.
    • (2013) Mol. Cell , vol.51 , pp. 807-818
    • Texari, L.1    Dieppois, G.2    Vinciguerra, P.3    Contreras, M.P.4    Groner, A.5    Letourneau, A.6    Stutz, F.7
  • 111
    • 84887433563 scopus 로고    scopus 로고
    • Nuclear pore proteins regulate chromatin structure and transcriptional memory by a conserved mechanism
    • Light W.H., Brickner J.H. Nuclear pore proteins regulate chromatin structure and transcriptional memory by a conserved mechanism. Nucleus 2013, 4:357-360.
    • (2013) Nucleus , vol.4 , pp. 357-360
    • Light, W.H.1    Brickner, J.H.2
  • 112
    • 14044266853 scopus 로고    scopus 로고
    • Gene recruitment of the activated INO1 locus to the nuclear membrane
    • Brickner J.H., Walter P. Gene recruitment of the activated INO1 locus to the nuclear membrane. PLoS Biol. 2004, 2:e342.
    • (2004) PLoS Biol. , vol.2
    • Brickner, J.H.1    Walter, P.2
  • 114
    • 84875478639 scopus 로고    scopus 로고
    • A conserved role for human Nup98 in altering chromatin structure and promoting epigenetic transcriptional memory
    • Light W.H., Freaney J., Sood V., Thompson A., D'Urso A., Horvath C.M., Brickner J.H. A conserved role for human Nup98 in altering chromatin structure and promoting epigenetic transcriptional memory. PLoS Biol. 2013, 11:e1001524.
    • (2013) PLoS Biol. , vol.11
    • Light, W.H.1    Freaney, J.2    Sood, V.3    Thompson, A.4    D'Urso, A.5    Horvath, C.M.6    Brickner, J.H.7
  • 115
    • 77957377062 scopus 로고    scopus 로고
    • Interaction of a DNA zip code with the nuclear pore complex promotes H2A.Z incorporation and INO1 transcriptional memory
    • Light W.H., Brickner D.G., Brand V.R., Brickner J.H. Interaction of a DNA zip code with the nuclear pore complex promotes H2A.Z incorporation and INO1 transcriptional memory. Mol. Cell 2010, 40:112-125.
    • (2010) Mol. Cell , vol.40 , pp. 112-125
    • Light, W.H.1    Brickner, D.G.2    Brand, V.R.3    Brickner, J.H.4
  • 116
    • 84888132934 scopus 로고    scopus 로고
    • SET for life: biochemical activities and biological functions of SET domain-containing proteins
    • Herz H.M., Garruss A., Shilatifard A. SET for life: biochemical activities and biological functions of SET domain-containing proteins. Trends Biochem. Sci. 2013, 38:621-639.
    • (2013) Trends Biochem. Sci. , vol.38 , pp. 621-639
    • Herz, H.M.1    Garruss, A.2    Shilatifard, A.3
  • 117
    • 84901446291 scopus 로고    scopus 로고
    • Mechanisms of epigenetic memory
    • D'Urso A., Brickner J.H. Mechanisms of epigenetic memory. Trends Genet. 2014, 30(6):230-236.
    • (2014) Trends Genet. , vol.30 , Issue.6 , pp. 230-236
    • D'Urso, A.1    Brickner, J.H.2
  • 120
    • 84904459489 scopus 로고    scopus 로고
    • Clinical translation of nuclear export inhibitors in cancer
    • Senapedis W.T., Baloglu E., Landesman Y. Clinical translation of nuclear export inhibitors in cancer. Semin. Cancer Biol. 2014, 27C:74-86.
    • (2014) Semin. Cancer Biol. , vol.27 C , pp. 74-86
    • Senapedis, W.T.1    Baloglu, E.2    Landesman, Y.3
  • 122
    • 84907598197 scopus 로고    scopus 로고
    • KPT-330 inhibitor of XPO1-mediated nuclear export has anti-proliferative activity in hepatocellular carcinoma
    • [Epub ahead of print]
    • Zheng Y., Gery S., Sun H., Shacham S., Kauffman M., Koeffler H.P. KPT-330 inhibitor of XPO1-mediated nuclear export has anti-proliferative activity in hepatocellular carcinoma. Cancer Chemother. Pharmacol. 2014, [Epub ahead of print].
    • (2014) Cancer Chemother. Pharmacol.
    • Zheng, Y.1    Gery, S.2    Sun, H.3    Shacham, S.4    Kauffman, M.5    Koeffler, H.P.6
  • 125
    • 84886796260 scopus 로고    scopus 로고
    • Gle1 functions during mRNA export in an oligomeric complex that is altered in human disease
    • Folkmann A.W., Collier S.E., Zhan X., Aditi, Ohi M.D., Wente S.R. Gle1 functions during mRNA export in an oligomeric complex that is altered in human disease. Cell 2013, 155:582-593.
    • (2013) Cell , vol.155 , pp. 582-593
    • Folkmann, A.W.1    Collier, S.E.2    Zhan, X.3    Aditi4    Ohi, M.D.5    Wente, S.R.6
  • 126
    • 84893385652 scopus 로고    scopus 로고
    • Insights into mRNA export-linked molecular mechanisms of human disease through a Gle1 structure-function analysis
    • Folkmann A.W., Dawson T.R., Wente S.R. Insights into mRNA export-linked molecular mechanisms of human disease through a Gle1 structure-function analysis. Adv. Biol. Regul. 2014, 54:74-91.
    • (2014) Adv. Biol. Regul. , vol.54 , pp. 74-91
    • Folkmann, A.W.1    Dawson, T.R.2    Wente, S.R.3
  • 127
    • 33745742173 scopus 로고    scopus 로고
    • Activation of the DExD/H-box protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export
    • Weirich C.S., Erzberger J.P., Flick J.S., Berger J.M., Thorner J., Weis K. Activation of the DExD/H-box protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export. Nat. Cell Biol. 2006, 8:668-676.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 668-676
    • Weirich, C.S.1    Erzberger, J.P.2    Flick, J.S.3    Berger, J.M.4    Thorner, J.5    Weis, K.6
  • 128
    • 33745736445 scopus 로고    scopus 로고
    • Inositol hexakisphosphate and Gle1 activate the DEAD-box protein Dbp5 for nuclear mRNA export
    • Alcazar-Roman A.R., Tran E.J., Guo S., Wente S.R. Inositol hexakisphosphate and Gle1 activate the DEAD-box protein Dbp5 for nuclear mRNA export. Nat. Cell Biol. 2006, 8:711-716.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 711-716
    • Alcazar-Roman, A.R.1    Tran, E.J.2    Guo, S.3    Wente, S.R.4
  • 129
    • 0033569797 scopus 로고    scopus 로고
    • The RNA export factor Gle1p is located on the cytoplasmic fibrils of the NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box protein Rat8p/Dbp5p and a new protein Ymr 255p
    • Strahm Y., Fahrenkrog B., Zenklusen D., Rychner E., Kantor J., Rosbach M., Stutz F. The RNA export factor Gle1p is located on the cytoplasmic fibrils of the NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box protein Rat8p/Dbp5p and a new protein Ymr 255p. EMBO J. 1999, 18:5761-5777.
    • (1999) EMBO J. , vol.18 , pp. 5761-5777
    • Strahm, Y.1    Fahrenkrog, B.2    Zenklusen, D.3    Rychner, E.4    Kantor, J.5    Rosbach, M.6    Stutz, F.7
  • 133
    • 84857733745 scopus 로고    scopus 로고
    • SMN in spinal muscular atrophy and snRNP biogenesis
    • Coady T.H., Lorson C.L. SMN in spinal muscular atrophy and snRNP biogenesis. Wiley Interdiscip. Rev. RNA 2011, 2:546-564.
    • (2011) Wiley Interdiscip. Rev. RNA , vol.2 , pp. 546-564
    • Coady, T.H.1    Lorson, C.L.2
  • 135
    • 84860464554 scopus 로고    scopus 로고
    • The long and the short of it: the role of the zinc finger polyadenosine RNA binding protein, Nab2, in control of poly(A) tail length
    • Soucek S., Corbett A.H., Fasken M.B. The long and the short of it: the role of the zinc finger polyadenosine RNA binding protein, Nab2, in control of poly(A) tail length. Biochim. Biophys. Acta 2012, 1819:546-554.
    • (2012) Biochim. Biophys. Acta , vol.1819 , pp. 546-554
    • Soucek, S.1    Corbett, A.H.2    Fasken, M.B.3
  • 136
    • 84862237468 scopus 로고    scopus 로고
    • New kid on the ID block: neural functions of the Nab2/ZC3H14 class of Cys(3)His tandem zinc-finger polyadenosine RNA binding proteins
    • Kelly S., Pak C., Garshasbi M., Kuss A., Corbett A.H., Moberg K. New kid on the ID block: neural functions of the Nab2/ZC3H14 class of Cys(3)His tandem zinc-finger polyadenosine RNA binding proteins. RNA Biol. 2012, 9:555-562.
    • (2012) RNA Biol. , vol.9 , pp. 555-562
    • Kelly, S.1    Pak, C.2    Garshasbi, M.3    Kuss, A.4    Corbett, A.H.5    Moberg, K.6
  • 137
    • 0027322091 scopus 로고
    • NAB2: a yeast nuclear polyadenylated RNA-binding protein essential for cell viability
    • Anderson J.T., Wilson S.M., Datar K.V., Swanson M.S. NAB2: a yeast nuclear polyadenylated RNA-binding protein essential for cell viability. Mol. Cell. Biol. 1993, 13:2730-2741.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2730-2741
    • Anderson, J.T.1    Wilson, S.M.2    Datar, K.V.3    Swanson, M.S.4
  • 139
    • 84898944790 scopus 로고    scopus 로고
    • A conserved role for the zinc finger polyadenosine RNA binding protein, ZC3H14, in control of poly(a) tail length
    • Kelly S.M., Leung S.W., Pak C., Banerjee A., Moberg K.H., Corbett A.H. A conserved role for the zinc finger polyadenosine RNA binding protein, ZC3H14, in control of poly(a) tail length. RNA 2014, 20(5):681-688.
    • (2014) RNA , vol.20 , Issue.5 , pp. 681-688
    • Kelly, S.M.1    Leung, S.W.2    Pak, C.3    Banerjee, A.4    Moberg, K.H.5    Corbett, A.H.6
  • 140
    • 84863838830 scopus 로고    scopus 로고
    • Cap-dependent translation initiation factor eIF4E: an emerging anticancer drug target
    • Jia Y., Polunovsky V., Bitterman P.B., Wagner C.R. Cap-dependent translation initiation factor eIF4E: an emerging anticancer drug target. Med. Res. Rev. 2012, 32:786-814.
    • (2012) Med. Res. Rev. , vol.32 , pp. 786-814
    • Jia, Y.1    Polunovsky, V.2    Bitterman, P.B.3    Wagner, C.R.4
  • 141
    • 84877843724 scopus 로고    scopus 로고
    • The oncogene eIF4E: using biochemical insights to target cancer
    • Carroll M., Borden K.L. The oncogene eIF4E: using biochemical insights to target cancer. J. Interferon Cytokine Res. 2013, 33:227-238.
    • (2013) J. Interferon Cytokine Res. , vol.33 , pp. 227-238
    • Carroll, M.1    Borden, K.L.2
  • 142
    • 84880498999 scopus 로고    scopus 로고
    • Conformational changes induced in the eukaryotic translation initiation factor eIF4E by a clinically relevant inhibitor, ribavirin triphosphate
    • Volpon L., Osborne M.J., Zahreddine H., Romeo A.A., Borden K.L. Conformational changes induced in the eukaryotic translation initiation factor eIF4E by a clinically relevant inhibitor, ribavirin triphosphate. Biochem. Biophys. Res. Commun. 2013, 434:614-619.
    • (2013) Biochem. Biophys. Res. Commun. , vol.434 , pp. 614-619
    • Volpon, L.1    Osborne, M.J.2    Zahreddine, H.3    Romeo, A.A.4    Borden, K.L.5
  • 145
    • 0033535342 scopus 로고    scopus 로고
    • Proteins connecting the nuclear pore complex with the nuclear interior
    • Strambio-de-Castillia C., Blobel G., Rout M.P. Proteins connecting the nuclear pore complex with the nuclear interior. J. Cell Biol. 1999, 144:839-855.
    • (1999) J. Cell Biol. , vol.144 , pp. 839-855
    • Strambio-de-Castillia, C.1    Blobel, G.2    Rout, M.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.