메뉴 건너뛰기




Volumn 28, Issue 1, 2014, Pages 36-45

Traffic to the inner membrane of the nuclear envelope

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL; CELL NUCLEUS MEMBRANE; CYTOPLASM; HUMAN; KINETICS; METABOLISM; TRANSPORT AT THE CELLULAR LEVEL;

EID: 84894073194     PISSN: 09550674     EISSN: 18790410     Source Type: Journal    
DOI: 10.1016/j.ceb.2014.01.006     Document Type: Review
Times cited : (26)

References (74)
  • 3
    • 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
  • 4
    • 0035834037 scopus 로고    scopus 로고
    • Nuclear envelope proteomics: novel integral membrane proteins of the inner nuclear membrane
    • Dreger M., Bengtsson L., Schöneberg T., Otto H., Hucho F. Nuclear envelope proteomics: novel integral membrane proteins of the inner nuclear membrane. Proc Natl Acad Sci U S A 2001, 98:11943-11948.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 11943-11948
    • Dreger, M.1    Bengtsson, L.2    Schöneberg, T.3    Otto, H.4    Hucho, F.5
  • 5
    • 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 2003, 301:1380-1382.
    • (2003) Science , vol.301 , pp. 1380-1382
    • Schirmer, E.C.1    Florens, L.2    Guan, T.3    Yates, J.R.4    Gerace, L.5
  • 7
    • 79959359806 scopus 로고    scopus 로고
    • Mutations causing Greenberg dysplasia but not Pelger anomaly uncouple enzymatic from structural functions of a nuclear membrane protein
    • Clayton P., Fischer B., Mann A., Mansour S., Rossier E., Veen M., Lang C., Baasanjav S., Kieslich M., Brossuleit K., et al. Mutations causing Greenberg dysplasia but not Pelger anomaly uncouple enzymatic from structural functions of a nuclear membrane protein. Nucleus 2010, 1:354-366.
    • (2010) Nucleus , vol.1 , pp. 354-366
    • Clayton, P.1    Fischer, B.2    Mann, A.3    Mansour, S.4    Rossier, E.5    Veen, M.6    Lang, C.7    Baasanjav, S.8    Kieslich, M.9    Brossuleit, K.10
  • 8
    • 0036699522 scopus 로고    scopus 로고
    • Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger-Huët anomaly)
    • Hoffmann K., Dreger C.K., Olins A.L., Olins D.E., Shultz L.D., Lucke B., Karl H., Kaps R., Müller D., Vaya A., et al. Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger-Huët anomaly). Nat Genet 2002, 31:410-414.
    • (2002) Nat Genet , vol.31 , pp. 410-414
    • Hoffmann, K.1    Dreger, C.K.2    Olins, A.L.3    Olins, D.E.4    Shultz, L.D.5    Lucke, B.6    Karl, H.7    Kaps, R.8    Müller, D.9    Vaya, A.10
  • 9
  • 11
    • 77449109551 scopus 로고    scopus 로고
    • Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes
    • Haque F., Mazzeo D., Patel J.T., Smallwood D.T., Ellis J.A., Shanahan C.M., Shackleton S. 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    Mazzeo, D.2    Patel, J.T.3    Smallwood, D.T.4    Ellis, J.A.5    Shanahan, C.M.6    Shackleton, S.7
  • 12
    • 84894028919 scopus 로고    scopus 로고
    • A classical NLS and the SUN domain contribute to the targeting of SUN2 to the INM
    • Turgay Y., Ungricht R., Rothballer A., Kiss A., Csucs G., Horvath P., Kutay U. A classical NLS and the SUN domain contribute to the targeting of SUN2 to the INM. EMBO J 2010, 119. 10.1038/emboj.2010.
    • (2010) EMBO J , pp. 119
    • Turgay, Y.1    Ungricht, R.2    Rothballer, A.3    Kiss, A.4    Csucs, G.5    Horvath, P.6    Kutay, U.7
  • 13
    • 79955966597 scopus 로고    scopus 로고
    • Multiple mechanisms actively target the SUN protein UNC-84 to the inner nuclear membrane
    • Tapley E.C., Ly N., Starr D.A. 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    Ly, N.2    Starr, D.A.3
  • 14
    • 80054041334 scopus 로고    scopus 로고
    • Membrane protein insertion at the endoplasmic reticulum
    • Shao S., Hegde R.S. Membrane protein insertion at the endoplasmic reticulum. Annu Rev Cell Dev Biol 2011, 27:25-56.
    • (2011) Annu Rev Cell Dev Biol , vol.27 , pp. 25-56
    • Shao, S.1    Hegde, R.S.2
  • 15
    • 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
  • 17
    • 78349279170 scopus 로고    scopus 로고
    • Truncated isoforms of Kap60 facilitate trafficking of Heh2 to the nuclear envelope
    • Liu D., Wu X., Summers M.D., Lee A., Ryan K.J., Braunagel S.C. 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    Wu, X.2    Summers, M.D.3    Lee, A.4    Ryan, K.J.5    Braunagel, S.C.6
  • 18
    • 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., Shao Y., Braunagel S.C., Summers M.D., Johnson A.E. 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    Shao, Y.2    Braunagel, S.C.3    Summers, M.D.4    Johnson, A.E.5
  • 20
    • 84876124126 scopus 로고    scopus 로고
    • Quantitative analysis of membrane protein transport across the nuclear pore complex
    • Meinema A.C., Poolman B., Veenhoff L.M. 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    Poolman, B.2    Veenhoff, L.M.3
  • 21
    • 0035102443 scopus 로고    scopus 로고
    • Targeting of C-terminal (tail)-anchored proteins: understanding how cytoplasmic activities are anchored to intracellular membranes
    • Wattenberg B., Lithgow T. Targeting of C-terminal (tail)-anchored proteins: understanding how cytoplasmic activities are anchored to intracellular membranes. Traffic 2001, 2:66-71.
    • (2001) Traffic , vol.2 , pp. 66-71
    • Wattenberg, B.1    Lithgow, T.2
  • 22
    • 79957838252 scopus 로고    scopus 로고
    • Subcellular localization of SUN2 is regulated by lamin A and Rab5
    • Liang Y., Chiu P.H., Yip K.Y., Chan S.Y. Subcellular localization of SUN2 is regulated by lamin A and Rab5. PLoS ONE 2011, 6:e20507.
    • (2011) PLoS ONE , vol.6
    • Liang, Y.1    Chiu, P.H.2    Yip, K.Y.3    Chan, S.Y.4
  • 23
    • 84881140677 scopus 로고    scopus 로고
    • The nuclear envelope LEM-domain protein emerin
    • Berk J.M., Tifft K.E., Wilson K.L. The nuclear envelope LEM-domain protein emerin. Nucleus 2013, 4:298-314.
    • (2013) Nucleus , vol.4 , pp. 298-314
    • Berk, J.M.1    Tifft, K.E.2    Wilson, K.L.3
  • 24
    • 84893813759 scopus 로고    scopus 로고
    • Syntaxin 6-mediated Golgi translocation plays an important role in nuclear functions of EGFR through microtubule-dependent trafficking
    • Du Y., Shen J., Hsu J.L., Han Z., Hsu M.-C., Yang C.-C., Kuo H.-P., Wang Y.N., Yamaguchi H., Miller S.A., et al. Syntaxin 6-mediated Golgi translocation plays an important role in nuclear functions of EGFR through microtubule-dependent trafficking. Oncogene 2013, 1. 10.1038/onc.2013.
    • (2013) Oncogene , pp. 1
    • Du, Y.1    Shen, J.2    Hsu, J.L.3    Han, Z.4    Hsu, M.-C.5    Yang, C.-C.6    Kuo, H.-P.7    Wang, Y.N.8    Yamaguchi, H.9    Miller, S.A.10
  • 25
  • 26
    • 11244316478 scopus 로고    scopus 로고
    • Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore
    • Ohba T., Schirmer E.C., Nishimoto T., Gerace L. 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    Schirmer, E.C.2    Nishimoto, T.3    Gerace, L.4
  • 27
    • 33748310680 scopus 로고    scopus 로고
    • Karyopherin-mediated import of integral inner nuclear membrane proteins
    • King M.C., Patrick Lusk C., 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    Patrick Lusk, C.2    Blobel, G.3
  • 28
    • 34247364639 scopus 로고    scopus 로고
    • Highway to the inner nuclear membrane: rules for the road
    • Lusk C.P., Blobel G., King M.C. 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    Blobel, G.2    King, M.C.3
  • 29
    • 84863816293 scopus 로고    scopus 로고
    • The transport of integral membrane proteins across the nuclear pore complex
    • Meinema A.C., Poolman B., Veenhoff L.M. 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    Poolman, B.2    Veenhoff, L.M.3
  • 30
    • 84861363181 scopus 로고    scopus 로고
    • FG repeats facilitate integral protein trafficking to the inner nuclear membrane
    • Kerr A.R., Schirmer E.C. FG repeats facilitate integral protein trafficking to the inner nuclear membrane. Commun Integr Biol 2011, 4:557-559.
    • (2011) Commun Integr Biol , vol.4 , pp. 557-559
    • Kerr, A.R.1    Schirmer, E.C.2
  • 33
    • 84861995457 scopus 로고    scopus 로고
    • Trafficking to uncharted territory of the nuclear envelope
    • Burns L.T., Wente S.R. Trafficking to uncharted territory of the nuclear envelope. Curr Opin Cell Biol 2012, 24:341-349.
    • (2012) Curr Opin Cell Biol , vol.24 , pp. 341-349
    • Burns, L.T.1    Wente, S.R.2
  • 34
    • 84872478119 scopus 로고    scopus 로고
    • Virus strategies for passing the nuclear envelope barrier
    • Kobiler O., Drayman N., Butin-Israeli V., Oppenheim A. Virus strategies for passing the nuclear envelope barrier. Nucleus 2012, 3:526-539.
    • (2012) Nucleus , vol.3 , pp. 526-539
    • Kobiler, O.1    Drayman, N.2    Butin-Israeli, V.3    Oppenheim, A.4
  • 35
    • 84872616937 scopus 로고    scopus 로고
    • The way out: what we know and do not know about herpesvirus nuclear egress
    • Mettenleiter T.C., Müller F., Granzow H., Klupp B.G. 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    Müller, F.2    Granzow, H.3    Klupp, B.G.4
  • 36
    • 84860852545 scopus 로고    scopus 로고
    • Nuclear envelope budding enables large ribonucleoprotein particle export during synaptic Wnt signaling
    • Speese S.D., Ashley J., Jokhi V., Nunnari J., Barria R., Li Y., Ataman B., Koon A., Chang Y.-T., Li Q., 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    Ashley, J.2    Jokhi, V.3    Nunnari, J.4    Barria, R.5    Li, Y.6    Ataman, B.7    Koon, A.8    Chang, Y.-T.9    Li, Q.10
  • 37
    • 84866854226 scopus 로고    scopus 로고
    • Alternative nuclear transport for cellular protein quality control
    • Rose A., Schlieker C. Alternative nuclear transport for cellular protein quality control. Trends Cell Biol 2012, 22:509-514.
    • (2012) Trends Cell Biol , vol.22 , pp. 509-514
    • Rose, A.1    Schlieker, C.2
  • 39
    • 73249130542 scopus 로고    scopus 로고
    • Structural analysis of a metazoan nuclear pore complex reveals a fused concentric ring architecture
    • Frenkiel-Krispin D., Maco B., Aebi U., Medalia O. Structural analysis of a metazoan nuclear pore complex reveals a fused concentric ring architecture. J Mol Biol 2010, 395:578-586.
    • (2010) J Mol Biol , vol.395 , pp. 578-586
    • Frenkiel-Krispin, D.1    Maco, B.2    Aebi, U.3    Medalia, O.4
  • 40
    • 77957687133 scopus 로고    scopus 로고
    • Perspective on the metazoan nuclear pore complex
    • Maimon T., Medalia O. Perspective on the metazoan nuclear pore complex. Nucleus 2010, 1:383-386.
    • (2010) Nucleus , vol.1 , pp. 383-386
    • Maimon, T.1    Medalia, O.2
  • 41
    • 34948891095 scopus 로고    scopus 로고
    • Snapshots of nuclear pore complexes in action captured by cryo-electron tomography
    • Beck M., Lucić V., Förster 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    Lucić, V.2    Förster, F.3    Baumeister, W.4    Medalia, O.5
  • 43
    • 67749124115 scopus 로고    scopus 로고
    • Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo
    • Anderson D.J., Vargas J.D., Hsiao J.P., Hetzer M.W. Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo. J Cell Biol 2009, 186:183-191.
    • (2009) J Cell Biol , vol.186 , pp. 183-191
    • Anderson, D.J.1    Vargas, J.D.2    Hsiao, J.P.3    Hetzer, M.W.4
  • 44
    • 79954591421 scopus 로고    scopus 로고
    • Lumenal interactions in nuclear pore complex assembly and stability
    • Yewdell W.T., Colombi P., Makhnevych T., Lusk C.P. Lumenal interactions in nuclear pore complex assembly and stability. Mol Biol Cell 2011, 22:1375-1388.
    • (2011) Mol Biol Cell , vol.22 , pp. 1375-1388
    • Yewdell, W.T.1    Colombi, P.2    Makhnevych, T.3    Lusk, C.P.4
  • 46
    • 77953724768 scopus 로고    scopus 로고
    • Cell cycle-dependent differences in nuclear pore complex assembly in metazoa
    • Doucet C.M., Talamas J.A., Hetzer M.W. Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. Cell 2010, 141:1030-1041.
    • (2010) Cell , vol.141 , pp. 1030-1041
    • Doucet, C.M.1    Talamas, J.A.2    Hetzer, M.W.3
  • 47
    • 79960233453 scopus 로고    scopus 로고
    • POM121 and Sun1 play a role in early steps of interphase NPC assembly
    • Talamas J.A., Hetzer M.W. POM121 and Sun1 play a role in early steps of interphase NPC assembly. J Cell Biol 2011, 194:27-37.
    • (2011) J Cell Biol , vol.194 , pp. 27-37
    • Talamas, J.A.1    Hetzer, M.W.2
  • 48
    • 78049508819 scopus 로고    scopus 로고
    • Pom121 links two essential subcomplexes of the nuclear pore complex core to the membrane
    • Mitchell J.M., Mansfeld J., Capitanio J., Kutay U., Wozniak R.W. 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    Mansfeld, J.2    Capitanio, J.3    Kutay, U.4    Wozniak, R.W.5
  • 49
    • 84856767246 scopus 로고    scopus 로고
    • A dominant-negative form of POM121 binds chromatin and disrupts the two separate modes of nuclear pore assembly
    • Shaulov L., Gruber R., Cohen I., Harel A. A dominant-negative form of POM121 binds chromatin and disrupts the two separate modes of nuclear pore assembly. J Cell Sci 2011, 124:3822-3834.
    • (2011) J Cell Sci , vol.124 , pp. 3822-3834
    • Shaulov, L.1    Gruber, R.2    Cohen, I.3    Harel, A.4
  • 50
    • 34848872591 scopus 로고    scopus 로고
    • The inner nuclear envelope as a transcription factor resting place
    • Heessen S., Fornerod M. The inner nuclear envelope as a transcription factor resting place. EMBO Rep 2007, 8:914-919.
    • (2007) EMBO Rep , vol.8 , pp. 914-919
    • Heessen, S.1    Fornerod, M.2
  • 51
  • 52
    • 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
  • 55
    • 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
  • 56
    • 84866595263 scopus 로고    scopus 로고
    • A portrait of the GET pathway as a surprisingly complicated young man
    • Denic V. A portrait of the GET pathway as a surprisingly complicated young man. Trends Biochem Sci 2012, 37:411-417.
    • (2012) Trends Biochem Sci , vol.37 , pp. 411-417
    • Denic, V.1
  • 57
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: composition, architecture, and transport mechanism
    • Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J Cell Biol 2000, 148:635-651.
    • (2000) J Cell Biol , vol.148 , pp. 635-651
    • Rout, M.P.1    Aitchison, J.D.2    Suprapto, A.3    Hjertaas, K.4    Zhao, Y.5    Chait, B.T.6
  • 59
    • 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
  • 60
    • 84883182912 scopus 로고    scopus 로고
    • Genetic analysis of Mps3 SUN domain mutants in Saccharomyces cerevisiae reveals an interaction with the SUN-like protein Slp1
    • Friederichs J.M., Gardner J.M., Smoyer C.J., Whetstine C.R., Gogol M., Slaughter B.D., Jaspersen S.L. Genetic analysis of Mps3 SUN domain mutants in Saccharomyces cerevisiae reveals an interaction with the SUN-like protein Slp1. G3 (Bethesda) 2012, 2:1703-1718.
    • (2012) G3 (Bethesda) , vol.2 , pp. 1703-1718
    • Friederichs, J.M.1    Gardner, J.M.2    Smoyer, C.J.3    Whetstine, C.R.4    Gogol, M.5    Slaughter, B.D.6    Jaspersen, S.L.7
  • 62
    • 2942533937 scopus 로고    scopus 로고
    • Sun2 is a novel mammalian inner nuclear membrane protein
    • Hodzic D.M. 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
  • 64
    • 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., Fritze C.E., Gerace L. 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    Fritze, C.E.2    Gerace, L.3
  • 65
    • 33750379023 scopus 로고    scopus 로고
    • The laminopathies: the functional architecture of the nucleus and its contribution to disease
    • Burke B., Stewart C.L. The laminopathies: the functional architecture of the nucleus and its contribution to disease. Annu Rev Genom Hum Genet 2006, 7:369-405.
    • (2006) Annu Rev Genom Hum Genet , vol.7 , pp. 369-405
    • Burke, B.1    Stewart, C.L.2
  • 66
    • 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., Panté N., Aebi U., Gerace L. 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    Panté, N.2    Aebi, U.3    Gerace, L.4
  • 67
    • 30544449477 scopus 로고    scopus 로고
    • LEM2 is a novel MAN1-related inner nuclear membrane protein associated with A-type lamins
    • Brachner A., Reipert S., Foisner R., Gotzmann J. LEM2 is a novel MAN1-related inner nuclear membrane protein associated with A-type lamins. J Cell Sci 2005, 118:5797-5810.
    • (2005) J Cell Sci , vol.118 , pp. 5797-5810
    • Brachner, A.1    Reipert, S.2    Foisner, R.3    Gotzmann, J.4
  • 68
    • 0036538599 scopus 로고    scopus 로고
    • Intracellular trafficking of MAN1, an integral protein of the nuclear envelope inner membrane
    • Wu W., Lin F., Worman H.J. 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    Lin, F.2    Worman, H.J.3
  • 69
    • 0027386803 scopus 로고
    • The first membrane spanning region of the lamin B receptor is sufficient for sorting to the inner nuclear membrane
    • Smith S., Blobel G. The first membrane spanning region of the lamin B receptor is sufficient for sorting to the inner nuclear membrane. J Cell Biol 1993, 120:631-637.
    • (1993) J Cell Biol , vol.120 , pp. 631-637
    • Smith, S.1    Blobel, G.2
  • 70
    • 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
  • 71
    • 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
  • 72
    • 33847367253 scopus 로고    scopus 로고
    • Lamin B receptor plays a role in stimulating nuclear envelope production and targeting membrane vesicles to chromatin during nuclear envelope assembly through direct interaction with importin beta
    • Ma Y., Cai S., Lv Q., Jiang Q., Zhang Q., Sodmergen, Zhai Z., Zhang C. Lamin B receptor plays a role in stimulating nuclear envelope production and targeting membrane vesicles to chromatin during nuclear envelope assembly through direct interaction with importin beta. J Cell Sci 2007, 120:520-530.
    • (2007) J Cell Sci , vol.120 , pp. 520-530
    • Ma, Y.1    Cai, S.2    Lv, Q.3    Jiang, Q.4    Zhang, Q.5    Sodmergen6    Zhai, Z.7    Zhang, C.8
  • 73
    • 0033549555 scopus 로고    scopus 로고
    • A visual screen of a GFP-fusion library identifies a new type of nuclear envelope membrane protein
    • Rolls M.M., Stein P.A., Taylor S.S., Ha E., McKeon F., Rapoport T.A. A visual screen of a GFP-fusion library identifies a new type of nuclear envelope membrane protein. J Cell Biol 1999, 146:29-44.
    • (1999) J Cell Biol , vol.146 , pp. 29-44
    • Rolls, M.M.1    Stein, P.A.2    Taylor, S.S.3    Ha, E.4    McKeon, F.5    Rapoport, T.A.6
  • 74
    • 13244279655 scopus 로고    scopus 로고
    • Analysis of the localization and topology of nurim, a polytopic protein tightly associated with the inner nuclear membrane
    • Hofemeister H., O'Hare P. Analysis of the localization and topology of nurim, a polytopic protein tightly associated with the inner nuclear membrane. J Biol Chem 2004, 280:2512-2521.
    • (2004) J Biol Chem , vol.280 , pp. 2512-2521
    • Hofemeister, H.1    O'Hare, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.