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Volumn 13, Issue 6, 2006, Pages 500-508

Importin-α-16 is a translocon-associated protein involved in sorting membrane proteins to the nuclear envelope

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; KARYOPHERIN ALPHA; MEMBRANE PROTEIN; TRANSLOCON;

EID: 33744915536     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb1098     Document Type: Article
Times cited : (62)

References (37)
  • 1
    • 28444472419 scopus 로고    scopus 로고
    • Pushing the envelope: Structure, function and dynamics of the nuclear periphery
    • Hetzer, M., Walther, T.C. & Mattaj, I.W. Pushing the envelope: structure, function and dynamics of the nuclear periphery. Annu. Rev. Cell Dev. Biol. 21, 347-380 (2005).
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 347-380
    • Hetzer, M.1    Walther, T.C.2    Mattaj, I.W.3
  • 2
    • 4344645948 scopus 로고    scopus 로고
    • Cotranslational integration and initial sorting at the endoplasmic reticulum translocon of protein 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 protein destined for the inner nuclear membrane. Proc. Natl Acad. Sci. USA 101, 12537-12542 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 12537-12542
    • Saksena, S.1    Shao, Y.2    Braunagel, S.C.3    Summers, M.D.4    Johnson, A.E.5
  • 3
    • 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. USA 101, 8372-8377 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 8372-8377
    • Braunagel, S.C.1
  • 4
    • 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. 167, 1051-1062 (2004).
    • (2004) J. Cell Biol. , vol.167 , pp. 1051-1062
    • Ohba, T.1    Schirmer, E.C.2    Nishimoto, T.3    Gerace, L.4
  • 5
    • 0030971788 scopus 로고    scopus 로고
    • N-terminal sequences from Autographa californica nuclear polyhedrosis virus envelope proteins ODV-E66 and ODV-E25 are sufficient to direct reporter proteins to the nuclear envelope, intranuclear microvesicles and the envelope of the occlusion-derived virus
    • Hong, T., Summers, M.D. & Braunagel, S.C. N-terminal sequences from Autographa californica nuclear polyhedrosis virus envelope proteins ODV-E66 and ODV-E25 are sufficient to direct reporter proteins to the nuclear envelope, intranuclear microvesicles and the envelope of the occlusion-derived virus. Proc. Natl Acad. Sci. USA 94, 4050-4055 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 4050-4055
    • Hong, T.1    Summers, M.D.2    Braunagel, S.C.3
  • 6
    • 0034763884 scopus 로고    scopus 로고
    • Effects of deletion and overexpression of the Autographa californica nuclear polyhedrosis virus FP25K gene on synthesis of two occlusion-derived virus envelope proteins and their transport into virus-induced intranuclear membranes
    • Rosas-Acosta, G., Braunagel, S.C. & Summers, M.D. Effects of deletion and overexpression of the Autographa californica nuclear polyhedrosis virus FP25K gene on synthesis of two occlusion-derived virus envelope proteins and their transport into virus-induced intranuclear membranes. J. Virol. 75, 10829-10842 (2001).
    • (2001) J. Virol. , vol.75 , pp. 10829-10842
    • Rosas-Acosta, G.1    Braunagel, S.C.2    Summers, M.D.3
  • 7
    • 0027985063 scopus 로고
    • Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore
    • Crowley, K.S., Liao, S., Worrell, V.E., Reinhart, G.D. & Johnson, A.E. Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore. Cell 78, 461-471 (1994).
    • (1994) Cell , vol.78 , pp. 461-471
    • Crowley, K.S.1    Liao, S.2    Worrell, V.E.3    Reinhart, G.D.4    Johnson, A.E.5
  • 8
    • 0027162564 scopus 로고
    • The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation
    • Crowley, K.S., Reinhart, G.D. & Johnson, A.E. The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation. Cell 73, 1101-1115 (1993).
    • (1993) Cell , vol.73 , pp. 1101-1115
    • Crowley, K.S.1    Reinhart, G.D.2    Johnson, A.E.3
  • 9
    • 4444293377 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the translationally controlled tumor protein gene in Bombyx mori
    • Lee, J.M. et al. Molecular cloning and characterization of the translationally controlled tumor protein gene in Bombyx mori. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 139, 35-43 (2004).
    • (2004) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.139 , pp. 35-43
    • Lee, J.M.1
  • 10
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul, S.F. et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25, 3389-3402 (1997).
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1
  • 12
    • 0036846540 scopus 로고    scopus 로고
    • Importin α can migrate into the nucleus in an importin β- and Ran-independent manner
    • Miyamoto, Y. et al. Importin α can migrate into the nucleus in an importin β- and Ran-independent manner. EMBO J. 21, 5833-5842 (2002).
    • (2002) EMBO J. , vol.21 , pp. 5833-5842
    • Miyamoto, Y.1
  • 13
    • 0141992130 scopus 로고    scopus 로고
    • Cotranslational protein integration into the ER membrane is mediated by the binding of nascent chains to translocon proteins
    • McCormick, P.J., Miao, Y., Shao, Y., Lin, J. & Johnson, A.E. Cotranslational protein integration into the ER membrane is mediated by the binding of nascent chains to translocon proteins. Mol. Cell 12, 329-341 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 329-341
    • McCormick, P.J.1    Miao, Y.2    Shao, Y.3    Lin, J.4    Johnson, A.E.5
  • 14
    • 0036469888 scopus 로고    scopus 로고
    • Importins fulfill a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains
    • Jakel, S., Mingot, J.-M., Schwarzmaier, P., Hartmann, E. & Görlich, D. Importins fulfill a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains. EMBO J. 21, 377-386 (2002).
    • (2002) EMBO J. , vol.21 , pp. 377-386
    • Jakel, S.1    Mingot, J.-M.2    Schwarzmaier, P.3    Hartmann, E.4    Görlich, D.5
  • 16
    • 8644262258 scopus 로고    scopus 로고
    • Importin beta: Conducting a much larger cellular symphony
    • Harel, A. & Forbes, D.J. Importin beta: conducting a much larger cellular symphony. Mol. Cell 16, 319-330 (2004).
    • (2004) Mol. Cell , vol.16 , pp. 319-330
    • Harel, A.1    Forbes, D.J.2
  • 17
    • 16344379538 scopus 로고    scopus 로고
    • Importin α transports CaMKIV to the nucleus without utilizing importin β
    • Kotera, I. et al. Importin α transports CaMKIV to the nucleus without utilizing importin β. EMBO J. 24, 942-951 (2005).
    • (2005) EMBO J. , vol.24 , pp. 942-951
    • Kotera, I.1
  • 18
    • 14744267687 scopus 로고    scopus 로고
    • Importin-α promotes passage through the nuclear pore complex of human immunodeficiency virus Type 1 Vpr
    • Kamata, M., Nitahara-Kasahara, Y., Miyamoto, Y., Yoneda, Y. & Aida, Y. Importin-α promotes passage through the nuclear pore complex of human immunodeficiency virus Type 1 Vpr. J. Virol. 79, 3557-3564 (2005).
    • (2005) J. Virol. , vol.79 , pp. 3557-3564
    • Kamata, M.1    Nitahara-Kasahara, Y.2    Miyamoto, Y.3    Yoneda, Y.4    Aida, Y.5
  • 19
    • 0033612576 scopus 로고    scopus 로고
    • Nuclear import of the TATA-binding protein: Mediation by the karyopherin Kap114p and a possible mechanism for intranuclear targeting
    • Pemberton, L.F., Rosenblum, J.S. & Blobel, G. Nuclear import of the TATA-binding protein: mediation by the karyopherin Kap114p and a possible mechanism for intranuclear targeting. J. Cell Biol. 145, 1407-1417 (1999).
    • (1999) J. Cell Biol. , vol.145 , pp. 1407-1417
    • Pemberton, L.F.1    Rosenblum, J.S.2    Blobel, G.3
  • 20
    • 0028064385 scopus 로고
    • Genetic and physical interactions between Srp1p and nuclear pore complex proteins Nup1p and Nup2p
    • Belanger, K.D., Kenna, M.A., Wei, S. & Davis, L.I. Genetic and physical interactions between Srp1p and nuclear pore complex proteins Nup1p and Nup2p. J. Cell Biol. 126, 619-630 (1994).
    • (1994) J. Cell Biol. , vol.126 , pp. 619-630
    • Belanger, K.D.1    Kenna, M.A.2    Wei, S.3    Davis, L.I.4
  • 21
    • 0033766479 scopus 로고    scopus 로고
    • Nup2p, a yeast nucleoporin, functions in bidirectional transport of importin α
    • Solsbacher, J., Maurer, P., Vogel, F. & Schlenstedt, G. Nup2p, a yeast nucleoporin, functions in bidirectional transport of importin α. Mol. Cell. Biol. 20, 8468-8479 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8468-8479
    • Solsbacher, J.1    Maurer, P.2    Vogel, F.3    Schlenstedt, G.4
  • 22
    • 0030930859 scopus 로고    scopus 로고
    • RanGTP-mediated nuclear export of karyopherin α involves its interaction with the nucleoporin Nup153
    • Moroianu, J., Blobel, G. & Radu, A. RanGTP-mediated nuclear export of karyopherin α involves its interaction with the nucleoporin Nup153. Proc. Natl Acad. Sci. USA 94, 9699-9704 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 9699-9704
    • Moroianu, J.1    Blobel, G.2    Radu, A.3
  • 23
    • 0037047430 scopus 로고    scopus 로고
    • Npap60/Nup50 is a tri-stable switch that stimulates importin-α: β-mediated nuclear protein import
    • Lindsay, M.E., Plafker, K., Smith, A.E., Clurman, B.E. & Macara, I.G. Npap60/Nup50 is a tri-stable switch that stimulates importin-α:β- mediated nuclear protein import. Cell 110, 349-360 (2002).
    • (2002) Cell , vol.110 , pp. 349-360
    • Lindsay, M.E.1    Plafker, K.2    Smith, A.E.3    Clurman, B.E.4    Macara, I.G.5
  • 24
    • 0037307453 scopus 로고    scopus 로고
    • Npap60: A new player in nuclear protein import
    • Moore, M.S. Npap60: a new player in nuclear protein import. Trends Cell Biol. 13, 61-64 (2003).
    • (2003) Trends Cell Biol. , vol.13 , pp. 61-64
    • Moore, M.S.1
  • 25
    • 27744577638 scopus 로고    scopus 로고
    • Nup50/Npap60 function in nuclear import complex disassembly and importin recycling
    • Matsuura, Y. & Stewart, M. Nup50/Npap60 function in nuclear import complex disassembly and importin recycling. EMBO J. 24, 3681-3689 (2005).
    • (2005) EMBO J. , vol.24 , pp. 3681-3689
    • Matsuura, Y.1    Stewart, M.2
  • 26
    • 4544365809 scopus 로고    scopus 로고
    • Integration of retrograde axonal and nuclear transport mechanisms in neurons: Implications for therapeutics
    • Hanz, S. & Fainzilber, M. Integration of retrograde axonal and nuclear transport mechanisms in neurons: implications for therapeutics. Neuroscientist 10, 404-408 (2004).
    • (2004) Neuroscientist , vol.10 , pp. 404-408
    • Hanz, S.1    Fainzilber, M.2
  • 27
    • 9144273965 scopus 로고    scopus 로고
    • Axoplasmic importins enable retrograde inujry signaling in lesioned nerve
    • Hanz, S. et al. Axoplasmic importins enable retrograde inujry signaling in lesioned nerve. Neuron 40, 1095-1104 (2003).
    • (2003) Neuron , vol.40 , pp. 1095-1104
    • Hanz, S.1
  • 28
    • 2342526606 scopus 로고    scopus 로고
    • Nucleus hears axon's pain
    • Blesch, A. & Tuszynski, M.H. Nucleus hears axon's pain. Nat. Med. 10, 236-237 (2004).
    • (2004) Nat. Med. , vol.10 , pp. 236-237
    • Blesch, A.1    Tuszynski, M.H.2
  • 29
    • 2342478595 scopus 로고    scopus 로고
    • Importin α associates with membranes and participates in nuclear envelope assembly in vitro
    • Machet, V., Köcher, T., Wilm, T. & Mattaj, I.W. Importin α associates with membranes and participates in nuclear envelope assembly in vitro. EMBO J. 23, 1526-1535 (2004).
    • (2004) EMBO J. , vol.23 , pp. 1526-1535
    • Machet, V.1    Köcher, T.2    Wilm, T.3    Mattaj, I.W.4
  • 30
    • 0034697971 scopus 로고    scopus 로고
    • Genetic evidence for selective transport of opsin and arrestin by kinesin-II in mammalian receptors
    • Marzalek, J.R. et al. Genetic evidence for selective transport of opsin and arrestin by kinesin-II in mammalian receptors. Cell 102, 175-187 (2000).
    • (2000) Cell , vol.102 , pp. 175-187
    • Marzalek, J.R.1
  • 31
    • 0036185994 scopus 로고    scopus 로고
    • Transport to the photoreceptor outer segment by myosin Vila and kinesin II
    • Williams, D.S. Transport to the photoreceptor outer segment by myosin Vila and kinesin II. Vision Res. 42, 455-462 (2002).
    • (2002) Vision Res. , vol.42 , pp. 455-462
    • Williams, D.S.1
  • 32
    • 0038558166 scopus 로고    scopus 로고
    • Importin α-regulated nucleation of microtubules by TPX2
    • Schatz, C.A. et al. Importin α-regulated nucleation of microtubules by TPX2. EMBO J. 22, 2060-2070 (2003).
    • (2003) EMBO J. , vol.22 , pp. 2060-2070
    • Schatz, C.A.1
  • 33
    • 17744380396 scopus 로고    scopus 로고
    • Ran induces spindle assembly by reversing the inhibitory effect of importin α on TPX2 activity
    • Gruss, O.J. et al. Ran induces spindle assembly by reversing the inhibitory effect of importin α on TPX2 activity. Cell 104, 83-93 (2001).
    • (2001) Cell , vol.104 , pp. 83-93
    • Gruss, O.J.1
  • 34
    • 0032484482 scopus 로고    scopus 로고
    • Autographa californica nuclear polyhedrosis virus: Subcellular localization and protein trafficking of BV/ODV-E26 to intranuclear membranes and viral envelopes
    • Beniya, H., Braunagel, S.C. & Summers, M.D. Autographa californica nuclear polyhedrosis virus: subcellular localization and protein trafficking of BV/ODV-E26 to intranuclear membranes and viral envelopes. Virology 240, 64-75 (1998).
    • (1998) Virology , vol.240 , pp. 64-75
    • Beniya, H.1    Braunagel, S.C.2    Summers, M.D.3
  • 35
    • 25144515509 scopus 로고    scopus 로고
    • Nuclear envelope, nuclear lamina, and inherited disease
    • Worman, H.J. & Courvalin, J.-C. Nuclear envelope, nuclear lamina, and inherited disease. Int. Rev. Cytol. 246, 231-279 (2005).
    • (2005) Int. Rev. Cytol. , vol.246 , pp. 231-279
    • Worman, H.J.1    Courvalin, J.-C.2
  • 36
    • 0029916756 scopus 로고    scopus 로고
    • Identification and analysis of an Autographa californica nuclear polyhedrosis virus structural protein of the occlusion-derived virus envelope, ODV-E56
    • Braunagel, S.C., Elton, D.M., Ma, H. & Summers, M.D. Identification and analysis of an Autographa californica nuclear polyhedrosis virus structural protein of the occlusion-derived virus envelope, ODV-E56. Virology 217, 97-110 (1996).
    • (1996) Virology , vol.217 , pp. 97-110
    • Braunagel, S.C.1    Elton, D.M.2    Ma, H.3    Summers, M.D.4


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