메뉴 건너뛰기




Volumn 20, Issue 24, 2009, Pages 5106-5116

Oxidative stress inhibits nuclear protein export by multiple mechanisms that target FG nucleoporins and Crm1

Author keywords

[No Author keywords available]

Indexed keywords

BETA N ACETYLHEXOSAMINIDASE; EXPORTIN 1; N ACETYLGLUCOSAMINE; NUCLEOPORIN; NUCLEOPORIN 98; NUCLEOPORIN NUP214; NUCLEOPORIN NUP358; NUCLEOPORIN NUP62; PHOSPHATASE; RAN PROTEIN; UNCLASSIFIED DRUG;

EID: 73849122773     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E09-05-0397     Document Type: Article
Times cited : (79)

References (40)
  • 1
    • 54049139647 scopus 로고    scopus 로고
    • Nucleoporin 88 (Nup88) is regulated by hypertonic stress in kidney cells to retain the transcription factor tonicity enhancer-binding protein (TonEBP) in the nucleus
    • Andres-Hernando, A., Lanaspa, M. A., Rivard, C. J., and Berl, T. (2008). Nucleoporin 88 (Nup88) is regulated by hypertonic stress in kidney cells to retain the transcription factor tonicity enhancer-binding protein (TonEBP) in the nucleus. J. Biol. Chem. 283, 25082-25090.
    • (2008) J. Biol. Chem , vol.283 , pp. 25082-25090
    • Andres-Hernando, A.1    Lanaspa, M.A.2    Rivard, C.J.3    Berl, T.4
  • 2
    • 17044441683 scopus 로고    scopus 로고
    • The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates
    • Bachi, A., et al. (2000). The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates. RNA 6, 136-158.
    • (2000) RNA , vol.6 , pp. 136-158
    • Bachi, A.1
  • 3
    • 1542374020 scopus 로고    scopus 로고
    • Nup358/RanBP2 attaches to the nuclear pore complex via association with Nup88 and Nup214/CAN and plays a supporting role in CRM1-mediated nuclear protein export
    • Bernad, R., van der Velde, H., Fornerod, M., and Pickersgill, H. (2004). Nup358/RanBP2 attaches to the nuclear pore complex via association with Nup88 and Nup214/CAN and plays a supporting role in CRM1-mediated nuclear protein export. Mol. Cell. Biol. 24, 2373-2384.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 2373-2384
    • Bernad, R.1    van der Velde, H.2    Fornerod, M.3    Pickersgill, H.4
  • 4
    • 58249089343 scopus 로고    scopus 로고
    • Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells
    • D'Angelo, M. A., Raices, M., Panowski, S. H., and Hetzer, M. W. (2009). Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells. Cell 136, 284-295.
    • (2009) Cell , vol.136 , pp. 284-295
    • D'Angelo, M.A.1    Raices, M.2    Panowski, S.H.3    Hetzer, M.W.4
  • 6
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in physiological control of cell function
    • Dröge, W. (2002). Free radicals in physiological control of cell function. Physiol. Rev. 82, 47-95.
    • (2002) Physiol. Rev , vol.82 , pp. 47-95
    • Dröge, W.1
  • 7
    • 2942632961 scopus 로고    scopus 로고
    • Role of Nup98 in nuclear entry of human immunodeficiency virus type 1 cDNA
    • Ebina, H., Aoki, J., Hatta, S., Yoshida, T., and Koyanagi, Y. (2004). Role of Nup98 in nuclear entry of human immunodeficiency virus type 1 cDNA. Microb. Infect. 6, 715-724.
    • (2004) Microb. Infect , vol.6 , pp. 715-724
    • Ebina, H.1    Aoki, J.2    Hatta, S.3    Yoshida, T.4    Koyanagi, Y.5
  • 8
    • 33846522832 scopus 로고    scopus 로고
    • Oxidative stress as the leading cause of acute myocardial infarction in diabetics
    • Filippo, C. D., Cuzzocrea, S., Rossi, F., Marfella, R., and D'Amico, M. (2006). Oxidative stress as the leading cause of acute myocardial infarction in diabetics. Cardiovasc. Drug Rev. 24, 77-87.
    • (2006) Cardiovasc. Drug Rev , vol.24 , pp. 77-87
    • Filippo, C.D.1    Cuzzocrea, S.2    Rossi, F.3    Marfella, R.4    D'Amico, M.5
  • 9
    • 48249085391 scopus 로고    scopus 로고
    • Oxidative stress as a major culprit in kidney disease in diabetes
    • Forbes, J. M., Coughlan, M. T., and Cooper, M. E. (2008). Oxidative stress as a major culprit in kidney disease in diabetes. Diabetes 57, 1446-1454.
    • (2008) Diabetes , vol.57 , pp. 1446-1454
    • Forbes, J.M.1    Coughlan, M.T.2    Cooper, M.E.3
  • 10
    • 0031053791 scopus 로고    scopus 로고
    • The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and a novel nuclear pore component Nup88
    • Fornerod, M., van Deursen, J., van Baal, S., Reynolds, A., Davis, D., Murti, K. G., Fransen, J., and Grosveld, G. (1997). The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and a novel nuclear pore component Nup88. EMBO J. 16, 807-816.
    • (1997) EMBO J , vol.16 , pp. 807-816
    • Fornerod, M.1    van Deursen, J.2    van Baal, S.3    Reynolds, A.4    Davis, D.5    Murti, K.G.6    Fransen, J.7    Grosveld, G.8
  • 11
    • 0036223543 scopus 로고    scopus 로고
    • Nup98 is a mobile nucleoporin with transcription dependent dynamics
    • Griffis, E. R., Altan, N., Lippincott-Schwartz, J., and Powers, M. A. (2002). Nup98 is a mobile nucleoporin with transcription dependent dynamics. Mol. Biol. Cell 13, 1282-1297.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1282-1297
    • Griffis, E.R.1    Altan, N.2    Lippincott-Schwartz, J.3    Powers, M.A.4
  • 12
    • 0037323478 scopus 로고    scopus 로고
    • Nup98 localizes to both nuclear and cytoplasmic sides of the nuclear pore and binds to two distinct nucleoporin subcomplexes
    • Griffis, E. R., Xu, S., and Powers, M. A. (2003). Nup98 localizes to both nuclear and cytoplasmic sides of the nuclear pore and binds to two distinct nucleoporin subcomplexes. Mol. Biol. Cell 14, 600-610.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 600-610
    • Griffis, E.R.1    Xu, S.2    Powers, M.A.3
  • 13
    • 33748657386 scopus 로고    scopus 로고
    • Nup214 is required for CRM1-dependent nuclear protein export in vivo
    • Hutten, S., and Kehlenbach, R. H. (2006). Nup214 is required for CRM1-dependent nuclear protein export in vivo. Mol. Cell. Biol. 26, 6772-6785.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 6772-6785
    • Hutten, S.1    Kehlenbach, R.H.2
  • 14
    • 33947726050 scopus 로고    scopus 로고
    • CRM1-mediated nuclear export: To the pore and beyond
    • Hutten, S., and Kehlenbach, R. H. (2007). CRM1-mediated nuclear export: to the pore and beyond. Trends Cell Biol. 17, 193-201.
    • (2007) Trends Cell Biol , vol.17 , pp. 193-201
    • Hutten, S.1    Kehlenbach, R.H.2
  • 15
    • 48249150289 scopus 로고    scopus 로고
    • The Nup358-RanGAP complex is required for efficient importin alpha/beta-dependent nuclear import
    • Hutten, S., Flotho, A., Melchior, F., and Kehlenbach, R. H. (2008). The Nup358-RanGAP complex is required for efficient importin alpha/beta-dependent nuclear import. Mol. Biol. Cell 19, 2300-2310.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2300-2310
    • Hutten, S.1    Flotho, A.2    Melchior, F.3    Kehlenbach, R.H.4
  • 16
    • 1842715846 scopus 로고    scopus 로고
    • The RanGAP1-RanBP2 complex is essential for microtubule-kinetochore interactions in vivo
    • Joseph, J., Liu, S., Jablonski, S. A., Yen, T. J., and Dasso, M. (2004). The RanGAP1-RanBP2 complex is essential for microtubule-kinetochore interactions in vivo. Curr. Biol. 14, 611-617.
    • (2004) Curr. Biol , vol.14 , pp. 611-617
    • Joseph, J.1    Liu, S.2    Jablonski, S.A.3    Yen, T.J.4    Dasso, M.5
  • 17
    • 38049150928 scopus 로고    scopus 로고
    • The nucleoporin Nup358 associates with and regulates interphase microtubules
    • Joseph, J., and Dasso, M. (2008). The nucleoporin Nup358 associates with and regulates interphase microtubules. FEBS Lett. 582, 190-196.
    • (2008) FEBS Lett , vol.582 , pp. 190-196
    • Joseph, J.1    Dasso, M.2
  • 18
    • 0033577860 scopus 로고    scopus 로고
    • A role for RanBP1 in the release of Crm1 from the nuclear pore complex in a terminal step of nuclear export
    • Kehlenbach, R. H., Dickmanns, Kehlenbach, A., A., Guan, T., and Gerace, L. (1999). A role for RanBP1 in the release of Crm1 from the nuclear pore complex in a terminal step of nuclear export. J. Cell Biol. 145, 645-657.
    • (1999) J. Cell Biol , vol.145 , pp. 645-657
    • Kehlenbach, R.1    Dickmanns, H.2    Kehlenbach, A.A.3    Guan, T.4    Gerace, L.5
  • 19
    • 44749083495 scopus 로고    scopus 로고
    • Dissection of the molecular mechanisms that control the nuclear accumulation of transport factors importin-α and CAS in stressed cells
    • Kodiha, M., Bański, P., Ho-Wo-Cheong, D., and Stochaj, U. (2008b). Dissection of the molecular mechanisms that control the nuclear accumulation of transport factors importin-α and CAS in stressed cells. Cell. Mol. Life Sci. 65, 1756-1767.
    • (2008) Cell. Mol. Life Sci , vol.65 , pp. 1756-1767
    • Kodiha, M.1    Bański, P.2    Ho-Wo-Cheong, D.3    Stochaj, U.4
  • 20
    • 55649105063 scopus 로고    scopus 로고
    • Kodiha, M., Brown, C. M., and Stochaj, U. (2008c). Analysis of signaling events by combining high-throughput screening technology with computer-based image analysis. Sci. Signal. 1, 12
    • Kodiha, M., Brown, C. M., and Stochaj, U. (2008c). Analysis of signaling events by combining high-throughput screening technology with computer-based image analysis. Sci. Signal. 1, 12
  • 21
    • 4344582296 scopus 로고    scopus 로고
    • Multiple mechanisms promote the inhibition of classical nuclear import upon exposure to severe oxidative stress
    • Kodiha, M., Chu, A., Matusiewicz, N., and Stochaj, U. (2004). Multiple mechanisms promote the inhibition of classical nuclear import upon exposure to severe oxidative stress. Cell Death Differ. 11, 862-874.
    • (2004) Cell Death Differ , vol.11 , pp. 862-874
    • Kodiha, M.1    Chu, A.2    Matusiewicz, N.3    Stochaj, U.4
  • 22
    • 39149111609 scopus 로고    scopus 로고
    • Oxidative stress mislocalizes and retains transport factor importin-α and nucleoporins Nup153 and Nup88 in nuclei where they generate high molecular mass complexes
    • Kodiha, M., Tran, D., Qian, C., Morogan, A., Presley, J. F., Brown, C. M., and Stochaj, U. (2008a). Oxidative stress mislocalizes and retains transport factor importin-α and nucleoporins Nup153 and Nup88 in nuclei where they generate high molecular mass complexes. Biochim. Biophys. Acta 1783, 405-418.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 405-418
    • Kodiha, M.1    Tran, D.2    Qian, C.3    Morogan, A.4    Presley, J.F.5    Brown, C.M.6    Stochaj, U.7
  • 23
    • 73849148866 scopus 로고    scopus 로고
    • Kodiha, M., Umar, R., and Stochaj, U. (2009). Optimized immunofluorescence staining protocols to detect the nucleoporin Nup98 in different subcellular compartments. Nat. Netw. Protoc. doi: 10.1038/nprot.2009. 16.
    • Kodiha, M., Umar, R., and Stochaj, U. (2009). Optimized immunofluorescence staining protocols to detect the nucleoporin Nup98 in different subcellular compartments. Nat. Netw. Protoc. doi: 10.1038/nprot.2009. 16.
  • 24
    • 70349284540 scopus 로고    scopus 로고
    • Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells. ACS
    • Leonard, S. E., Reddie, K. G., and Carroll, K. S. (2009) Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells. ACS Chem. Biol. 4, 783-799.
    • (2009) Chem. Biol , vol.4 , pp. 783-799
    • Leonard, S.E.1    Reddie, K.G.2    Carroll, K.S.3
  • 25
    • 0035954439 scopus 로고    scopus 로고
    • Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export
    • Lindsay, M. E., Holaska, J. M., Welch, K., Paschal, B. M., and Macara, I. G. (2001). Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export. J. Cell Biol. 153, 1391-1402.
    • (2001) J. Cell Biol , vol.153 , pp. 1391-1402
    • Lindsay, M.E.1    Holaska, J.M.2    Welch, K.3    Paschal, B.M.4    Macara, I.G.5
  • 26
    • 33645015535 scopus 로고    scopus 로고
    • Nuclear transport is becoming crystal clear
    • Madrid, A. S., and Weis, K. (2005). Nuclear transport is becoming crystal clear. Chromosoma 115, 98-109.
    • (2005) Chromosoma , vol.115 , pp. 98-109
    • Madrid, A.S.1    Weis, K.2
  • 27
    • 33644863491 scopus 로고    scopus 로고
    • Caspases target only two architectural components within the core structure of the nuclear pore complex
    • Patre, M., Tabbert, A., Hermann, D., Walczak, H., Rackwitz, H., Cordes, V. C., and Ferrando-May, E. (2006). Caspases target only two architectural components within the core structure of the nuclear pore complex. J. Biol. Chem. 281, 1296-1304.
    • (2006) J. Biol. Chem , vol.281 , pp. 1296-1304
    • Patre, M.1    Tabbert, A.2    Hermann, D.3    Walczak, H.4    Rackwitz, H.5    Cordes, V.C.6    Ferrando-May, E.7
  • 29
    • 0031046477 scopus 로고    scopus 로고
    • The vertebrate GLFG nucleoporin, Nup98, is an essential component of multiple RNA export pathways
    • Powers, M. A., Forbes, D. J., Dahlberg, J. E., and Lund, E. (1997). The vertebrate GLFG nucleoporin, Nup98, is an essential component of multiple RNA export pathways. J. Cell Biol. 136, 241-250.
    • (1997) J. Cell Biol , vol.136 , pp. 241-250
    • Powers, M.A.1    Forbes, D.J.2    Dahlberg, J.E.3    Lund, E.4
  • 30
    • 33749170007 scopus 로고    scopus 로고
    • The carrier Msn5p/Kap142p promotes nuclear export of the hsp70 Ssa4p and relocates in response to stress
    • Quan, X., Tsoulos, P., Kuritzky, A., Zhang, R., and Stochaj, U. (2006). The carrier Msn5p/Kap142p promotes nuclear export of the hsp70 Ssa4p and relocates in response to stress. Mol. Microbiol. 62, 592-609.
    • (2006) Mol. Microbiol , vol.62 , pp. 592-609
    • Quan, X.1    Tsoulos, P.2    Kuritzky, A.3    Zhang, R.4    Stochaj, U.5
  • 31
    • 33644851224 scopus 로고    scopus 로고
    • Monitoring the disruption of nuclear envelopes in interphase cells with GFP-β- galactosidase
    • Sánchez, L., Kodiha, M., and Stochaj, U. (2005). Monitoring the disruption of nuclear envelopes in interphase cells with GFP-β- galactosidase. J. Biomol. Tech. 16, 235-238.
    • (2005) J. Biomol. Tech , vol.16 , pp. 235-238
    • Sánchez, L.1    Kodiha, M.2    Stochaj, U.3
  • 32
    • 17044415652 scopus 로고    scopus 로고
    • Modularity within the architecture of the nuclear pore complex
    • Schwartz, T. U. (2005). Modularity within the architecture of the nuclear pore complex. Curr. Opin. Struct. Biol. 15, 221-226.
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 221-226
    • Schwartz, T.U.1
  • 33
    • 33745858668 scopus 로고    scopus 로고
    • The N-terminal domain of the mammalian nucleoporin p62 interacts with other nucleoporins of the FXFG family during interphase
    • Stochaj, U., Bański, P., Kodiha, M., and Matusiewicz, N. (2006). The N-terminal domain of the mammalian nucleoporin p62 interacts with other nucleoporins of the FXFG family during interphase. Exp. Cell Res. 312, 2490-2499.
    • (2006) Exp. Cell Res , vol.312 , pp. 2490-2499
    • Stochaj, U.1    Bański, P.2    Kodiha, M.3    Matusiewicz, N.4
  • 34
    • 0033729420 scopus 로고    scopus 로고
    • Stochaj, Rassadi, U., R., and Chiu, J. (2000). Stress-mediated inhibition of classical nuclear import pathway and nuclear accumulation of the small GTPase Gsp1p. FASEB J. 14, 2130-2132.
    • Stochaj, Rassadi, U., R., and Chiu, J. (2000). Stress-mediated inhibition of classical nuclear import pathway and nuclear accumulation of the small GTPase Gsp1p. FASEB J. 14, 2130-2132.
  • 35
    • 33744967486 scopus 로고    scopus 로고
    • Dynamic nuclear pore complexes, life on the edge
    • Tran, E. J., and Wente, S. R. (2006). Dynamic nuclear pore complexes, life on the edge. Cell 125, 1041-1053.
    • (2006) Cell , vol.125 , pp. 1041-1053
    • Tran, E.J.1    Wente, S.R.2
  • 36
    • 36749081534 scopus 로고    scopus 로고
    • Crossing the nuclear envelope, hierarchical regulation of nucleocytoplasmic transport
    • Terry, L. J., Shows, E. B., and Wente, S. R. (2007). Crossing the nuclear envelope, hierarchical regulation of nucleocytoplasmic transport. Science 318, 1412-1416.
    • (2007) Science , vol.318 , pp. 1412-1416
    • Terry, L.J.1    Shows, E.B.2    Wente, S.R.3
  • 38
    • 60349095205 scopus 로고    scopus 로고
    • Zachara, N. E. (2008). Detection and analysis of (O-linked β-N-acetylglucosamine)-modified proteins. In: The Nucleus, 2, Chromatin, Transcription, Envelope, Proteins, Dynamics, and Imaging, ed. R. Hancock, Totowa, NJ: Humana Press, 227-254.
    • Zachara, N. E. (2008). Detection and analysis of (O-linked β-N-acetylglucosamine)-modified proteins. In: The Nucleus, Volume 2, Chromatin, Transcription, Envelope, Proteins, Dynamics, and Imaging, ed. R. Hancock, Totowa, NJ: Humana Press, 227-254.
  • 39
    • 3042534011 scopus 로고    scopus 로고
    • Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress. A survival response of mammalian cells
    • Zachara, N. E., O'Donnell, N., Cheung, W. D., Mercer, J. J., Marth, J. D., and Hart, G. W. (2004). Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress. A survival response of mammalian cells. J. Biol. Chem. 279, 30133-30142.
    • (2004) J. Biol. Chem , vol.279 , pp. 30133-30142
    • Zachara, N.E.1    O'Donnell, N.2    Cheung, W.D.3    Mercer, J.J.4    Marth, J.D.5    Hart, G.W.6
  • 40
    • 0032888954 scopus 로고    scopus 로고
    • Nucleoporin Nup98 and Nup214 participate in nuclear export of human immunodeficiency virus type 1
    • Zolothukin, A. S., and Felber, B. K. (1999). Nucleoporin Nup98 and Nup214 participate in nuclear export of human immunodeficiency virus type 1 Rev. J. Virol. 73, 120-127.
    • (1999) Rev. J. Virol , vol.73 , pp. 120-127
    • Zolothukin, A.S.1    Felber, B.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.