메뉴 건너뛰기




Volumn 318, Issue 10, 2012, Pages 1086-1093

Cellular stress stimulates nuclear localization signal (NLS) independent nuclear transport of MRJ

Author keywords

DnaJB6; Heat shock; MRJ; NLS

Indexed keywords

CHAPERONE; CYTOKINE; HEAT SHOCK PROTEIN 40; PROTEIN MRJ; UNCLASSIFIED DRUG;

EID: 84860358930     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2012.03.024     Document Type: Article
Times cited : (9)

References (44)
  • 3
    • 79955072223 scopus 로고    scopus 로고
    • Molecular chaperone-mediated rescue of mitophagy by a Parkin RING1 domain mutant
    • Rose J.M., Novoselov S.S., Robinson P.A., Cheetham M.E. Molecular chaperone-mediated rescue of mitophagy by a Parkin RING1 domain mutant. Hum Mol Genet. 2011, 20(1):16-27.
    • (2011) Hum Mol Genet. , vol.20 , Issue.1 , pp. 16-27
    • Rose, J.M.1    Novoselov, S.S.2    Robinson, P.A.3    Cheetham, M.E.4
  • 4
    • 0037205425 scopus 로고    scopus 로고
    • Characterization of a brain-enriched chaperone, MRJ, that inhibits Huntingtin aggregation and toxicity independently
    • Chuang J.Z., Zhou H., Zhu M., Li S.H., Li X.J., Sung C.H. Characterization of a brain-enriched chaperone, MRJ, that inhibits Huntingtin aggregation and toxicity independently. J. Biol. Chem. 2002, 277:19831-19838.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19831-19838
    • Chuang, J.Z.1    Zhou, H.2    Zhu, M.3    Li, S.H.4    Li, X.J.5    Sung, C.H.6
  • 7
    • 74049156323 scopus 로고    scopus 로고
    • Neural stem cell self-renewal requires the Mrj co-chaperone
    • Watson E.D., Mattar P., Schuurmans C., Cross J.C. Neural stem cell self-renewal requires the Mrj co-chaperone. Dev. Dyn. 2009, 238:2564-2574.
    • (2009) Dev. Dyn. , vol.238 , pp. 2564-2574
    • Watson, E.D.1    Mattar, P.2    Schuurmans, C.3    Cross, J.C.4
  • 8
    • 59349103723 scopus 로고    scopus 로고
    • Cell cycle specific expression and nucleolar localization of human J-domain containing co-chaperone Mrj
    • Dey S., Banerjee P., Saha P. Cell cycle specific expression and nucleolar localization of human J-domain containing co-chaperone Mrj. Mol. Cell. Biochem. 2009, 322:137-142.
    • (2009) Mol. Cell. Biochem. , vol.322 , pp. 137-142
    • Dey, S.1    Banerjee, P.2    Saha, P.3
  • 9
    • 0032930952 scopus 로고    scopus 로고
    • Mrj encodes a DnaJ-related co-chaperone that is essential for murine placental development
    • Hunter P.J., Swanson B.J., Haendel M.A., Lyons G.E., Cross J.C. Mrj encodes a DnaJ-related co-chaperone that is essential for murine placental development. Development 1999, 126:1247-1258.
    • (1999) Development , vol.126 , pp. 1247-1258
    • Hunter, P.J.1    Swanson, B.J.2    Haendel, M.A.3    Lyons, G.E.4    Cross, J.C.5
  • 10
    • 0347356276 scopus 로고    scopus 로고
    • Determination of downstream targets of FGF signalling using gene trap and cDNA subtractive approaches
    • Tateossian H., Powles N., Dickinson R., Ficker M., Maconochie M. Determination of downstream targets of FGF signalling using gene trap and cDNA subtractive approaches. Exp. Cell Res. 2004, 292:101-114.
    • (2004) Exp. Cell Res. , vol.292 , pp. 101-114
    • Tateossian, H.1    Powles, N.2    Dickinson, R.3    Ficker, M.4    Maconochie, M.5
  • 11
    • 34249059782 scopus 로고    scopus 로고
    • The Mrj co-chaperone mediates keratin turnover and prevents the formation of toxic inclusion bodies in trophoblast cells of the placenta
    • Watson E.D., Geary-Joo C., Hughes M., Cross J.C. The Mrj co-chaperone mediates keratin turnover and prevents the formation of toxic inclusion bodies in trophoblast cells of the placenta. Development 2007, 134:1809-1817.
    • (2007) Development , vol.134 , pp. 1809-1817
    • Watson, E.D.1    Geary-Joo, C.2    Hughes, M.3    Cross, J.C.4
  • 14
    • 84867399176 scopus 로고    scopus 로고
    • DNAJB6 chaperones PP2A mediated dephosphorylation of GSK3beta to downregulate beta-catenin transcription target, osteopontin, Oncogene in press, doi:.
    • A. Mitra, M.E. Menezes, L.K. Pannell, M.S. Mulekar, R.E. Honkanen, L.A. Shevde, R.S. Samant, DNAJB6 chaperones PP2A mediated dephosphorylation of GSK3beta to downregulate beta-catenin transcription target, osteopontin, Oncogene in press, doi:. http://doi:10.1038/onc.2011.623.
    • Mitra, A.1    Menezes, M.E.2    Pannell, L.K.3    Mulekar, M.S.4    Honkanen, R.E.5    Shevde, L.A.6    Samant, R.S.7
  • 15
    • 38349158107 scopus 로고    scopus 로고
    • Hsp40 facilitates nuclear import of the human immunodeficiency virus type 2 Vpx-mediated preintegration complex
    • Cheng X., Belshan M., Ratner L. Hsp40 facilitates nuclear import of the human immunodeficiency virus type 2 Vpx-mediated preintegration complex. J. Virol. 2008, 82:1229-1237.
    • (2008) J. Virol. , vol.82 , pp. 1229-1237
    • Cheng, X.1    Belshan, M.2    Ratner, L.3
  • 16
    • 77955287732 scopus 로고    scopus 로고
    • DNAJB6 induces degradation of beta-catenin and causes partial reversal of mesenchymal phenotype
    • Mitra A., Menezes M.E., Shevde L.A., Samant R.S. DNAJB6 induces degradation of beta-catenin and causes partial reversal of mesenchymal phenotype. J Biol Chem 2010, 285(32):24686-24694.
    • (2010) J Biol Chem , vol.285 , Issue.32 , pp. 24686-24694
    • Mitra, A.1    Menezes, M.E.2    Shevde, L.A.3    Samant, R.S.4
  • 17
    • 27644521346 scopus 로고    scopus 로고
    • The DnaJ-related factor Mrj interacts with nuclear factor of activated T cells c3 and mediates transcriptional repression through class II histone deacetylase recruitment
    • Dai Y.S., Xu J., Molkentin J.D. The DnaJ-related factor Mrj interacts with nuclear factor of activated T cells c3 and mediates transcriptional repression through class II histone deacetylase recruitment. Mol. Cell. Biol. 2005, 25:9936-9948.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 9936-9948
    • Dai, Y.S.1    Xu, J.2    Molkentin, J.D.3
  • 20
    • 33751265748 scopus 로고    scopus 로고
    • The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones
    • Qiu X.B., Shao Y.M., Miao S., Wang L. The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones. Cell. Mol. Life Sci. 2006, 63:2560-2570.
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 2560-2570
    • Qiu, X.B.1    Shao, Y.M.2    Miao, S.3    Wang, L.4
  • 21
    • 0031793127 scopus 로고    scopus 로고
    • Heat shock protein 70 kDa: molecular biology, biochemistry, and physiology
    • Kiang J.G., Tsokos G.C. Heat shock protein 70 kDa: molecular biology, biochemistry, and physiology. Pharmacol. Ther. 1998, 80:183-201.
    • (1998) Pharmacol. Ther. , vol.80 , pp. 183-201
    • Kiang, J.G.1    Tsokos, G.C.2
  • 22
    • 33845194459 scopus 로고    scopus 로고
    • Molecular cloning of the heat-shock cognate 70 (Hsc70) gene from the two-spotted spider mite, Tetranychus urticae, and its expression in response to heat shock and starvation
    • Shim J.K., Jung D.O., Park J.W., Kim D.W., Ha D.M., Lee K.Y. Molecular cloning of the heat-shock cognate 70 (Hsc70) gene from the two-spotted spider mite, Tetranychus urticae, and its expression in response to heat shock and starvation. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 2006, 145:288-295.
    • (2006) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.145 , pp. 288-295
    • Shim, J.K.1    Jung, D.O.2    Park, J.W.3    Kim, D.W.4    Ha, D.M.5    Lee, K.Y.6
  • 23
    • 37249020018 scopus 로고    scopus 로고
    • Nucleocytoplasmic trafficking of the molecular chaperone Hsp104 in unstressed and heat-shocked cells
    • Tkach J.M., Glover J.R. Nucleocytoplasmic trafficking of the molecular chaperone Hsp104 in unstressed and heat-shocked cells. Traffic 2008, 9:39-56.
    • (2008) Traffic , vol.9 , pp. 39-56
    • Tkach, J.M.1    Glover, J.R.2
  • 24
    • 38749099057 scopus 로고    scopus 로고
    • Physical and functional interaction of Runt-related protein 1 with hypoxia-inducible factor-1alpha
    • Peng Z.G., Zhou M.Y., Huang Y., Qiu J.H., Wang L.S., Liao S.H., Dong S., Chen G.Q. Physical and functional interaction of Runt-related protein 1 with hypoxia-inducible factor-1alpha. Oncogene 2008, 27:839-847.
    • (2008) Oncogene , vol.27 , pp. 839-847
    • Peng, Z.G.1    Zhou, M.Y.2    Huang, Y.3    Qiu, J.H.4    Wang, L.S.5    Liao, S.H.6    Dong, S.7    Chen, G.Q.8
  • 26
    • 0033587716 scopus 로고    scopus 로고
    • TID1, a human homolog of the Drosophila tumor suppressor l(2)tid, encodes two mitochondrial modulators of apoptosis with opposing functions
    • Syken J., De-Medina T., Munger K. TID1, a human homolog of the Drosophila tumor suppressor l(2)tid, encodes two mitochondrial modulators of apoptosis with opposing functions. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:8499-8504.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 8499-8504
    • Syken, J.1    De-Medina, T.2    Munger, K.3
  • 27
    • 14544290988 scopus 로고    scopus 로고
    • Constitutive nuclear import and stress-regulated nucleocytoplasmic shuttling of mammalian heat-shock factor 1
    • Vujanac M., Fenaroli A., Zimarino V. Constitutive nuclear import and stress-regulated nucleocytoplasmic shuttling of mammalian heat-shock factor 1. Traffic 2005, 6:214-229.
    • (2005) Traffic , vol.6 , pp. 214-229
    • Vujanac, M.1    Fenaroli, A.2    Zimarino, V.3
  • 28
    • 0033828673 scopus 로고    scopus 로고
    • Nuclear translocation and aggregate formation of heat shock cognate protein 70 (Hsc70) in oxidative stress and apoptosis
    • Dastoor Z., Dreyer J. Nuclear translocation and aggregate formation of heat shock cognate protein 70 (Hsc70) in oxidative stress and apoptosis. J. Cell Sci. 2000, 113(Pt 16):2845-2854.
    • (2000) J. Cell Sci. , vol.113 , Issue.PART 16 , pp. 2845-2854
    • Dastoor, Z.1    Dreyer, J.2
  • 29
    • 0032825496 scopus 로고    scopus 로고
    • The net repressor is regulated by nuclear export in response to anisomycin, UV, and heat shock
    • Ducret C., Maira S.M., Dierich A., Wasylyk B. The net repressor is regulated by nuclear export in response to anisomycin, UV, and heat shock. Mol. Cell. Biol. 1999, 19:7076-7087.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7076-7087
    • Ducret, C.1    Maira, S.M.2    Dierich, A.3    Wasylyk, B.4
  • 31
    • 48149098070 scopus 로고    scopus 로고
    • The Hsp40 family chaperone protein DnaJB6 enhances Schlafen1 nuclear localization which is critical for promotion of cell-cycle arrest in T-cells
    • Zhang Y., Yang Z., Cao Y., Zhang S., Li H., Huang Y., Ding Y.Q., Liu X. The Hsp40 family chaperone protein DnaJB6 enhances Schlafen1 nuclear localization which is critical for promotion of cell-cycle arrest in T-cells. Biochem. J. 2008, 413:239-250.
    • (2008) Biochem. J. , vol.413 , pp. 239-250
    • Zhang, Y.1    Yang, Z.2    Cao, Y.3    Zhang, S.4    Li, H.5    Huang, Y.6    Ding, Y.Q.7    Liu, X.8
  • 32
    • 3242725198 scopus 로고    scopus 로고
    • HIF activation by pH-dependent nucleolar sequestration of VHL
    • Mekhail K., Gunaratnam L., Bonicalzi M.E., Lee S. HIF activation by pH-dependent nucleolar sequestration of VHL. Nat. Cell Biol. 2004, 6:642-647.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 642-647
    • Mekhail, K.1    Gunaratnam, L.2    Bonicalzi, M.E.3    Lee, S.4
  • 33
    • 0344011603 scopus 로고    scopus 로고
    • Disruption of the nucleolus mediates stabilization of p53 in response to DNA damage and other stresses
    • Rubbi C.P., Milner J. Disruption of the nucleolus mediates stabilization of p53 in response to DNA damage and other stresses. EMBO J. 2003, 22:6068-6077.
    • (2003) EMBO J. , vol.22 , pp. 6068-6077
    • Rubbi, C.P.1    Milner, J.2
  • 34
    • 2342491487 scopus 로고    scopus 로고
    • Nucleolar protein NPM interacts with HDM2 and protects tumor suppressor protein p53 from HDM2-mediated degradation
    • Kurki S., Peltonen K., Latonen L., Kiviharju T.M., Ojala P.M., Meek D., Laiho M. Nucleolar protein NPM interacts with HDM2 and protects tumor suppressor protein p53 from HDM2-mediated degradation. Cancer Cell 2004, 5:465-475.
    • (2004) Cancer Cell , vol.5 , pp. 465-475
    • Kurki, S.1    Peltonen, K.2    Latonen, L.3    Kiviharju, T.M.4    Ojala, P.M.5    Meek, D.6    Laiho, M.7
  • 35
    • 0036315747 scopus 로고    scopus 로고
    • Stress-dependent nucleolin mobilization mediated by p53-nucleolin complex formation
    • Daniely Y., Dimitrova D.D., Borowiec J.A. Stress-dependent nucleolin mobilization mediated by p53-nucleolin complex formation. Mol. Cell. Biol. 2002, 22:6014-6022.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6014-6022
    • Daniely, Y.1    Dimitrova, D.D.2    Borowiec, J.A.3
  • 36
    • 78651476942 scopus 로고    scopus 로고
    • The Nucleolus Takes Control of Protein Trafficking Under Cellular Stress
    • Nalabothula N., Indig F.E., Carrier F. The Nucleolus Takes Control of Protein Trafficking Under Cellular Stress. Mol, Cell Pharmacol 2010, 2:203-212.
    • (2010) Mol, Cell Pharmacol , vol.2 , pp. 203-212
    • Nalabothula, N.1    Indig, F.E.2    Carrier, F.3
  • 37
    • 17444430871 scopus 로고    scopus 로고
    • The nucleolus as a stress sensor: JNK2 inactivates the transcription factor TIF-IA and down-regulates rRNA synthesis
    • Mayer C., Bierhoff H., Grummt I. The nucleolus as a stress sensor: JNK2 inactivates the transcription factor TIF-IA and down-regulates rRNA synthesis. Genes Dev. 2005, 19:933-941.
    • (2005) Genes Dev. , vol.19 , pp. 933-941
    • Mayer, C.1    Bierhoff, H.2    Grummt, I.3
  • 38
    • 25444473870 scopus 로고    scopus 로고
    • Cellular stress and nucleolar function
    • Mayer C., Grummt I. Cellular stress and nucleolar function. Cell Cycle 2005, 4:1036-1038.
    • (2005) Cell Cycle , vol.4 , pp. 1036-1038
    • Mayer, C.1    Grummt, I.2
  • 39
    • 58149379611 scopus 로고    scopus 로고
    • Activation of an endogenous suicide response after perturbation of rRNA synthesis leads to neurodegeneration in mice
    • Parlato R., Kreiner G., Erdmann G., Rieker C., Stotz S., Savenkova E., Berger S., Grummt I., Schutz G. Activation of an endogenous suicide response after perturbation of rRNA synthesis leads to neurodegeneration in mice. J. Neurosci. 2008, 28:12759-12764.
    • (2008) J. Neurosci. , vol.28 , pp. 12759-12764
    • Parlato, R.1    Kreiner, G.2    Erdmann, G.3    Rieker, C.4    Stotz, S.5    Savenkova, E.6    Berger, S.7    Grummt, I.8    Schutz, G.9
  • 42
    • 33846652552 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1alpha is a key regulator of metastasis in a transgenic model of cancer initiation and progression
    • Liao D., Corle C., Seagroves T.N., Johnson R.S. Hypoxia-inducible factor-1alpha is a key regulator of metastasis in a transgenic model of cancer initiation and progression. Cancer Res. 2007, 67:563-572.
    • (2007) Cancer Res. , vol.67 , pp. 563-572
    • Liao, D.1    Corle, C.2    Seagroves, T.N.3    Johnson, R.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.