메뉴 건너뛰기




Volumn 273, Issue 2, 2006, Pages 315-324

The monopartite nuclear localization signal of autoimmune regulator mediates its nuclear import and interaction with multiple importin α molecules

Author keywords

Autoimmune regulator (AIRE); Importin ; Karyopherin ; Nuclear import

Indexed keywords

AUTOIMMUNE REGULATOR PROTEIN; KARYOPHERIN ALPHA;

EID: 33645037895     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.05065.x     Document Type: Article
Times cited : (27)

References (53)
  • 1
    • 0021807826 scopus 로고
    • Autoimmune polyendocrinopathy-candidiasis- ectodermal dystrophy (APECED): Autosomal recessive inheritance
    • Ahonen P 1985 Autoimmune polyendocrinopathy-candidiasis- ectodermal dystrophy (APECED): autosomal recessive inheritance Clin Genet 27 535 542
    • (1985) Clin Genet , vol.27 , pp. 535-542
    • Ahonen, P.1
  • 2
    • 0025295238 scopus 로고
    • Clinical variation of autoimmune polyendocrinopathy-candidiasis- ectodermal dystrophy (APECED) in a series of 68 patients
    • Ahonen P Myllärniemi S Sipilä I Perheentupa J 1990 Clinical variation of autoimmune polyendocrinopathy-candidiasis-ectodermal dystrophy (APECED) in a series of 68 patients N Engl J Med 322 1829 1836
    • (1990) N Engl J Med , vol.322 , pp. 1829-1836
    • Ahonen, P.1    Myllärniemi, S.2    Sipilä, I.3    Perheentupa, J.4
  • 3
    • 0346599403 scopus 로고    scopus 로고
    • An autoimmune disease, APECED, caused by mutations in a novel gene featuring two PHD-type zinc-finger domains. the Finnish-German APECED Consortium. Autoimmune Polyendocrinopathy-Candidiasis-Ectodermal Dystrophy
    • Consortium TF-GA 1997 An autoimmune disease, APECED, caused by mutations in a novel gene featuring two PHD-type zinc-finger domains. The Finnish-German APECED Consortium. Autoimmune Polyendocrinopathy-Candidiasis-Ectodermal Dystrophy Nat Genet 17 399 403
    • (1997) Nat Genet , vol.17 , pp. 399-403
    • Tf-Ga, C.1
  • 5
    • 0036081840 scopus 로고    scopus 로고
    • APS-I/APECED: The clinical disease and therapy
    • vi
    • Perheentupa J 2002 APS-I/APECED: the clinical disease and therapy Endocrinol Metab Clin North Am 31 295 320 vi
    • (2002) Endocrinol Metab Clin North Am , vol.31 , pp. 295-320
    • Perheentupa, J.1
  • 6
    • 0032127876 scopus 로고    scopus 로고
    • The APECED polyglandular autoimmune syndrome protein, AIRE-1, contains the SAND domain and is probably a transcription factor
    • Gibson TJ Ramu C Gemünd C Aasland R 1998 The APECED polyglandular autoimmune syndrome protein, AIRE-1, contains the SAND domain and is probably a transcription factor Trends Biochem Sci 23 242 244
    • (1998) Trends Biochem Sci , vol.23 , pp. 242-244
    • Gibson, T.J.1    Ramu, C.2    Gemünd, C.3    Aasland, R.4
  • 8
    • 0035374352 scopus 로고    scopus 로고
    • Subcellular localization of the autoimmune regulator protein: Characterization of nuclear targeting and transcriptional activation domain
    • Pitkänen J Vahamurto P Krohn K Peterson P 2001 Subcellular localization of the autoimmune regulator protein: characterization of nuclear targeting and transcriptional activation domain J Biol Chem 276 19597 19602
    • (2001) J Biol Chem , vol.276 , pp. 19597-19602
    • Pitkänen, J.1    Vahamurto, P.2    Krohn, K.3    Peterson, P.4
  • 14
    • 0034662906 scopus 로고    scopus 로고
    • Normal thymic architecture and negative selection are associated with Aire expression, the gene defective in the autoimmune-polyendocrinopathy- candidiasis-ectodermal dystrophy (APECED)
    • Zuklys S Balciunaite G Agarwal A Fasler-Kan E Palmer E Holländer GA 2000 Normal thymic architecture and negative selection are associated with Aire expression, the gene defective in the autoimmune-polyendocrinopathy-candidiasis- ectodermal dystrophy (APECED) J Immunol 165 1976 1983
    • (2000) J Immunol , vol.165 , pp. 1976-1983
    • Zuklys, S.1    Balciunaite, G.2    Agarwal, A.3    Fasler-Kan, E.4    Palmer, E.5    Holländer, G.A.6
  • 15
    • 0023900635 scopus 로고
    • Tolerance in T-cell-receptor transgenic mice involves deletion of nonmature CD4+8+ thymocytes
    • Kisielow P Bluthmann H Staerz UD Steinmetz M von Boehmer H 1988 Tolerance in T-cell-receptor transgenic mice involves deletion of nonmature CD4+8+ thymocytes Nature 333 742 746
    • (1988) Nature , vol.333 , pp. 742-746
    • Kisielow, P.1    Bluthmann, H.2    Staerz, U.D.3    Steinmetz, M.4    Von Boehmer, H.5
  • 16
    • 0029005494 scopus 로고
    • Mechanisms of immune tolerance induction through the thymic expression of a peripheral tissue-specific protein
    • Antonia SJ Geiger T Miller J Flavell RA 1995 Mechanisms of immune tolerance induction through the thymic expression of a peripheral tissue-specific protein Int Immunol 7 715 725
    • (1995) Int Immunol , vol.7 , pp. 715-725
    • Antonia, S.J.1    Geiger, T.2    Miller, J.3    Flavell, R.A.4
  • 17
    • 7044220808 scopus 로고    scopus 로고
    • Regulating self-tolerance by deregulating gene expression
    • Gotter J Kyewski B 2004 Regulating self-tolerance by deregulating gene expression Curr Opin Immunol 16 741 745
    • (2004) Curr Opin Immunol , vol.16 , pp. 741-745
    • Gotter, J.1    Kyewski, B.2
  • 22
    • 0032924111 scopus 로고    scopus 로고
    • AIRE encodes a nuclear protein co-localizing with cytoskeletal filaments: Altered sub-cellular distribution of mutants lacking the PHD zinc fingers
    • Rinderle C Christensen HM Schweiger S Lehrach H Yaspo ML 1999 AIRE encodes a nuclear protein co-localizing with cytoskeletal filaments: altered sub-cellular distribution of mutants lacking the PHD zinc fingers Hum Mol Genet 8 277 290
    • (1999) Hum Mol Genet , vol.8 , pp. 277-290
    • Rinderle, C.1    Christensen, H.M.2    Schweiger, S.3    Lehrach, H.4    Yaspo, M.L.5
  • 23
    • 14544299215 scopus 로고    scopus 로고
    • Mechanisms of receptor-mediated nuclear import and nuclear export
    • Pemberton LF Paschal BM 2005 Mechanisms of receptor-mediated nuclear import and nuclear export Traffic 6 187 198
    • (2005) Traffic , vol.6 , pp. 187-198
    • Pemberton, L.F.1    Paschal, B.M.2
  • 24
    • 0021269089 scopus 로고
    • Sequence requirements for nuclear location of simian virus 40 large-T antigen
    • Kalderon D Richardson WD Markham AF Smith AE 1984 Sequence requirements for nuclear location of simian virus 40 large-T antigen Nature 311 33 38
    • (1984) Nature , vol.311 , pp. 33-38
    • Kalderon, D.1    Richardson, W.D.2    Markham, A.F.3    Smith, A.E.4
  • 25
    • 0025949412 scopus 로고
    • Nuclear targeting sequences - A consensus?
    • Dingwall C Laskey RA 1991 Nuclear targeting sequences - a consensus? Trends Biochem Sci 16 478 481
    • (1991) Trends Biochem Sci , vol.16 , pp. 478-481
    • Dingwall, C.1    Laskey, R.A.2
  • 26
    • 0026078249 scopus 로고
    • Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: Identification of a class of bipartite nuclear targeting sequence
    • Robbins J Dilworth SM Laskey RA Dingwall C 1991 Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: identification of a class of bipartite nuclear targeting sequence Cell 64 615 623
    • (1991) Cell , vol.64 , pp. 615-623
    • Robbins, J.1    Dilworth, S.M.2    Laskey, R.A.3    Dingwall, C.4
  • 32
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Görlich D Kutay U 1999 Transport between the cell nucleus and the cytoplasm Annu Rev Cell Dev Biol 15 607 660
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 607-660
    • Görlich, D.1    Kutay, U.2
  • 33
    • 0027994484 scopus 로고
    • RAG-1 interacts with the repeated amino acid motif of the human homologue of the yeast protein SRP1
    • Cortes P Ye ZS Baltimore D 1994 RAG-1 interacts with the repeated amino acid motif of the human homologue of the yeast protein SRP1 Proc Natl Acad Sci USA 91 7633 7637
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7633-7637
    • Cortes, P.1    Ye, Z.S.2    Baltimore, D.3
  • 34
    • 0028239241 scopus 로고
    • Rch1, a protein that specifically interacts with the RAG-1 recombination-activating protein
    • Cuomo CA Kirch SA Gyuris J Brent R Oettinger MA 1994 Rch1, a protein that specifically interacts with the RAG-1 recombination-activating protein Proc Natl Acad Sci USA 91 6156 6160
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6156-6160
    • Cuomo, C.A.1    Kirch, S.A.2    Gyuris, J.3    Brent, R.4    Oettinger, M.A.5
  • 35
    • 0043034223 scopus 로고    scopus 로고
    • Cloning of two novel human importin-alpha subunits and analysis of the expression pattern of the importin-alpha protein family
    • Köhler M Ansieau S Prehn S Leutz A Haller H Hartmann E 1997 Cloning of two novel human importin-alpha subunits and analysis of the expression pattern of the importin-alpha protein family EJB Lett 417 104 108
    • (1997) EJB Lett , vol.417 , pp. 104-108
    • Köhler, M.1    Ansieau, S.2    Prehn, S.3    Leutz, A.4    Haller, H.5    Hartmann, E.6
  • 36
    • 0030994992 scopus 로고    scopus 로고
    • Cloning of a cDNA encoding a novel importin-alpha homologue, Qip1: Discrimination of Qip1 and Rch1 from hSrp1 by their ability to interact with DNA helicase Q1/RecQL
    • Seki T Tada S Katada T Enomoto T 1997 Cloning of a cDNA encoding a novel importin-alpha homologue, Qip1: discrimination of Qip1 and Rch1 from hSrp1 by their ability to interact with DNA helicase Q1/RecQL Biochem Biophys Res Commun 234 48 53
    • (1997) Biochem Biophys Res Commun , vol.234 , pp. 48-53
    • Seki, T.1    Tada, S.2    Katada, T.3    Enomoto, T.4
  • 38
    • 0041344551 scopus 로고    scopus 로고
    • Importin alpha nuclear localization signal binding sites for STAT1, STAT2, and influenza a virus nucleoprotein
    • Melén K Fagerlund R Franke J Köhler M Kinnunen L Julkunen I 2003 Importin alpha nuclear localization signal binding sites for STAT1, STAT2, and influenza A virus nucleoprotein J Biol Chem 278 28193 28200
    • (2003) J Biol Chem , vol.278 , pp. 28193-28200
    • Melén, K.1    Fagerlund, R.2    Franke, J.3    Köhler, M.4    Kinnunen, L.5    Julkunen, I.6
  • 39
    • 0031882574 scopus 로고    scopus 로고
    • Cloning and characterization of hSRP1 gamma, a tissue-specific nuclear transport factor
    • Nachury MV Ryder UW Lamond AI Weis K 1998 Cloning and characterization of hSRP1 gamma, a tissue-specific nuclear transport factor Proc Natl Acad Sci USA 95 582 587
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 582-587
    • Nachury, M.V.1    Ryder, U.W.2    Lamond, A.I.3    Weis, K.4
  • 40
    • 8644276304 scopus 로고    scopus 로고
    • In vivo analysis of importin alpha proteins reveals cellular proliferation inhibition and substrate specificity
    • Quensel C Friedrich B Sommer T Hartmann E Köhler M 2004 In vivo analysis of importin alpha proteins reveals cellular proliferation inhibition and substrate specificity Mol Cell Biol 24 10246 10255
    • (2004) Mol Cell Biol , vol.24 , pp. 10246-10255
    • Quensel, C.1    Friedrich, B.2    Sommer, T.3    Hartmann, E.4    Köhler, M.5
  • 41
    • 19044367766 scopus 로고    scopus 로고
    • Arginine/lysine-rich nuclear localization signals mediate interactions between dimeric STATs and importin alpha 5
    • Fagerlund R Melén K Kinnunen L Julkunen I 2002 Arginine/lysine-rich nuclear localization signals mediate interactions between dimeric STATs and importin alpha 5 J Biol Chem 277 30072 30078
    • (2002) J Biol Chem , vol.277 , pp. 30072-30078
    • Fagerlund, R.1    Melén, K.2    Kinnunen, L.3    Julkunen, I.4
  • 42
    • 18144426719 scopus 로고    scopus 로고
    • NF-{kappa}B is transported into the nucleus by importin {alpha}3 and importin {alpha}4
    • Fagerlund R Kinnunen L Köhler M Julkunen I Melén K 2005 NF-{kappa}B is transported into the nucleus by importin {alpha}3 and importin {alpha}4 J Biol Chem 280 15942 15951
    • (2005) J Biol Chem , vol.280 , pp. 15942-15951
    • Fagerlund, R.1    Kinnunen, L.2    Köhler, M.3    Julkunen, I.4    Melén, K.5
  • 43
    • 0029921174 scopus 로고    scopus 로고
    • A 41 amino acid motif in importin-alpha confers binding to importin-beta and hence transit into the nucleus
    • Görlich D Henklein P Laskey RA Hartmann E 1996 A 41 amino acid motif in importin-alpha confers binding to importin-beta and hence transit into the nucleus EMBO J 15 1810 1817
    • (1996) EMBO J , vol.15 , pp. 1810-1817
    • Görlich, D.1    Henklein, P.2    Laskey, R.A.3    Hartmann, E.4
  • 44
    • 0028266975 scopus 로고
    • A repeating amino acid motif shared by proteins with diverse cellular roles
    • Peifer M Berg S Reynolds AB 1994 A repeating amino acid motif shared by proteins with diverse cellular roles Cell 76 789 791
    • (1994) Cell , vol.76 , pp. 789-791
    • Peifer, M.1    Berg, S.2    Reynolds, A.B.3
  • 45
    • 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 1998 Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha Cell 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
  • 46
    • 0034653375 scopus 로고    scopus 로고
    • Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin alpha
    • Conti E Kuriyan J 2000 Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin alpha Struct Fold Des 8 329 338
    • (2000) Struct Fold des , vol.8 , pp. 329-338
    • Conti, E.1    Kuriyan, J.2
  • 47
    • 0034646565 scopus 로고    scopus 로고
    • Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-alpha
    • Fontes MR Teh T Kobe B 2000 Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-alpha J Mol Biol 297 1183 1194
    • (2000) J Mol Biol , vol.297 , pp. 1183-1194
    • Fontes, M.R.1    Teh, T.2    Kobe, B.3
  • 48
    • 0033841253 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of transcription factors
    • Cartwright P Helin K 2000 Nucleocytoplasmic shuttling of transcription factors Cell Mol Life Sci 57 1193 1206
    • (2000) Cell Mol Life Sci , vol.57 , pp. 1193-1206
    • Cartwright, P.1    Helin, K.2
  • 49
    • 0346157329 scopus 로고    scopus 로고
    • The ins and outs of transcriptional control: Nucleocytoplasmic shuttling in development and disease
    • Smith JM Koopman PA 2004 The ins and outs of transcriptional control: nucleocytoplasmic shuttling in development and disease Trends Genet 20 4 8
    • (2004) Trends Genet , vol.20 , pp. 4-8
    • Smith, J.M.1    Koopman, P.A.2
  • 51
    • 0032956197 scopus 로고    scopus 로고
    • Design of conditionally active STATs: Insights into STAT activation and gene regulatory function
    • Milocco LH Haslam JA Rosen J Seidel HM 1999 Design of conditionally active STATs: insights into STAT activation and gene regulatory function Mol Cell Biol 19 2913 2920
    • (1999) Mol Cell Biol , vol.19 , pp. 2913-2920
    • Milocco, L.H.1    Haslam, J.A.2    Rosen, J.3    Seidel, H.M.4
  • 52
    • 0025268284 scopus 로고
    • SV-poly: A versatile mammalian expression vector
    • Stacey A Schnieke A 1990 SV-poly: a versatile mammalian expression vector Nucleic Acids Res 18 2829
    • (1990) Nucleic Acids Res , vol.18 , pp. 2829
    • Stacey, A.1    Schnieke, A.2
  • 53
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK
    • Laemmli UK 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 680 685
    • (1970) Nature , vol.227 , pp. 680-685


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.