메뉴 건너뛰기




Volumn 13, Issue 8, 1999, Pages 935-945

Control of the nuclear localization of Extradenticle by competing nuclear import and export signals

Author keywords

Drosophila; Extradenticle; Homothorax; Nuclear localization

Indexed keywords

ARTICLE; CELLULAR DISTRIBUTION; DROSOPHILA; NONHUMAN; NUCLEAR LOCALIZATION SIGNAL; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN LOCALIZATION; SIGNAL TRANSDUCTION;

EID: 0344436081     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.13.8.935     Document Type: Article
Times cited : (200)

References (46)
  • 1
    • 0031793140 scopus 로고    scopus 로고
    • Generation of multiple antagonistic domains along the proximodistal axis during Drosophila leg development
    • Abu-Shaar, M. and R.S. Mann. 1998. Generation of multiple antagonistic domains along the proximodistal axis during Drosophila leg development. Development 125: 3821-3830.
    • (1998) Development , vol.125 , pp. 3821-3830
    • Abu-Shaar, M.1    Mann, R.S.2
  • 2
    • 0031043928 scopus 로고    scopus 로고
    • Nucleocytoplasmic localisation of extradenticle protein is spatially regulated throughout development in Drosophila
    • Aspland, S.E. and R.A. White. 1997. Nucleocytoplasmic localisation of extradenticle protein is spatially regulated throughout development in Drosophila. Development 124: 741-747.
    • (1997) Development , vol.124 , pp. 741-747
    • Aspland, S.E.1    White, R.A.2
  • 3
    • 0026509949 scopus 로고
    • NF-kappa B and related proteins: Rel/dorsal homologies meet ankyrin-like repeats
    • Blank, V., P. Kourilsky, and A. Israel. 1992. NF-kappa B and related proteins: Rel/dorsal homologies meet ankyrin-like repeats. Trends Biochem. Sci. 17: 135-140.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 135-140
    • Blank, V.1    Kourilsky, P.2    Israel, A.3
  • 4
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand, A. and N. Perrimon. 1993. Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development 118: 401-415.
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.1    Perrimon, N.2
  • 5
    • 0032575492 scopus 로고    scopus 로고
    • The cAMP-dependent protein kinase site (Ser312) enhances dorsal nuclear import through facilitating nuclear localization sequence/importin interaction
    • Briggs, L.J., D. Stein, J. Goltz, V.C. Corrigan, A. Efthymiadis, S. Hubner, and D.A. Jans. 1998. The cAMP-dependent protein kinase site (Ser312) enhances dorsal nuclear import through facilitating nuclear localization sequence/importin interaction. J. Biol. Chem. 273: 22745-22752.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22745-22752
    • Briggs, L.J.1    Stein, D.2    Goltz, J.3    Corrigan, V.C.4    Efthymiadis, A.5    Hubner, S.6    Jans, D.A.7
  • 6
    • 0026906639 scopus 로고
    • New motif in PBX genes
    • Burglin, T.R. and G. Ruvkun. 1992. New motif in PBX genes. Nat. Genet. 1: 319-320.
    • (1992) Nat. Genet. , vol.1 , pp. 319-320
    • Burglin, T.R.1    Ruvkun, G.2
  • 7
    • 0032537066 scopus 로고    scopus 로고
    • Control of antennal versus leg development in Drosophila
    • Casares, F. and R.S. Mann. 1998. Control of antennal versus leg development in Drosophila. Nature 392: 723-726.
    • (1998) Nature , vol.392 , pp. 723-726
    • Casares, F.1    Mann, R.S.2
  • 8
    • 0030813558 scopus 로고    scopus 로고
    • Meis proteins are major in vivo DNA binding partners for wild-type but not chimeric Pbx proteins
    • Chang, C.P., Y. Jacobs, T. Nakamura, N.A. Jenkins, N.G. Copeland, and M.L. Cleary. 1997. Meis proteins are major in vivo DNA binding partners for wild-type but not chimeric Pbx proteins. Mol. Cell. Biol. 17: 5679-5687.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5679-5687
    • Chang, C.P.1    Jacobs, Y.2    Nakamura, T.3    Jenkins, N.A.4    Copeland, N.G.5    Cleary, M.L.6
  • 9
    • 0031712371 scopus 로고    scopus 로고
    • BMPs, Smads and metalloproteases: Extracellular and intracellular modes of negative regulation
    • Cho, K.W. and I.L. Blitz. 1998. BMPs, Smads and metalloproteases: Extracellular and intracellular modes of negative regulation. Curr. Opin. Genet. Dev. 8: 443-449.
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 443-449
    • Cho, K.W.1    Blitz, I.L.2
  • 10
    • 0025949412 scopus 로고
    • Nuclear targeting sequences - A consensus?
    • Dingwall, C. and R.A. Laskey. 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
  • 11
    • 0029130169 scopus 로고
    • The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs
    • Fischer, U., J. Huber, W.C. Boelens, I.W. Mattaj, and R. Luhrmann. 1995. The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell 82: 475-483.
    • (1995) Cell , vol.82 , pp. 475-483
    • Fischer, U.1    Huber, J.2    Boelens, W.C.3    Mattaj, I.W.4    Luhrmann, R.5
  • 12
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod, M., M. Ohno, M. Yoshida, and I.W. Mattaj. 1997. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 90: 1051-1060.
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 13
    • 0030831534 scopus 로고    scopus 로고
    • CRM1 is responsible for intracellular transport mediated by the nuclear export signal
    • Fukuda, M., S. Asano, T. Nakamura, M. Adachi, M. Yoshida, M. Yanagida, and E. Nishida. 1997. CRM1 is responsible for intracellular transport mediated by the nuclear export signal. Nature 390: 308-311.
    • (1997) Nature , vol.390 , pp. 308-311
    • Fukuda, M.1    Asano, S.2    Nakamura, T.3    Adachi, M.4    Yoshida, M.5    Yanagida, M.6    Nishida, E.7
  • 14
    • 0028176570 scopus 로고
    • Dorsal, a Drosophila Rel-like protein, is phosphorylated upon activation of the transmembrane protein Toll
    • Gillespie, S.K. and S.A. Wasserman. 1994. Dorsal, a Drosophila Rel-like protein, is phosphorylated upon activation of the transmembrane protein Toll. Mol. Cell. Biol. 14: 3559-3568.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3559-3568
    • Gillespie, S.K.1    Wasserman, S.A.2
  • 15
    • 0030468935 scopus 로고    scopus 로고
    • Genetic evidence for the subdivision of the arthropod limb into coxopodite and telopodite
    • Gonzalez-Crespo, S. and G. Morata. 1996. Genetic evidence for the subdivision of the arthropod limb into coxopodite and telopodite. Development 122: 3921-3928.
    • (1996) Development , vol.122 , pp. 3921-3928
    • Gonzalez-Crespo, S.1    Morata, G.2
  • 16
  • 17
    • 0032191341 scopus 로고    scopus 로고
    • STAT structure and function in signaling
    • Hoey, T. and U. Schindler. 1998. STAT structure and function in signaling. Curr. Opin. Genet. Dev. 8: 582-587.
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 582-587
    • Hoey, T.1    Schindler, U.2
  • 19
    • 0025919717 scopus 로고
    • p34cdc2-mediated phosphorylation at T124 inhibits nuclear import of SV-40 T antigen proteins
    • Jans, D.A., M.J. Ackermann, J.R. Bischoff, D.H. Beach, and R. Peters. 1991. p34cdc2-mediated phosphorylation at T124 inhibits nuclear import of SV-40 T antigen proteins. J. Cell. Biol. 115: 1203-1212.
    • (1991) J. Cell. Biol. , vol.115 , pp. 1203-1212
    • Jans, D.A.1    Ackermann, M.J.2    Bischoff, J.R.3    Beach, D.H.4    Peters, R.5
  • 20
    • 0032563319 scopus 로고    scopus 로고
    • Degradation signal masking by heterodimerization of MATα2 and MATa1 blocks their mutual destruction by the ubiquitin-proteasome pathway
    • Johnson, P.R., R. Swanson, L. Rakhilina, and M. Hochstrasser. 1998. Degradation signal masking by heterodimerization of MATα2 and MATa1 blocks their mutual destruction by the ubiquitin-proteasome pathway. Cell 94: 217-227.
    • (1998) Cell , vol.94 , pp. 217-227
    • Johnson, P.R.1    Swanson, R.2    Rakhilina, L.3    Hochstrasser, M.4
  • 21
    • 0025137176 scopus 로고
    • A new homeobox gene contributes the DNA binding domain of the t(1:19) translocation protein in pre-B ALL
    • Kamps, M.P., C. Murre, X.-h. Sun, and D. Baltimore. 1990. A new homeobox gene contributes the DNA binding domain of the t(1:19) translocation protein in pre-B ALL. Cell 60: 547-555.
    • (1990) Cell , vol.60 , pp. 547-555
    • Kamps, M.P.1    Murre, C.2    X-H, S.3    Baltimore, D.4
  • 22
    • 0031446339 scopus 로고    scopus 로고
    • Meis1 and pKnox1 bind DNA cooperatively with Pbx1 utilizing an interaction surface disrupted in oncoprotein E2a-Pbx1
    • Knoepfler, P., K. Calvo, H. Chen, S. Antonarakis, and M. Kamps. 1997. Meis1 and pKnox1 bind DNA cooperatively with Pbx1 utilizing an interaction surface disrupted in oncoprotein E2a-Pbx1. Proc. Natl. Acad. Sci. 94: 14553-14558.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 14553-14558
    • Knoepfler, P.1    Calvo, K.2    Chen, H.3    Antonarakis, S.4    Kamps, M.5
  • 24
    • 0031940786 scopus 로고    scopus 로고
    • Dorsotonals/homothorax, the Drosophila homologue of meis1, interacts with extradenticle in patterning of the embryonic PNS
    • Kurant, E., C.-Y. Pai, R. Sharf, N. Halachmi, Y. Sun, and A. Salzberg. 1998. dorsotonals/homothorax, the Drosophila homologue of meis1, interacts with extradenticle in patterning of the embryonic PNS. Development 125: 1037-1048.
    • (1998) Development , vol.125 , pp. 1037-1048
    • Kurant, E.1    Pai, C.-Y.2    Sharf, R.3    Halachmi, N.4    Sun, Y.5    Salzberg, A.6
  • 25
    • 0031028382 scopus 로고    scopus 로고
    • Nuclear localization of cyclin B1 mediates its biological activity and is regulated by phosphorylation
    • Li, J., A.N. Meyer, and D.J. Donoghue. 1997. Nuclear localization of cyclin B1 mediates its biological activity and is regulated by phosphorylation. Proc. Natl. Acad. Sci. 94: 502-507.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 502-507
    • Li, J.1    Meyer, A.N.2    Donoghue, D.J.3
  • 26
    • 0029955433 scopus 로고    scopus 로고
    • Nuclear import of the homeodomain protein Extradenticle in response to Decapentaplegic and Wingless signalling
    • Mann, R. and M. Abu-Shaar. 1996. Nuclear import of the homeodomain protein Extradenticle in response to Decapentaplegic and Wingless signalling. Nature 383: 630-633.
    • (1996) Nature , vol.383 , pp. 630-633
    • Mann, R.1    Abu-Shaar, M.2
  • 28
    • 0028151047 scopus 로고
    • Dachshund encodes a nuclear protein required for normal eye and leg development in Drosophila
    • Mardon, G., N.M. Solomon, and G.M. Rubin. 1994. dachshund encodes a nuclear protein required for normal eye and leg development in Drosophila. Development 120: 3473-3486.
    • (1994) Development , vol.120 , pp. 3473-3486
    • Mardon, G.1    Solomon, N.M.2    Rubin, G.M.3
  • 29
  • 30
    • 0025064238 scopus 로고
    • Chromosomal translocation t(1: 19) results in synthesis of a homeobox fusion mRNA that codes for a potential chimeric transcription factor
    • Nourse, J., J. Mellentin, N. Galili, J. Wilkinson, E. Stanbridge, S. Smith, and M. Cleary. 1990. Chromosomal translocation t(1: 19) results in synthesis of a homeobox fusion mRNA that codes for a potential chimeric transcription factor. Cell 60: 535-545.
    • (1990) Cell , vol.60 , pp. 535-545
    • Nourse, J.1    Mellentin, J.2    Galili, N.3    Wilkinson, J.4    Stanbridge, E.5    Smith, S.6    Cleary, M.7
  • 31
    • 0030748907 scopus 로고    scopus 로고
    • Evidence for a role of CRM1 in signal-mediated nuclear protein export
    • Ossareh-Nazari, B., F. Bachelerie, and C. Dargemont. 1997. Evidence for a role of CRM1 in signal-mediated nuclear protein export. Science 278: 141-144.
    • (1997) Science , vol.278 , pp. 141-144
    • Ossareh-Nazari, B.1    Bachelerie, F.2    Dargemont, C.3
  • 32
    • 0031818290 scopus 로고    scopus 로고
    • Leptomycin B inhibits equine infectious anemia virus Rev and feline immunodeficiency virus rev function but not the function of the hepatitis B virus posttranscriptional regulatory element
    • Otero, G.C., M.E. Harris, J.E. Donello, and T.J. Hope. 1998. Leptomycin B inhibits equine infectious anemia virus Rev and feline immunodeficiency virus rev function but not the function of the hepatitis B virus posttranscriptional regulatory element. J. Virol. 72: 7593-7597.
    • (1998) J. Virol. , vol.72 , pp. 7593-7597
    • Otero, G.C.1    Harris, M.E.2    Donello, J.E.3    Hope, T.J.4
  • 33
    • 0032006566 scopus 로고    scopus 로고
    • The Homothorax homeoprotein activates the nuclear localization of another homeoprotein, extradenticle, and suppresses eye development in Drosophila
    • Pai, C.-Y., T. Kuo, T. Jaw, E. Kurant, C. Chen, D. Bessarab, A. Salzberg, and Y. Sun. 1998. The Homothorax homeoprotein activates the nuclear localization of another homeoprotein, extradenticle, and suppresses eye development in Drosophila. Genes & Dev. 12: 435-446.
    • (1998) Genes & Dev. , vol.12 , pp. 435-446
    • Pai, C.-Y.1    Kuo, T.2    Jaw, T.3    Kurant, E.4    Chen, C.5    Bessarab, D.6    Salzberg, A.7    Sun, Y.8
  • 34
    • 0025365228 scopus 로고
    • Mutations in the Drosophila gene extradenticle affect the way specific homeo domain proteins regulate segmental identity
    • Peifer, M. and E. Wieschaus. 1990. Mutations in the Drosophila gene extradenticle affect the way specific homeo domain proteins regulate segmental identity. Genes & Dev. 4: 1209-1223.
    • (1990) Genes & Dev. , vol.4 , pp. 1209-1223
    • Peifer, M.1    Wieschaus, E.2
  • 35
    • 0032053727 scopus 로고    scopus 로고
    • Regulation of E2F4 mitogenic activity during terminal differentiation by its heterodimerization partners for nuclear translocation
    • Puri, P.L., L. Cimino, M. Fulco, C. Zimmerman, N.B. La Thangue, A. Giordano, A. Graessmann, and M. Levrero. 1998. Regulation of E2F4 mitogenic activity during terminal differentiation by its heterodimerization partners for nuclear translocation. Cancer Res. 58: 1325-1331.
    • (1998) Cancer Res. , vol.58 , pp. 1325-1331
    • Puri, P.L.1    Cimino, L.2    Fulco, M.3    Zimmerman, C.4    La Thangue, N.B.5    Giordano, A.6    Graessmann, A.7    Levrero, M.8
  • 36
    • 0027519720 scopus 로고
    • extradenticle, a regulator of homeotic gene activity, is a homolog of the homeobox-containing human proto-oncogene pbx1
    • Rauskolb, C., M. Peifer, and E. Wieschaus. 1993. extradenticle, a regulator of homeotic gene activity, is a homolog of the homeobox-containing human proto-oncogene pbx1. Cell 74: 1-20.
    • (1993) Cell , vol.74 , pp. 1-20
    • Rauskolb, C.1    Peifer, M.2    Wieschaus, E.3
  • 37
    • 0025853591 scopus 로고
    • Individual stripe regulatory elements in the Drosophila hairy promoter respond to maternal, gap, and pair-rule genes
    • Riddihough, G. and D. Ish-Horowicz. 1991. Individual stripe regulatory elements in the Drosophila hairy promoter respond to maternal, gap, and pair-rule genes. Genes & Dev. 5: 840-854.
    • (1991) Genes & Dev. , vol.5 , pp. 840-854
    • Riddihough, G.1    Ish-Horowicz, D.2
  • 38
    • 0030725941 scopus 로고    scopus 로고
    • Nuclear translocation of Extradenticle requires homothorax, which encodes an Extradenticle-related homeodomain protein
    • Rieckhof, G., F. Casares, H.D. Ryoo, M. Abu-Shaar, and R.S. Mann. 1997. Nuclear translocation of Extradenticle requires homothorax, which encodes an Extradenticle-related homeodomain protein. Cell 91: 171-183.
    • (1997) Cell , vol.91 , pp. 171-183
    • Rieckhof, G.1    Casares, F.2    Ryoo, H.D.3    Abu-Shaar, M.4    Mann, R.S.5
  • 39
    • 0026026630 scopus 로고
    • The rate of nuclear cytoplasmic protein transport is determined by the casein kinase II site flanking the nuclear localization sequence of the SV40 T-antigen
    • Rihs, H.P., D.A. Jans, H. Fan, and R. Peters. 1991. The rate of nuclear cytoplasmic protein transport is determined by the casein kinase II site flanking the nuclear localization sequence of the SV40 T-antigen. EMBO J. 10: 633-639.
    • (1991) EMBO J. , vol.10 , pp. 633-639
    • Rihs, H.P.1    Jans, D.A.2    Fan, H.3    Peters, R.4
  • 40
    • 0025931225 scopus 로고
    • A conserved family of nuclear phosphoproteins localized to sites of polymerase II transcription
    • Roth, M.B., A.M. Zahler, and J.A. Stolk. 1991. A conserved family of nuclear phosphoproteins localized to sites of polymerase II transcription. J. Cell Biol. 115: 587-596.
    • (1991) J. Cell Biol. , vol.115 , pp. 587-596
    • Roth, M.B.1    Zahler, A.M.2    Stolk, J.A.3
  • 41
    • 0029761681 scopus 로고    scopus 로고
    • Role of kinases and the phosphatase calcineurin in the nuclear shuttling of transcription factor NF-AT4
    • Shibasaki, F., E.R. Price, D. Milan, and F. McKeon. 1996. Role of kinases and the phosphatase calcineurin in the nuclear shuttling of transcription factor NF-AT4. Nature 382: 370-373.
    • (1996) Nature , vol.382 , pp. 370-373
    • Shibasaki, F.1    Price, E.R.2    Milan, D.3    McKeon, F.4
  • 42
    • 0030985459 scopus 로고    scopus 로고
    • Exportin 1 (Crm1p) is an essential nuclear export factor
    • Stade, K., C.S. Ford, C. Guthrie, and K. Weis. 1997. Exportin 1 (Crm1p) is an essential nuclear export factor. Cell 90: 1041-1050.
    • (1997) Cell , vol.90 , pp. 1041-1050
    • Stade, K.1    Ford, C.S.2    Guthrie, C.3    Weis, K.4
  • 44
    • 0029851762 scopus 로고    scopus 로고
    • Rapid shuttling of NF-AT in discrimination of Ca2+ signals and immunosuppression
    • Timmerman, L.A., N.A. Clipstone, S.N. Ho, J.P. Northrop, and G.R. Crabtree. 1996. Rapid shuttling of NF-AT in discrimination of Ca2+ signals and immunosuppression. Nature 383: 837-840.
    • (1996) Nature , vol.383 , pp. 837-840
    • Timmerman, L.A.1    Clipstone, N.A.2    Ho, S.N.3    Northrop, J.P.4    Crabtree, G.R.5
  • 45
    • 0029130168 scopus 로고
    • Identification of a signal for rapid export of proteins from the nucleus
    • Wen, W., J.L. Meinkoth, R.Y. Tsien, and S.S. Taylor. 1995. Identification of a signal for rapid export of proteins from the nucleus. Cell 82: 463-473.
    • (1995) Cell , vol.82 , pp. 463-473
    • Wen, W.1    Meinkoth, J.L.2    Tsien, R.Y.3    Taylor, S.S.4
  • 46
    • 0032955485 scopus 로고    scopus 로고
    • Proximodistal axis formation in the Drosophila leg: Subdivision into proximal and distal domains by Homothorax and Distal-less
    • Wu, J. and S.M. Cohen. 1999. Proximodistal axis formation in the Drosophila leg: Subdivision into proximal and distal domains by Homothorax and Distal-less. Development 126: 109-117.
    • (1999) Development , vol.126 , pp. 109-117
    • Wu, J.1    Cohen, S.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.