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Volumn 287, Issue 12, 2012, Pages 8932-8943

Identification of a nuclear localization sequence in β-arrestin-1 and its functional implications

Author keywords

[No Author keywords available]

Indexed keywords

ARRESTINS; CELLULAR LOCALIZATION; CREB BINDING PROTEINS; GENE TRANSCRIPTIONS; MUTATIONAL ANALYSIS; NUCLEAR FACTORS; NUCLEAR IMPORT; NUCLEAR LOCALIZATION; NUCLEAR LOCALIZATION SEQUENCES; POST-TRANSLATIONAL MODIFICATIONS; SEQUENCE ANALYSIS; STRUCTURAL BASIS; TRANSCRIPTIONAL ACTIVITY; TRANSCRIPTIONAL REGULATION; TRANSFECTED CELLS; WILD TYPES; WILD-TYPE CONTROLS;

EID: 84858612683     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.294058     Document Type: Article
Times cited : (47)

References (50)
  • 1
    • 0023515309 scopus 로고
    • Functional desensitization of the isolated β-adrenergic receptor by the β-adrenergic receptor kinase. Potential role of an analog of the retinal protein arrestin (48-kDa protein)
    • Benovic, J. L., Kühn, H., Weyand, I., Codina, J., Caron, M. G., and Lefkowitz, R. J. (1987) Functional desensitization of the isolated β-adrenergic receptor by the β-adrenergic receptor kinase. Potential role of an analog of the retinal protein arrestin (48-kDa protein). Proc. Natl. Acad. Sci. U.S.A. 84, 8879-8882
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 8879-8882
    • Benovic, J.L.1    Kühn, H.2    Weyand, I.3    Codina, J.4    Caron, M.G.5    Lefkowitz, R.J.6
  • 2
    • 0025352299 scopus 로고
    • β-Arrestin. A protein that regulates β-adrenergic receptor function
    • Lohse, M. J., Benovic, J. L., Codina, J., Caron, M. G., and Lefkowitz, R. J. (1990) β-Arrestin. A protein that regulates β-adrenergic receptor function. Science 248, 1547-1550
    • (1990) Science , vol.248 , pp. 1547-1550
    • Lohse, M.J.1    Benovic, J.L.2    Codina, J.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 3
    • 0035903669 scopus 로고    scopus 로고
    • β-arrestin- and c-Src-dependent degradation of G-protein-coupled receptor kinase 2
    • DOI 10.1093/emboj/20.18.5129
    • Penela, P., Elorza, A., Sarnago, S., and Mayor, F., Jr. (2001) β-Arrestin- and c-Src-dependent degradation of G-protein-coupled receptor kinase 2. EMBO J. 20, 5129-5138 (Pubitemid 32910908)
    • (2001) EMBO Journal , vol.20 , Issue.18 , pp. 5129-5138
    • Penela, P.1    Elorza, A.2    Sarnago, S.3    Mayor Jr., F.4
  • 4
    • 0034646687 scopus 로고    scopus 로고
    • β-arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of β-arrestin1-dependent targeting of c-SRC in receptor endocytosis
    • DOI 10.1074/jbc.275.15.11312
    • Miller, W. E., Maudsley, S., Ahn, S., Khan, K. D., Luttrell, L. M., and Lefkowitz, R. J. (2000) β-Arrestin-1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of β-arrestin-1-dependent targeting of c-SRC in receptor endocytosis. J. Biol. Chem. 275, 11312-11319 (Pubitemid 30212780)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.15 , pp. 11312-11319
    • Miller, W.E.1    Maudsley, S.2    Ahn, S.3    Khan, K.D.4    Luttrell, L.M.5    Lefkowitz, R.J.6
  • 5
    • 0347695992 scopus 로고    scopus 로고
    • β-Arrestin1 Mediates Insulin-like Growth Factor 1 (IGF-1) Activation of Phosphatidylinositol 3-Kinase (PI3K) and Anti-apoptosis
    • DOI 10.1074/jbc.M309968200
    • Povsic, T. J., Kohout, T. A., and Lefkowitz, R. J. (2003) β-Arrestin-1 mediates insulin-like growth factor 1 (IGF-1) activation of phosphatidylinositol 3-kinase (PI3K) and anti-apoptosis. J. Biol. Chem. 278, 51334-51339 (Pubitemid 38020372)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.51 , pp. 51334-51339
    • Povsic, T.J.1    Kohout, T.A.2    Lefkowitz, R.J.3
  • 6
    • 22744449073 scopus 로고    scopus 로고
    • An Akt/β-arrestin 2/PP2A signaling complex mediates dopaminergic neurotransmission and behavior
    • DOI 10.1016/j.cell.2005.05.012, PII S0092867405004575
    • Beaulieu, J. M., Sotnikova, T. D., Marion, S., Lefkowitz, R. J., Gainetdinov, R. R., and Caron, M. G. (2005) An Akt·β-arrestin 2·PP2A signaling complex mediates dopaminergic neurotransmission and behavior. Cell 122, 261-273 (Pubitemid 41032989)
    • (2005) Cell , vol.122 , Issue.2 , pp. 261-273
    • Beaulieu, J.-M.1    Sotnikova, T.D.2    Marion, S.3    Lefkowitz, R.J.4    Gainetdinov, R.R.5    Caron, M.G.6
  • 7
    • 58249088830 scopus 로고    scopus 로고
    • β-Arrestin-1 interacts with the G-protein subunits β1γ2 and promotes β1γ2-dependent Akt signaling for NF-κB activation
    • Yang, M., He, R. L., Benovic, J. L., and Ye, R. D. (2009) β-Arrestin-1 interacts with the G-protein subunits β1γ2 and promotes β1γ2-dependent Akt signaling for NF-κB activation. Biochem. J. 417, 287-296
    • (2009) Biochem. J. , vol.417 , pp. 287-296
    • Yang, M.1    He, R.L.2    Benovic, J.L.3    Ye, R.D.4
  • 11
    • 74049094108 scopus 로고    scopus 로고
    • Arrestin orchestrates cross-talk between G protein-coupled receptors to modulate the spatiotemporal activation of ERK MAPK
    • Cervantes, D., Crosby, C., and Xiang, Y. (2010) Arrestin orchestrates cross-talk between G protein-coupled receptors to modulate the spatiotemporal activation of ERK MAPK. Circ. Res. 106, 79-88
    • (2010) Circ. Res. , vol.106 , pp. 79-88
    • Cervantes, D.1    Crosby, C.2    Xiang, Y.3
  • 12
    • 31344463886 scopus 로고    scopus 로고
    • Association of β-arrestin and TRAF6 negatively regulates Toll-like receptor-interleukin 1 receptor signaling
    • DOI 10.1038/ni1294, PII N1294
    • Wang, Y., Tang, Y., Teng, L., Wu, Y., Zhao, X., and Pei, G. (2006) Association of β-arrestin and TRAF6 negatively regulates Toll-like receptor-interleukin 1 receptor signaling. Nat. Immunol. 7, 139-147 (Pubitemid 43135879)
    • (2006) Nature Immunology , vol.7 , Issue.2 , pp. 139-147
    • Wang, Y.1    Tang, Y.2    Teng, L.3    Wu, Y.4    Zhao, X.5    Pei, G.6
  • 13
    • 33845960758 scopus 로고    scopus 로고
    • Arrestin-2 and G protein-coupled receptor kinase 5 interact with NFßB1 p105 and negatively regulate lipopolysaccharide-stimulated ERK1/2 activation in macrophages
    • DOI 10.1074/jbc.M605376200
    • Parameswaran, N., Pao, C. S., Leonhard, K. S., Kang, D. S., Kratz, M., Ley, S. C., and Benovic, J. L. (2006) Arrestin-2 and G protein-coupled receptor kinase 5 interact with NFßB1 p105 and negatively regulate lipopolysaccharide-stimulated ERK1/2 activation in macrophages. J. Biol. Chem. 281, 34159-34170 (Pubitemid 46036624)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.45 , pp. 34159-34170
    • Parameswaran, N.1    Pao, C.S.2    Leonhard, K.S.3    Dong, S.K.4    Kratz, M.5    Ley, S.C.6    Benovic, J.L.7
  • 15
    • 2342510314 scopus 로고    scopus 로고
    • Identification of β-arrestin2 as a G protein-coupled receptor-stimulated regulator of NF-κB pathways
    • DOI 10.1016/S1097-2765(04)00216-3, PII S1097276504002163
    • Gao, H., Sun, Y., Wu, Y., Luan, B., Wang, Y., Qu, B., and Pei, G. (2004) Identification of β-arrestin-2 as a G protein-coupled receptor-stimulated regulator of NF-κB pathways. Mol. Cell 14, 303-317 (Pubitemid 38591402)
    • (2004) Molecular Cell , vol.14 , Issue.3 , pp. 303-317
    • Gao, H.1    Sun, Y.2    Wu, Y.3    Luan, B.4    Wang, Y.5    Qu, B.6    Pei, G.7
  • 16
    • 0041341922 scopus 로고    scopus 로고
    • Requirement of Gβγ and c-Src in D2 dopamine receptor-mediated nuclear factor-κB activation
    • DOI 10.1124/mol.64.2.447
    • Yang, M., Zhang, H., Voyno-Yasenetskaya, T., and Ye, R. D. (2003) Requirement of Gβγ and c-Src in D2 dopamine receptor-mediated nuclear factor-κB activation. Mol. Pharmacol. 64, 447-455 (Pubitemid 36910009)
    • (2003) Molecular Pharmacology , vol.64 , Issue.2 , pp. 447-455
    • Yang, M.1    Zhang, H.2    Voyno-Yasenetskaya, T.3    Ye, R.D.4
  • 17
    • 55949084354 scopus 로고    scopus 로고
    • β-Arrestin-2 is required for lysophosphatidic acid-induced NF-κB activation
    • Sun, J., and Lin, X. (2008) β-Arrestin-2 is required for lysophosphatidic acid-induced NF-κB activation. Proc. Natl. Acad. Sci. U.S.A. 105, 17085-17090
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 17085-17090
    • Sun, J.1    Lin, X.2
  • 18
    • 28344452845 scopus 로고    scopus 로고
    • A nuclear function of β-arrestin1 in GPCR signaling: Regulation of histone acetylation and gene transcription
    • DOI 10.1016/j.cell.2005.09.011, PII S0092867405009645
    • Kang, J., Shi, Y., Xiang, B., Qu, B., Su, W., Zhu, M., Zhang, M., Bao, G., Wang, F., Zhang, X., Yang, R., Fan, F., Chen, X., Pei, G., and Ma, L. (2005) A nuclear function of β-arrestin-1 in GPCR signaling. Regulation of histone acetylation and gene transcription. Cell 123, 833-847 (Pubitemid 41721030)
    • (2005) Cell , vol.123 , Issue.5 , pp. 833-847
    • Kang, J.1    Shi, Y.2    Xiang, B.3    Qu, B.4    Su, W.5    Zhu, M.6    Zhang, M.7    Bao, G.8    Wang, F.9    Zhang, X.10    Yang, R.11    Fan, F.12    Chen, X.13    Pei, G.14    Ma, L.15
  • 19
    • 52649085868 scopus 로고    scopus 로고
    • Nuclear β-arrestin-1 functions as a scaffold for the dephosphorylation of STAT1 and moderates the antiviral activity of IFN-γ
    • Mo, W., Zhang, L., Yang, G., Zhai, J., Hu, Z., Chen, Y., Chen, X., Hui, L., Huang, R., and Hu, G. (2008) Nuclear β-arrestin-1 functions as a scaffold for the dephosphorylation of STAT1 and moderates the antiviral activity of IFN-γ. Mol. Cell 31, 695-707
    • (2008) Mol. Cell , vol.31 , pp. 695-707
    • Mo, W.1    Zhang, L.2    Yang, G.3    Zhai, J.4    Hu, Z.5    Chen, Y.6    Chen, X.7    Hui, L.8    Huang, R.9    Hu, G.10
  • 20
    • 0037020264 scopus 로고    scopus 로고
    • Differential nucleocytoplasmic shuttling of β-arrestins. Characterization of a leucine-rich nuclear export signal in β-arrestin-2
    • Scott, M. G., Le Rouzic, E., Périanin, A., Pierotti, V., Enslen, H., Benichou, S., Marullo, S., and Benmerah, A. (2002) Differential nucleocytoplasmic shuttling of β-arrestins. Characterization of a leucine-rich nuclear export signal in β-arrestin-2. J. Biol. Chem. 277, 37693-37701
    • (2002) J. Biol. Chem. , vol.277 , pp. 37693-37701
    • Scott, M.G.1    Le Rouzic, E.2    Périanin, A.3    Pierotti, V.4    Enslen, H.5    Benichou, S.6    Marullo, S.7    Benmerah, A.8
  • 21
    • 36749081534 scopus 로고    scopus 로고
    • Crossing the nuclear envelope: Hierarchical regulation of nucleocytoplasmic transport
    • DOI 10.1126/science.1142204
    • Terry, L. J., Shows, E. B., and Wente, S. R. (2007) Crossing the nuclear envelope. Hierarchical regulation of nucleocytoplasmic transport. Science 318, 1412-1416 (Pubitemid 350208921)
    • (2007) Science , vol.318 , Issue.5855 , pp. 1412-1416
    • Terry, L.J.1    Shows, E.B.2    Wente, S.R.3
  • 22
    • 0142149147 scopus 로고    scopus 로고
    • Dissection of the karyopherin alpha nuclear localization signal (NLS)-binding groove: Functional requirements for NLS binding
    • DOI 10.1074/jbc.M307162200
    • Leung, S. W., Harreman, M. T., Hodel, M. R., Hodel, A. E., and Corbett, A. H. (2003) Dissection of the karyopherin alpha nuclear localization signal (NLS)-binding groove. Functional requirements for NLS binding. J. Biol. Chem. 278, 41947-41953 (Pubitemid 37310457)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.43 , pp. 41947-41953
    • Leung, S.W.1    Harreman, M.T.2    Hodel, M.R.3    Hodel, A.E.4    Corbett, A.H.5
  • 23
    • 0033501039 scopus 로고    scopus 로고
    • Nucleocytoplasmic protein transport and recycling of Ran
    • DOI 10.1247/csf.24.425
    • Yoneda, Y., Hieda, M., Nagoshi, E., and Miyamoto, Y. (1999) Nucleocytoplasmic protein transport and recycling of Ran. Cell Struct. Funct. 24, 425-433 (Pubitemid 30128949)
    • (1999) Cell Structure and Function , vol.24 , Issue.6 , pp. 425-433
    • Yoneda, Y.1    Hieda, M.2    Nagoshi, E.3    Miyamoto, V.4
  • 24
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam, J. D., Lebovitz, R. M., and Roeder, R. G. (1983) Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11, 1475-1489
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 26
    • 0029909907 scopus 로고    scopus 로고
    • Bradykinin stimulates NF-κB activation and interleukin 1β gene expression in cultured human fibroblasts
    • Pan, Z. K., Zuraw, B. L., Lung, C. C., Prossnitz, E. R., Browning, D. D., and Ye, R. D. (1996) Bradykinin stimulates NF-κB activation and interleukin 1β gene expression in cultured human fibroblasts. J. Clin. Invest. 98, 2042-2049 (Pubitemid 26376292)
    • (1996) Journal of Clinical Investigation , vol.98 , Issue.9 , pp. 2042-2049
    • Pan, Z.K.1    Zuraw, B.L.2    Lung, C.-C.3    Prossnitz, E.R.4    Browning, D.D.5    Ye, R.D.6
  • 27
    • 0038514264 scopus 로고    scopus 로고
    • Subcellular localization of β-arrestins is determined by their intact N domain and the nuclear export signal at the C terminus
    • DOI 10.1074/jbc.M208109200
    • Wang, P., Wu, Y., Ge, X., Ma, L., and Pei, G. (2003) Subcellular localization of β-arrestins is determined by their intact N domain and the nuclear export signal at the C terminus. J. Biol. Chem. 278, 11648-11653 (Pubitemid 36792727)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.13 , pp. 11648-11653
    • Wang, P.1    Wu, Y.2    Ge, X.3    Ma, L.4    Pei, G.5
  • 28
    • 33847176295 scopus 로고    scopus 로고
    • Molecular mechanism of the nuclear protein import cycle
    • Stewart, M. (2007) Molecular mechanism of the nuclear protein import cycle. Nat. Rev. Mol. Cell Biol. 8, 195-208
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 195-208
    • Stewart, M.1
  • 29
    • 0029060051 scopus 로고
    • The nuclear pore complex
    • Davis, L. I. (1995) The nuclear pore complex. Annu. Rev. Biochem. 64, 865-896
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 865-896
    • Davis, L.I.1
  • 31
    • 0035979737 scopus 로고    scopus 로고
    • Duration of nuclear NF-κB action regulated by reversible acetylation
    • Chen, Lf., Fischle, W., Verdin, E., and Greene, W. C. (2001) Duration of nuclear NF-κB action regulated by reversible acetylation. Science 293, 1653-1657
    • (2001) Science , vol.293 , pp. 1653-1657
    • Chen, Lf.1    Fischle, W.2    Verdin, E.3    Greene, W.C.4
  • 32
    • 0037011056 scopus 로고    scopus 로고
    • Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-κB
    • DOI 10.1093/emboj/cdf660
    • Chen, L. F., Mu, Y., and Greene, W. C. (2002) Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-κB. EMBO J. 21, 6539-6548 (Pubitemid 35448431)
    • (2002) EMBO Journal , vol.21 , Issue.23 , pp. 6539-6548
    • Chen, L.-F.1    Mu, Y.2    Greene, W.C.3
  • 34
    • 0037451357 scopus 로고    scopus 로고
    • Transcriptional activation of the NF-κB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1)
    • DOI 10.1093/emboj/cdg139
    • Vermeulen, L., De Wilde, G., Van Damme, P., Vanden Berghe, W., and Haegeman, G. (2003) Transcriptional activation of the NF-κB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1). EMBO J. 22, 1313-1324 (Pubitemid 36362695)
    • (2003) EMBO Journal , vol.22 , Issue.6 , pp. 1313-1324
    • Vermeulen, L.1    De Wilde, G.2    Van Damme, P.3    Vanden, B.W.4    Haegeman, G.5
  • 35
    • 33645971047 scopus 로고    scopus 로고
    • Good cop, bad cop. The different faces of NF-κB
    • Perkins, N. D., and Gilmore, T. D. (2006) Good cop, bad cop. The different faces of NF-κB. Cell Death Differ. 13, 759-772
    • (2006) Cell Death Differ. , vol.13 , pp. 759-772
    • Perkins, N.D.1    Gilmore, T.D.2
  • 36
    • 0026078249 scopus 로고
    • Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: Identification of a class of bipartite nuclear targeting sequence
    • Robbins, J., Dilworth, S. M., Laskey, R. A., and 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 (Pubitemid 121002977)
    • (1991) Cell , vol.64 , Issue.3 , pp. 615-623
    • Robbins, J.1    Dilworth, S.M.2    Laskey, R.A.3    Dingwall, C.4
  • 37
    • 0034802172 scopus 로고    scopus 로고
    • Crystal structure of β-arrestin at 1.9 Å: Possible mechanism of receptor binding and membrane translocation
    • DOI 10.1016/S0969-2126(01)00644-X, PII S096921260100644X
    • Han, M., Gurevich, V. V., Vishnivetskiy, S. A., Sigler, P. B., and Schubert, C. (2001) Crystal structure of β-arrestin at 1.9 Å. Possible mechanism of receptor binding and membrane translocation. Structure 9, 869-880 (Pubitemid 32913504)
    • (2001) Structure , vol.9 , Issue.9 , pp. 869-880
    • Han, M.1    Gurevich, V.V.2    Vishnivetskiy, S.A.3    Sigler, P.B.4    Schubert, C.5
  • 38
    • 0034859839 scopus 로고    scopus 로고
    • Multiple pathways contribute to nuclear import of core histones
    • DOI 10.1093/embo-reports/kve168
    • Mühlhäusser, P., Müller, E. C., Otto, A., and Kutay, U. (2001) Multiple pathways contribute to nuclear import of core histones. EMBO Rep. 2, 690-696 (Pubitemid 32798711)
    • (2001) EMBO Reports , vol.2 , Issue.8 , pp. 690-696
    • Muhlhausser, P.1    Muller, E.-C.2    Otto, A.3    Kutay, U.4
  • 39
    • 4544352379 scopus 로고    scopus 로고
    • Characterization of karyopherin cargoes reveals unique mechanisms of Kap121p-mediated nuclear import
    • DOI 10.1128/MCB.24.19.8487-8503.2004
    • Leslie, D. M., Zhang, W., Timney, B. L., Chait, B. T., Rout, M. P., Wozniak, R. W., and Aitchison, J. D. (2004) Characterization of karyopherin cargoes reveals unique mechanisms of Kap121p-mediated nuclear import. Mol. Cell. Biol. 24, 8487-8503 (Pubitemid 39245071)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.19 , pp. 8487-8503
    • Leslie, D.M.1    Zhang, W.2    Timney, B.L.3    Chait, B.T.4    Rout, M.P.5    Wozniak, R.W.6    Aitchison, J.D.7
  • 40
    • 0024022449 scopus 로고
    • Identification of domains involved in nuclear uptake and histone binding of protein N1 of Xenopus laevis
    • Kleinschmidt, J. A., and Seiter, A. (1988) Identification of domains involved in nuclear uptake and histone binding of protein N1 of Xenopus laevis. EMBO J. 7, 1605-1614
    • (1988) EMBO J. , vol.7 , pp. 1605-1614
    • Kleinschmidt, J.A.1    Seiter, A.2
  • 41
    • 33646942810 scopus 로고    scopus 로고
    • Nonvisual arrestin oligomerization and cellular localization are regulated by inositol hexakisphosphate binding
    • DOI 10.1074/jbc.M512703200
    • Milano, S. K., Kim, Y. M., Stefano, F. P., Benovic, J. L., and Brenner, C. (2006) Nonvisual arrestin oligomerization and cellular localization are regulated by inositol hexakisphosphate binding. J. Biol. Chem. 281, 9812-9823 (Pubitemid 43864700)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.14 , pp. 9812-9823
    • Milano, S.K.1    Kim, Y.-M.2    Stefano, F.P.3    Benovic, J.L.4    Brenner, C.5
  • 42
    • 79551687952 scopus 로고    scopus 로고
    • Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual subtypes
    • Zhan, X., Gimenez, L. E., Gurevich, V. V., and Spiller, B. W. (2011) Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual subtypes. J. Mol. Biol. 406, 467-478
    • (2011) J. Mol. Biol. , vol.406 , pp. 467-478
    • Zhan, X.1    Gimenez, L.E.2    Gurevich, V.V.3    Spiller, B.W.4
  • 43
  • 44
    • 33746351059 scopus 로고    scopus 로고
    • Visual and both non-visual arrestins in their "inactive" conformation bind JNK3 and Mdm2 and relocalize them from the nucleus to the cytoplasm
    • DOI 10.1074/jbc.M603659200
    • Song, X., Raman, D., Gurevich, E. V., Vishnivetskiy, S. A., and Gurevich, V. V. (2006) Visual and both non-visual arrestins in their "inactive" conformation bind JNK3 and Mdm2 and relocalize them from the nucleus to the cytoplasm. J. Biol. Chem. 281, 21491-21499 (Pubitemid 44115487)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.30 , pp. 21491-21499
    • Song, X.1    Raman, D.2    Gurevich, E.V.3    Vishnivetskiy, S.A.4    Gurevich, V.V.5
  • 45
    • 0021269089 scopus 로고
    • Sequence requirements for nuclear location of simian virus 40 large-T antigen
    • Kalderon, D., Richardson, W. D., Markham, A. F., and Smith, A. E. (1984) Sequence requirements for nuclear location of simian virus 40 large-T antigen. Nature 311, 33-38 (Pubitemid 14065276)
    • (1984) Nature , vol.311 , Issue.5981 , pp. 33-38
    • Kalderon, D.1    Richardson, W.D.2    Markham, A.F.3    Smith, A.E.4
  • 46
    • 0026551292 scopus 로고
    • Nuclear translocation of viral Jun but not of cellular Jun is cell cycle dependent
    • Chida, K., and Vogt, P. K. (1992) Nuclear translocation of viral Jun but not of cellular Jun is cell cycle dependent. Proc. Natl. Acad. Sci. U.S.A. 89, 4290-4294
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 4290-4294
    • Chida, K.1    Vogt, P.K.2
  • 47
    • 0037073722 scopus 로고    scopus 로고
    • Nuclear translocation of Plk1 mediated by its bipartite nuclear localization signal
    • DOI 10.1074/jbc.M206307200
    • Taniguchi, E., Toyoshima-Morimoto, F., and Nishida, E. (2002) Nuclear translocation of plk1 mediated by its bipartite nuclear localization signal. J. Biol. Chem. 277, 48884-48888 (Pubitemid 35470857)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.50 , pp. 48884-48888
    • Taniguchi, E.1    Toyoshima-Morimoto, F.2    Nishida, E.3
  • 48
    • 30544452321 scopus 로고    scopus 로고
    • Identification of a functional bipartite nuclear localization signal in the tumor suppressor parafibromin
    • DOI 10.1038/sj.onc.1208778, PII 1208778
    • Hahn, M. A., and Marsh, D. J. (2005) Identification of a functional bipartite nuclear localization signal in the tumor suppressor parafibromin. Oncogene 24, 6241-6248 (Pubitemid 43080047)
    • (2005) Oncogene , vol.24 , Issue.41 , pp. 6241-6248
    • Hahn, M.A.1    Marsh, D.J.2
  • 49
    • 33746776838 scopus 로고    scopus 로고
    • Rules for Nuclear Localization Sequence Recognition by Karyopherinβ2
    • DOI 10.1016/j.cell.2006.05.049, PII S009286740600910X
    • Lee, B. J., Cansizoglu, A. E., Süel, K. E., Louis, T. H., Zhang, Z., and Chook, Y. M. (2006) Rules for nuclear localization sequence recognition by karyopherin β2. Cell 126, 543-558 (Pubitemid 44163605)
    • (2006) Cell , vol.126 , Issue.3 , pp. 543-558
    • Lee, B.J.1    Cansizoglu, A.E.2    Suel, K.E.3    Louis, T.H.4    Zhang, Z.5    Chook, Y.M.6
  • 50
    • 0033527576 scopus 로고    scopus 로고
    • The human tap nuclear RNA export factor contains a novel transportin-dependent nuclear localization signal that lacks nuclear export signal function
    • Truant, R., Kang, Y., and Cullen, B. R. (1999) The human tap nuclear RNA export factor contains a novel transportin-dependent nuclear localization signal that lacks nuclear export signal function. J. Biol. Chem. 274, 32167-32171
    • (1999) J. Biol. Chem. , vol.274 , pp. 32167-32171
    • Truant, R.1    Kang, Y.2    Cullen, B.R.3


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