메뉴 건너뛰기




Volumn 6, Issue 12, 2009, Pages 917-922

An auxin-based degron system for the rapid depletion of proteins in nonplant cells

Author keywords

[No Author keywords available]

Indexed keywords

AUXIN; GREEN FLUORESCENT PROTEIN; INDOLEACETIC ACID DERIVATIVE; PROTEIN; UBIQUITIN PROTEIN LIGASE;

EID: 73349085934     PISSN: 15487091     EISSN: 15491676     Source Type: Journal    
DOI: 10.1038/nmeth.1401     Document Type: Article
Times cited : (1128)

References (35)
  • 1
    • 0024041732 scopus 로고
    • Site-specifc DNA recombination in mammalian cells by the Cre recombinase of bacteriophage P1
    • Sauer, B. & Henderson, N. Site-specifc DNA recombination in mammalian cells by the Cre recombinase of bacteriophage P1. Proc. Natl. Acad. Sci. USA 85, 5166-5170 (1988).
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5166-5170
    • Sauer, B.1    Henderson, N.2
  • 2
    • 0026720075 scopus 로고
    • Tight control of gene expression in mammalian cells by tetracycline-responsive promoters
    • Gossen, M. & Bujard, H. Tight control of gene expression in mammalian cells by tetracycline-responsive promoters. Proc. Natl. Acad. Sci. USA 89, 5547-5551 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5547-5551
    • Gossen, M.1    Bujard, H.2
  • 3
    • 0035942736 scopus 로고    scopus 로고
    • Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
    • Elbashir, S.M. et al. Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411, 494-498 (2001).
    • (2001) Nature , vol.411 , pp. 494-498
    • Elbashir, S.M.1
  • 4
    • 0023789310 scopus 로고
    • A movable and regulable inactivation function within the steroid binding domain of the glucocorticoid receptor
    • Picard, D., Salser, S.J. & Yamamoto, K.R. A movable and regulable inactivation function within the steroid binding domain of the glucocorticoid receptor. Cell 54, 1073-1080 (1988).
    • (1988) Cell , vol.54 , pp. 1073-1080
    • Picard, D.1    Salser, S.J.2    Yamamoto, K.R.3
  • 5
    • 52049084405 scopus 로고    scopus 로고
    • The anchor-away technique: Rapid, conditional establishment of yeast mutant phenotypes
    • Haruki, H., Nishikawa, J. & Laemmli, U.K. The anchor-away technique: rapid, conditional establishment of yeast mutant phenotypes. Mol. Cell 31, 925-932 (2008).
    • (2008) Mol. Cell , vol.31 , pp. 925-932
    • Haruki, H.1    Nishikawa, J.2    Laemmli, U.K.3
  • 6
    • 0034581173 scopus 로고    scopus 로고
    • Posttranslational regulation of proteins by fusions to steroid-binding domains
    • Picard, D. Posttranslational regulation of proteins by fusions to steroid-binding domains. Methods Enzymol. 327, 385-401 (2000).
    • (2000) Methods Enzymol. , vol.327 , pp. 385-401
    • Picard, D.1
  • 7
    • 13444263620 scopus 로고    scopus 로고
    • Targeted protein degradation
    • Zhou, P. Targeted protein degradation. Curr. Opin. Chem. Biol. 9, 51-55 (2005).
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 51-55
    • Zhou, P.1
  • 8
    • 30744457822 scopus 로고    scopus 로고
    • Conditional control of protein function
    • Banaszynski, L.A. & Wandless, T.J. Conditional control of protein function. Chem. Biol. 13, 11-21 (2006).
    • (2006) Chem. Biol. , vol.13 , pp. 11-21
    • Banaszynski, L.A.1    Wandless, T.J.2
  • 9
    • 0029075876 scopus 로고
    • Redirecting the specifcity of ubiquitination by modifying ubiquitin-conjugating enzymes
    • Gosink, M.M. & Vierstra, R.D. Redirecting the specifcity of ubiquitination by modifying ubiquitin-conjugating enzymes. Proc. Natl. Acad. Sci. USA 92, 9117-9121 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9117-9121
    • Gosink, M.M.1    Vierstra, R.D.2
  • 10
    • 0033638333 scopus 로고    scopus 로고
    • Harnessing the ubiquitination machinery to target the degradation of specifc cellular proteins
    • Zhou, P., Bogacki, R., McReynolds, L. & Howley, P.M. Harnessing the ubiquitination machinery to target the degradation of specifc cellular proteins. Mol. Cell 6, 751-756 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 751-756
    • Zhou, P.1    Bogacki, R.2    McReynolds, L.3    Howley, P.M.4
  • 11
    • 0035902475 scopus 로고    scopus 로고
    • Protacs: Chimeric molecules that target proteins to the Skp1-Cullin-F box complex for ubiquitination and degradation
    • Sakamoto, K.M. et al. Protacs: chimeric molecules that target proteins to the Skp1-Cullin-F box complex for ubiquitination and degradation. Proc. Natl. Acad. Sci. USA 98, 8554-8559 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8554-8559
    • Sakamoto, K.M.1
  • 12
    • 1642343326 scopus 로고    scopus 로고
    • Chemical genetic control of protein levels: Selective in vivo targeted degradation
    • Schneekloth, J.S. Jr. et al. Chemical genetic control of protein levels: selective in vivo targeted degradation. J. Am. Chem. Soc. 126, 3748-3754 (2004).
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3748-3754
    • Schneekloth Jr., J.S.1
  • 13
    • 0344198598 scopus 로고    scopus 로고
    • Exploring the functional complexity of cellular proteins by protein knockout
    • Zhang, J., Zheng, N. & Zhou, P. Exploring the functional complexity of cellular proteins by protein knockout. Proc. Natl. Acad. Sci. USA 100, 14127-14132 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14127-14132
    • Zhang, J.1    Zheng, N.2    Zhou, P.3
  • 14
    • 0028213449 scopus 로고
    • Heat-inducible degron: A method for constructing temperature-sensitive mutants
    • Dohmen, R.J., Wu, P. & Varshavsky, A. Heat-inducible degron: a method for constructing temperature-sensitive mutants. Science 263, 1273-1276 (1994).
    • (1994) Science , vol.263 , pp. 1273-1276
    • Dohmen, R.J.1    Wu, P.2    Varshavsky, A.3
  • 15
    • 0034595448 scopus 로고    scopus 로고
    • Uninterrupted MCM2-7 function required for DNA replication fork progression
    • Labib, K., Tercero, J.A. & Diffey, J.F.X. Uninterrupted MCM2-7 function required for DNA replication fork progression. Science 288, 1643-1647 (2000).
    • (2000) Science , vol.288 , pp. 1643-1647
    • Labib, K.1    Tercero, J.A.2    Diffey, J.F.X.3
  • 16
    • 0038680253 scopus 로고    scopus 로고
    • Functional proteomic identifcation of DNA replication proteins by induced proteolysis in vivo
    • Kanemaki, M., Sanchez-Diaz, A., Gambus, A. & Labib, K. Functional proteomic identifcation of DNA replication proteins by induced proteolysis in vivo. Nature 423, 720-724 (2003).
    • (2003) Nature , vol.423 , pp. 720-724
    • Kanemaki, M.1    Sanchez-Diaz, A.2    Gambus, A.3    Labib, K.4
  • 17
    • 43149091910 scopus 로고    scopus 로고
    • Inn1 couples contraction of the actomyosin ring to membrane ingression during cytokinesis in budding yeast
    • Sanchez-Diaz, A. et al. Inn1 couples contraction of the actomyosin ring to membrane ingression during cytokinesis in budding yeast. Nat. Cell Biol. 10, 395-406 (2008).
    • (2008) Nat. Cell Biol. , vol.10 , pp. 395-406
    • Sanchez-Diaz, A.1
  • 18
    • 53549087771 scopus 로고    scopus 로고
    • Cell-cycle coordination between DNA replication and recombination revealed by a vertebrate N-end rule degron-Rad51
    • Su, X., Bernal, J.A. & Venkitaraman, A.R. Cell-cycle coordination between DNA replication and recombination revealed by a vertebrate N-end rule degron-Rad51. Nat. Struct. Mol. Biol. 15, 1049-1058 (2008).
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1049-1058
    • Su, X.1    Bernal, J.A.2    Venkitaraman, A.R.3
  • 19
    • 33748195107 scopus 로고    scopus 로고
    • A rapid, reversible, and tunable method to regulate protein function in living cells using synthetic small molecules
    • Banaszynski, L.A., Chen, L.C., Maynard-Smith, L.A., Ooi, A.G. & Wandless, T.J. A rapid, reversible, and tunable method to regulate protein function in living cells using synthetic small molecules. Cell 126, 995-1004 (2006).
    • (2006) Cell , vol.126 , pp. 995-1004
    • Banaszynski, L.A.1    Chen, L.C.2    Maynard-Smith, L.A.3    Ooi, A.G.4    Wandless, T.J.5
  • 21
    • 36749062385 scopus 로고    scopus 로고
    • Rapid control of protein level in the apicomplexan Toxoplasma gondii
    • Herm-Gotz, A. et al. Rapid control of protein level in the apicomplexan Toxoplasma gondii. Nat. Methods 4, 1003-1005 (2007).
    • (2007) Nat. Methods , vol.4 , pp. 1003-1005
    • Herm-Gotz, A.1
  • 22
    • 36749086400 scopus 로고    scopus 로고
    • An FKBP destabilization domain modulates protein levels in Plasmodium falciparum
    • Armstrong, C.M. & Goldberg, D.E. An FKBP destabilization domain modulates protein levels in Plasmodium falciparum. Nat. Methods 4, 1007-1009 (2007).
    • (2007) Nat. Methods , vol.4 , pp. 1007-1009
    • Armstrong, C.M.1    Goldberg, D.E.2
  • 23
    • 33750361422 scopus 로고    scopus 로고
    • Auxin in action: Signalling, transport and the control of plant growth and development
    • Teale, W.D., Paponov, I.A. & Palme, K. Auxin in action: signalling, transport and the control of plant growth and development. Nat. Rev. Mol. Cell Biol. 7, 847-859 (2006).
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 847-859
    • Teale, W.D.1    Paponov, I.A.2    Palme, K.3
  • 24
    • 0031975589 scopus 로고    scopus 로고
    • The TIR1 protein of Arabidopsis functions in auxin response and is related to human SKP2 and yeast grr1p
    • Ruegger, M. et al. The TIR1 protein of Arabidopsis functions in auxin response and is related to human SKP2 and yeast grr1p. Genes Dev. 12, 198-207 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 198-207
    • Ruegger, M.1
  • 25
    • 0033165998 scopus 로고    scopus 로고
    • Identifcation of an SCF ubiquitin-ligase complex required for auxin response in Arabidopsis thaliana
    • Gray, W.M. et al. Identifcation of an SCF ubiquitin-ligase complex required for auxin response in Arabidopsis thaliana. Genes Dev. 13, 1678-1691 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1678-1691
    • Gray, W.M.1
  • 26
    • 19544379019 scopus 로고    scopus 로고
    • The F-box protein TIR1 is an auxin receptor
    • Dharmasiri, N., Dharmasiri, S. & Estelle, M. The F-box protein TIR1 is an auxin receptor. Nature 435, 441-445 (2005).
    • (2005) Nature , vol.435 , pp. 441-445
    • Dharmasiri, N.1    Dharmasiri, S.2    Estelle, M.3
  • 27
    • 19544386804 scopus 로고    scopus 로고
    • The Arabidopsis F-box protein TIR1 is an auxin receptor
    • Kepinski, S. & Leyser, O. The Arabidopsis F-box protein TIR1 is an auxin receptor. Nature 435, 446-451 (2005).
    • (2005) Nature , vol.435 , pp. 446-451
    • Kepinski, S.1    Leyser, O.2
  • 28
    • 34247219263 scopus 로고    scopus 로고
    • Mechanism of auxin perception by the TIR1 ubiquitin ligase
    • Tan, X. et al. Mechanism of auxin perception by the TIR1 ubiquitin ligase. Nature 446, 640-645 (2007).
    • (2007) Nature , vol.446 , pp. 640-645
    • Tan, X.1
  • 29
    • 0030140041 scopus 로고    scopus 로고
    • Early genes and auxin action
    • Abel, S. & Theologis, A. Early genes and auxin action. Plant Physiol. 111, 9-17 (1996).
    • (1996) Plant Physiol. , vol.111 , pp. 9-17
    • Abel, S.1    Theologis, A.2
  • 30
    • 33646839060 scopus 로고    scopus 로고
    • The Arabidopsis Aux/IAA protein family has diversifed in degradation and auxin responsiveness
    • Dreher, K.A., Brown, J., Saw, R.E. & Callis, J. The Arabidopsis Aux/IAA protein family has diversifed in degradation and auxin responsiveness. Plant Cell 18, 699-714 (2006).
    • (2006) Plant Cell , vol.18 , pp. 699-714
    • Dreher, K.A.1    Brown, J.2    Saw, R.E.3    Callis, J.4
  • 31
    • 0034676443 scopus 로고    scopus 로고
    • Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex
    • Schulman, B.A. et al. Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex. Nature 408, 381-386 (2000).
    • (2000) Nature , vol.408 , pp. 381-386
    • Schulman, B.A.1
  • 32
    • 0033600872 scopus 로고    scopus 로고
    • Characterization of a novel kinetochore protein, CENP-H
    • Sugata, N., Munekata, E. & Todokoro, K. Characterization of a novel kinetochore protein, CENP-H. J. Biol. Chem. 274, 27343-27346 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 27343-27346
    • Sugata, N.1    Munekata, E.2    Todokoro, K.3
  • 33
    • 17944382377 scopus 로고    scopus 로고
    • CENP-H, a constitutive centromere component, is required for centromere targeting of CENP-C in vertebrate cells
    • Fukagawa, T. et al. CENP-H, a constitutive centromere component, is required for centromere targeting of CENP-C in vertebrate cells. EMBO J. 20, 4603-4617 (2001).
    • (2001) EMBO J. , vol.20 , pp. 4603-4617
    • Fukagawa, T.1
  • 34
    • 0032926333 scopus 로고    scopus 로고
    • Peroxidase-catalyzed effects of indole-3-acetic acid and analogues on lipid membranes, DNA, and mammalian cells in vitro
    • Folkes, L.K., Dennis, M.F., Stratford, M.R., Candeias, L.P. & Wardman, P. Peroxidase-catalyzed effects of indole-3-acetic acid and analogues on lipid membranes, DNA, and mammalian cells in vitro. Biochem. Pharmacol. 57, 375-382 (1999).
    • (1999) Biochem. Pharmacol. , vol.57 , pp. 375-382
    • Folkes, L.K.1    Dennis, M.F.2    Stratford, M.R.3    Candeias, L.P.4    Wardman, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.