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Volumn 7, Issue , 2016, Pages

Pironetin reacts covalently with cysteine-316 of α-tubulin to destabilize microtubule

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TUBULIN; ANTINEOPLASTIC AGENT; BETA TUBULIN; BETA2 TUBULIN; COLCHICINE; CYSTEINE; LACTONE DERIVATIVE; NATURAL PRODUCT; PIRONETIN; TUBULIN; UNCLASSIFIED DRUG; VINBLASTINE; PYRONE DERIVATIVE;

EID: 84977097910     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms12103     Document Type: Article
Times cited : (98)

References (42)
  • 1
    • 70349580048 scopus 로고    scopus 로고
    • Molecular Biology of the Cell
    • Alberts, B. et al. Molecular Biology of the Cell (Garland Science, 2008)
    • (2008) Garland Science
    • Alberts, B.1
  • 2
    • 77957374075 scopus 로고    scopus 로고
    • Microtubule-binding agents: A dynamic field of cancer therapeutics
    • Dumontet, C. & Jordan, M. A. Microtubule-binding agents: a dynamic field of cancer therapeutics. Nat. Rev. Drug Discov. 9, 790-803 (2010)
    • (2010) Nat. Rev. Drug Discov , vol.9 , pp. 790-803
    • Dumontet, C.1    Jordan, M.A.2
  • 3
    • 0015520389 scopus 로고
    • Maytansine, a novel antileukemic ansa macrolide from Maytenus ovatus
    • Kupchan, S. M. et al. Maytansine, a novel antileukemic ansa macrolide from Maytenus ovatus. J. Am. Chem. Soc. 94, 1354-1356 (1972)
    • (1972) J. Am. Chem. Soc , vol.94 , pp. 1354-1356
    • Kupchan, S.M.1
  • 4
    • 77649191871 scopus 로고    scopus 로고
    • Microtubules and resistance to tubulin-binding agents
    • Kavallaris, M. Microtubules and resistance to tubulin-binding agents. Nat. Rev. Cancer 10, 194-204 (2010)
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 194-204
    • Kavallaris, M.1
  • 5
    • 0029063397 scopus 로고
    • Structure of tubulin at 6.5 and location of the taxol-binding site
    • Nogales, E., Wolf, S. G., Khan, I. A., Luduena, R. F. & Downing, K. H. Structure of tubulin at 6.5 and location of the taxol-binding site. Nature 375, 424-427 (1995)
    • (1995) Nature , vol.375 , pp. 424-427
    • Nogales, E.1    Wolf, S.G.2    Khan, I.A.3    Luduena, R.F.4    Downing, K.H.5
  • 6
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of alpha betatubulin at 3.5A resolution
    • Lowe, J., Li, H., Downing, K. H. & Nogales, E. Refined structure of alpha betatubulin at 3.5A resolution. J. Mol. Biol. 313, 1045-1057 (2001)
    • (2001) J. Mol. Biol , vol.313 , pp. 1045-1057
    • Lowe, J.1    Li, H.2    Downing, K.H.3    Nogales, E.4
  • 7
    • 1642401199 scopus 로고    scopus 로고
    • Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain
    • Ravelli, R. B. et al. Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. Nature 428, 198-202 (2004)
    • (2004) Nature , vol.428 , pp. 198-202
    • Ravelli, R.B.1
  • 8
    • 19544393159 scopus 로고    scopus 로고
    • Structural basis for the regulation of tubulin by vinblastine
    • Gigant, B. et al. Structural basis for the regulation of tubulin by vinblastine. Nature 435, 519-522 (2005)
    • (2005) Nature , vol.435 , pp. 519-522
    • Gigant, B.1
  • 9
    • 84873090491 scopus 로고    scopus 로고
    • Molecular mechanism of action of microtubule-stabilizing anticancer agents
    • Prota, A. E. et al. Molecular mechanism of action of microtubule-stabilizing anticancer agents. Science 339, 587-590 (2013)
    • (2013) Science , vol.339 , pp. 587-590
    • Prota, A.E.1
  • 10
    • 84907270556 scopus 로고    scopus 로고
    • A new tubulin-binding site and pharmacophore for microtubule-destabilizing anticancer drugs
    • Prota, A. E. et al. A new tubulin-binding site and pharmacophore for microtubule-destabilizing anticancer drugs. Proc. Natl Acad. Sci. USA 111, 13817-13821 (2014)
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 13817-13821
    • Prota, A.E.1
  • 11
    • 84893516156 scopus 로고    scopus 로고
    • Structural basis of microtubule stabilization by laulimalide and peloruside A
    • Prota, A. E. et al. Structural basis of microtubule stabilization by laulimalide and peloruside A. Angew. Chem. Int. Ed. 53, 1621-1625 (2014)
    • (2014) Angew. Chem. Int. Ed , vol.53 , pp. 1621-1625
    • Prota, A.E.1
  • 12
    • 79953299183 scopus 로고    scopus 로고
    • Drugs that target dynamic microtubules: A new molecular perspective
    • Stanton, R. A., Gernert, K. M., Nettles, J. H. & Aneja, R. Drugs that target dynamic microtubules: a new molecular perspective. Med. Res. Rev. 31, 443-481 (2011)
    • (2011) Med. Res. Rev , vol.31 , pp. 443-481
    • Stanton, R.A.1    Gernert, K.M.2    Nettles, J.H.3    Aneja, R.4
  • 13
    • 84861488421 scopus 로고    scopus 로고
    • Modifications on the basic skeletons of vinblastine and vincristine
    • Keglevich, P., Hazai, L., Kalaus, G. & Szantay, C. Modifications on the basic skeletons of vinblastine and vincristine. Molecules 17, 5893-5914 (2012)
    • (2012) Molecules , vol.17 , pp. 5893-5914
    • Keglevich, P.1    Hazai, L.2    Kalaus, G.3    Szantay, C.4
  • 14
    • 84885457038 scopus 로고    scopus 로고
    • Potent vinblastine C20 ureas displaying additionally improved activity against a vinblastineresistant cancer cell line
    • Barker, T. J., Duncan, K. K., Otrubova, K. & Boger, D. L. Potent vinblastine C20 ureas displaying additionally improved activity against a vinblastineresistant cancer cell line. ACS Med. Chem. Lett. 4, 985-988 (2013)
    • (2013) ACS Med. Chem. Lett , vol.4 , pp. 985-988
    • Barker, T.J.1    Duncan, K.K.2    Otrubova, K.3    Boger, D.L.4
  • 15
    • 38549161093 scopus 로고    scopus 로고
    • Is class III beta-tubulin a predictive factor in patients receiving tubulin-binding agents?
    • Seve, P. & Dumontet, C. Is class III beta-tubulin a predictive factor in patients receiving tubulin-binding agents? Lancet Oncol. 9, 168-175 (2008)
    • (2008) Lancet Oncol , vol.9 , pp. 168-175
    • Seve, P.1    Dumontet, C.2
  • 17
    • 0029996440 scopus 로고    scopus 로고
    • Chemical modification of PA-48153C, a novel immunosuppressant isolated from Streptomyces prunicolor PA-48153
    • Yasui, K. et al. Chemical modification of PA-48153C, a novel immunosuppressant isolated from Streptomyces prunicolor PA-48153. J. Antibiot. (Tokyo) 49, 173-180 (1996)
    • (1996) J. Antibiot. (Tokyo) , vol.49 , pp. 173-180
    • Yasui, K.1
  • 18
    • 84938422247 scopus 로고    scopus 로고
    • The mechanism of the interactions of pironetin analog/combretastatin A-4 hybrids with tubulin
    • Torijano-Gutierrez, S. et al. The mechanism of the interactions of pironetin analog/combretastatin A-4 hybrids with tubulin. Arch. Pharm. (Weinheim) 348, 541-547 (2015)
    • (2015) Arch. Pharm. (Weinheim) , vol.348 , pp. 541-547
    • Torijano-Gutierrez, S.1
  • 19
    • 0344653657 scopus 로고    scopus 로고
    • Cell cycle arrest and antitumor activity of pironetin and its derivatives
    • Kondoh, M. et al. Cell cycle arrest and antitumor activity of pironetin and its derivatives. Cancer Lett. 126, 29-32 (1998)
    • (1998) Cancer Lett , vol.126 , pp. 29-32
    • Kondoh, M.1
  • 20
    • 34247112846 scopus 로고    scopus 로고
    • Antiproliferating activity of the mitotic inhibitor pironetin against vindesine- and paclitaxel-resistant human small cell lung cancer H69 cells
    • Yoshida, M. et al. Antiproliferating activity of the mitotic inhibitor pironetin against vindesine- and paclitaxel-resistant human small cell lung cancer H69 cells. Anticancer Res. 27, 729-736 (2007)
    • (2007) Anticancer Res , vol.27 , pp. 729-736
    • Yoshida, M.1
  • 21
    • 0033152543 scopus 로고    scopus 로고
    • Apoptosis induction via microtubule disassembly by an antitumour compound, pironetin
    • Kondoh, M., Usui, T., Nishikiori, T., Mayumi, T. & Osada, H. Apoptosis induction via microtubule disassembly by an antitumour compound, pironetin. Biochem. J. 340 Pt 2 411-416 (1999)
    • (1999) Biochem. J. 340 Pt , vol.2 , pp. 411-416
    • Kondoh, M.1    Usui, T.2    Nishikiori, T.3    Mayumi, T.4    Osada, H.5
  • 22
    • 3042686764 scopus 로고    scopus 로고
    • The anticancer natural product pironetin selectively targets Lys352 of alpha-tubulin
    • Usui, T. et al. The anticancer natural product pironetin selectively targets Lys352 of alpha-tubulin. Chem. Biol. 11, 799-806 (2004)
    • (2004) Chem. Biol , vol.11 , pp. 799-806
    • Usui, T.1
  • 24
    • 84882331938 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of truncated alpha-tubulinbinding pironetin analogues lacking alkyl pendants in the side chain or the dihydropyrone ring
    • Panos, J. et al. Synthesis and biological evaluation of truncated alpha-tubulinbinding pironetin analogues lacking alkyl pendants in the side chain or the dihydropyrone ring. Org. Biomol. Chem. 11, 5809-5826 (2013)
    • (2013) Org. Biomol. Chem , vol.11 , pp. 5809-5826
    • Panos, J.1
  • 25
    • 79953199726 scopus 로고    scopus 로고
    • Design and synthesis of pironetin analogues with simplified structure and study of their interactions with microtubules
    • Marco, J. A. et al. Design and synthesis of pironetin analogues with simplified structure and study of their interactions with microtubules. Eur. J. Med. Chem. 46, 1630-1637 (2011)
    • (2011) Eur. J. Med. Chem , vol.46 , pp. 1630-1637
    • Marco, J.A.1
  • 26
    • 0034121816 scopus 로고    scopus 로고
    • Synthesis of pironetin and related analogs: Studies on structure-activity relationships as tubulin assembly inhibitors
    • Watanabe, H. et al. Synthesis of pironetin and related analogs: studies on structure-activity relationships as tubulin assembly inhibitors. J. Antibiot. (Tokyo) 53, 540-545 (2000)
    • (2000) J. Antibiot. (Tokyo) , vol.53 , pp. 540-545
    • Watanabe, H.1
  • 27
    • 84860390007 scopus 로고    scopus 로고
    • The determinants that govern microtubule assembly from the atomic structure of GTP-tubulin
    • Nawrotek, A., Knossow, M. & Gigant, B. The determinants that govern microtubule assembly from the atomic structure of GTP-tubulin. J. Mol. Biol. 412, 35-42 (2011)
    • (2011) J. Mol. Biol , vol.412 , pp. 35-42
    • Nawrotek, A.1    Knossow, M.2    Gigant, B.3
  • 28
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: A tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr
    • Schuttelkopf, A. W. & van Aalten, D. M. PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr. D Biol. Crystallogr. 60, 1355-1363 (2004)
    • (2004) D Biol. Crystallogr , vol.60 , pp. 1355-1363
    • Schuttelkopf, A.W.1    Van Aalten, D.M.2
  • 29
    • 34548675565 scopus 로고    scopus 로고
    • Insight into the GTPase activity of tubulin from complexes with stathmin-like domains
    • Wang, C., Cormier, A., Gigant, B. & Knossow, M. Insight into the GTPase activity of tubulin from complexes with stathmin-like domains. Biochemistry 46, 10595-10602 (2007)
    • (2007) Biochemistry , vol.46 , pp. 10595-10602
    • Wang, C.1    Cormier, A.2    Gigant, B.3    Knossow, M.4
  • 30
  • 31
    • 84897109910 scopus 로고    scopus 로고
    • The novel microtubule-destabilizing drug BAL27862 binds to the colchicine site of tubulin with distinct effects on microtubule organization
    • Prota, A. E. et al. The novel microtubule-destabilizing drug BAL27862 binds to the colchicine site of tubulin with distinct effects on microtubule organization. J. Mol. Biol. 426, 1848-1860 (2014)
    • (2014) J. Mol. Biol , vol.426 , pp. 1848-1860
    • Prota, A.E.1
  • 32
    • 0028103275 scopus 로고
    • N. The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project
    • Collaborative Computational Project, N. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763 (1994)
    • (1994) Acta Crystallogr. D Biol. Crystallogr , vol.50 , pp. 760-763
  • 34
    • 76449099287 scopus 로고    scopus 로고
    • XDS. Acta Crystallogr
    • Kabsch, W. XDS. Acta Crystallogr. D Biol. Crystallogr. 66, 125-132 (2010)
    • (2010) D Biol. Crystallogr , vol.66 , pp. 125-132
    • Kabsch, W.1
  • 35
    • 75649151032 scopus 로고    scopus 로고
    • Xia2: An expert system for macromolecular crystallography data reduction
    • Winter, G. xia2: an expert system for macromolecular crystallography data reduction. J. Appl. Cryst. 43, 5 (2010)
    • (2010) J. Appl. Cryst , vol.43 , pp. 5
    • Winter, G.1
  • 36
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007)
    • (2007) J. Appl. Crystallogr , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 38
    • 79953763877 scopus 로고    scopus 로고
    • REFMAC5 for the refinement of macromolecular crystal structures
    • Murshudov, G. N. et al. REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr. D Biol. Crystallogr. 67, 355-367 (2011)
    • (2011) Acta Crystallogr. D Biol. Crystallogr , vol.67 , pp. 355-367
    • Murshudov, G.N.1
  • 39
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O. & Mann, M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68, 850-858 (1996)
    • (1996) Anal. Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 40
    • 0019833086 scopus 로고
    • Effects of inhibitors of tubulin polymerization on GTP hydrolysis
    • Lin, C. M. & Hamel, E. Effects of inhibitors of tubulin polymerization on GTP hydrolysis. J. Biol. Chem. 256, 9242-9245 (1981)
    • (1981) J. Biol. Chem , vol.256 , pp. 9242-9245
    • Lin, C.M.1    Hamel, E.2
  • 41
    • 0018570883 scopus 로고
    • Effect of antimitotic drugs on tubulin GTPase activity and self-assembly
    • David-Pfeuty, T., Simon, C. & Pantaloni, D. Effect of antimitotic drugs on tubulin GTPase activity and self-assembly. J. Biol. Chem. 254, 11696-11702 (1979)
    • (1979) J. Biol. Chem , vol.254 , pp. 11696-11702
    • David-Pfeuty, T.1    Simon, C.2    Pantaloni, D.3
  • 42
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • Karplus, P. A. & Diederichs, K. Linking crystallographic model and data quality. Science 336, 1030-1033 (2012)
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2


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