The natural product cucurbitacin e inhibits depolymerization of actin filaments

ACS Chemical Biology

Volumn 7, Issue 9, 2012, Pages 1502-1508

  Sörensen, Pia M ^a   Iacob, Roxana E ^b   Fritzsche, Marco ^c   Engen, John R ^b   Brieher, William M ^d   Charras, Guillaume ^c   Eggert, Ulrike S ^a,e  

^a HARVARD MEDICAL SCHOOL   (United States)

^b NORTHEASTERN UNIVERSITY   (United States)

^c UNIVERSITY COLLEGE LONDON   (United Kingdom)

^d UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^e KING'S COLLEGE LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CUCURBITACIN; CUCURBITACIN E; F ACTIN; G ACTIN; JASPAMIDE; NATURAL PRODUCT; PHALLOIDIN; UNCLASSIFIED DRUG;

ACTIN FILAMENT; ARTICLE; CONTROLLED STUDY; DEPOLYMERIZATION; DRUG MECHANISM; FLUORESCENCE; HUMAN; HUMAN CELL; PRIORITY JOURNAL;

ACTIN CYTOSKELETON; ACTINS; ANIMALS; BIOLOGICAL AGENTS; CUCURBITACEAE; DEPSIPEPTIDES; HELA CELLS; HUMANS; POLYMERIZATION; RABBITS; TRITERPENES;

EID: 84868087963     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb300254s     Document Type: Article

References (34)

1. Siripala, A. D., and Welch, M. D. (2007) SnapShot: actin regulators II. Cell 128, 1014.
2. Siripala, A. D., and Welch, M. D. (2007) SnapShot: actin regulators I. Cell 128, 626.
3. Campellone, K. G., and Welch, M. D. (2010) A nucleator arms race: cellular control of actin assembly. Nat. Rev. Mol. Cell. Biol. 11, 237-251.
4. Winder, S. J. (2003) Structural insights into actin-binding, branching and bundling proteins. Curr. Opin. Cell. Biol. 15, 14-22. (Pubitemid 36044710)
5. Atilla-Gokcumen, G. E., Castoreno, A. B., Sasse, S., and Eggert, U. S. (2010) Making the cut: the chemical biology of cytokinesis. ACS Chem. Biol. 5, 79-90.
6. Peterson, J. R., and Mitchison, T. J. (2002) Small molecules, big impact: a history of chemical inhibitors and the cytoskeleton. Chem. Biol. 9, 1275-1285. (Pubitemid 36010683)
7. Spector, I., Shochet, N. R., Kashman, Y., and Groweiss, A. (1983) Latrunculins: novel marine toxins that disrupt microfilament organization in cultured cells. Science 219, 493-495. (Pubitemid 13189272)
8. Bubb, M. R., Senderowicz, A. M., Sausville, E. A., Duncan, K. L., and Korn, E. D. (1994) Jasplakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin. J. Biol. Chem. 269, 14869-14871. (Pubitemid 24198320)
9. Forscher, P., and Smith, S. J. (1988) Actions of cytochalasins on the organization of actin filaments and microtubules in a neuronal growth cone. J. Cell Biol. 107, 1505-1516.
10. Eggert, U. S., Kiger, A. A., Richter, C., Perlman, Z. E., Perrimon, N., Mitchison, T. J., and Field, C. M. (2004) Parallel chemical genetic and genome-wide RNAi screens identify cytokinesis inhibitors and targets. PLoS Biol. 2, e379.
11. Maloney, K. N., Fujita, M., Eggert, U. S., Schroeder, F. C., Field, C. M., Mitchison, T. J., and Clardy, J. (2008) Actin-aggregating cucurbitacins from Physocarpus capitatus. J. Nat. Prod. 71, 1927-1929.
12. Chen, J. C., Chiu, M. H., Nie, R. L., Cordell, G. A., and Qiu, S. X. (2005) Cucurbitacins and cucurbitane glycosides: structures and biological activities. Nat. Prod. Rep. 22, 386-399.
13. Raikhlin-Eisenkraft, B., and Bentur, Y. (2000) Ecbalium elaterium (squirting cucumber)-remedy or poison? J. Toxicol. Clin. Toxicol. 38, 305-308. (Pubitemid 30397693)
14. Graness, A., Poli, V., and Goppelt-Struebe, M. (2006) STAT3- independent inhibition of lysophosphatidic acid-mediated upregulation of connective tissue growth factor (CTGF) by cucurbitacin I. Biochem. Pharmacol. 72, 32-41. (Pubitemid 43795344)
15. Duncan, K. L., Duncan, M. D., Alley, M. C., and Sausville, E. A. (1996) Cucurbitacin E-induced disruption of the actin and vimentin cytoskeleton in prostate carcinoma cells. Biochem. Pharmacol. 52, 1553-1560. (Pubitemid 26375461)
16. Momma, K., Masuzawa, Y., Nakai, N., Chujo, M., Murakami, A., Kioka, N., Kiyama, Y., Akita, T., and Nagao, M. (2008) Direct interaction of Cucurbitacin E isolated from Alsomitra macrocarpa to actin filament. Cytotechnology 56, 33-39.
17. Knecht, D. A., LaFleur, R. A., Kahsai, A. W., Argueta, C. E., Beshir, A. B., and Fenteany, G. (2010) Cucurbitacin I inhibits cell motility by indirectly interfering with actin dynamics. PLoS One 5, e14039.
18. Cooper, J. A., Walker, S. B., and Pollard, T. D. (1983) Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization. J. Muscle Res. Cell Motil. 4, 253-262. (Pubitemid 13069975)
19. Lees, A., Haddad, J. G., and Lin, S. (1984) Brevin and vitamin D binding protein: comparison of the effects of two serum proteins on actin assembly and disassembly. Biochemistry 23, 3038-3047. (Pubitemid 14099203)
20. Heidecker, M., Yan-Marriott, Y., and Marriott, G. (1995) Proximity relationships and structural dynamics of the phalloidin binding site of actin filaments in solution and on single actin filaments on heavy meromyosin. Biochemistry 34, 11017-11025.
21. Kouyama, T., and Mihashi, K. (1981) Fluorimetry study of N-(1- pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. Eur. J. Biochem. 114, 33-38. (Pubitemid 11101489)
22. Kiuchi, T., Nagai, T., Ohashi, K., and Mizuno, K. (2011) Measurements of spatiotemporal changes in G-actin concentration reveal its effect on stimulus-induced actin assembly and lamellipodium extension. J. Cell Biol. 193, 365-380.
23. Oda, T., Iwasa, M., Aihara, T., Maeda, Y., and Narita, A. (2009) The nature of the globular- to fibrous-actin transition. Nature 457, 441-445.
24. Oda, T., and Maeda, Y. (2010) Multiple conformations of F-actin. Structure 18, 761-767.
25. Galkin, V. E., Orlova, A., Schroder, G. F., and Egelman, E. H. (2010) Structural polymorphism in F-actin. Nat. Struct. Mol. Biol. 17, 1318-1323.
26. Kueh, H. Y., Brieher, W. M., and Mitchison, T. J. (2008) Dynamic stabilization of actin filaments. Proc. Natl. Acad. Sci. U.S.A. 105, 16531-16536.
27. Egelman, E. H., and Orlova, A. (1995) Allostery, cooperativity, and different structural states in F-actin. J. Struct. Biol. 115, 159-162.
28. Papp, G., Bugyi, B., Ujfalusi, Z., Barko, S., Hild, G., Somogyi, B., and Nyitrai, M. (2006) Conformational changes in actin filaments induced by formin binding to the barbed end. Biophys. J. 91, 2564-2572. (Pubitemid 44511711)
29. Galkin, V. E., Orlova, A., and Egelman, E. H. (2012) Actin filaments as tension sensors. Curr. Biol. 22, R96-R101.
30. Liu, D. F., Wang, D., and Stracher, A. (1990) The accessibility of the thiol groups on G- and F-actin of rabbit muscle. Biochem. J. 266, 453-459. (Pubitemid 20090146)
31. Kabsch, W., and Vandekerckhove, J. (1992) Structure and function of actin. Annu. Rev. Biophys. Biomol. Struct. 21, 49-76.
32. Insall, R. H., and Machesky, L. M. (2009) Actin dynamics at the leading edge: from simple machinery to complex networks. Dev. Cell 17, 310-322.
33. Andrianantoandro, E., and Pollard, T. D. (2006) Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin. Mol. Cell 24, 13-23. (Pubitemid 44466682)
34. Lee, D. H., Thoennissen, N. H., Goff, C., Iwanski, G. B., Forscher, C., Doan, N. B., Said, J. W., and Koeffler, H. P. (2011) Synergistic effect of low-dose cucurbitacin B and low-dose methotrexate for treatment of human osteosarcoma. Cancer Lett. 306, 161-170.