Nucleotide-dependent bending flexibility of tubulin regulates microtubule assembly

Nature

Volumn 435, Issue 7044, 2005, Pages 911-915

  Wang, Hong Wei ^a,b   Nogales, Eva ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; DIMERS; HYDROLYSIS; POLYMERIZATION; POLYMERS; STRUCTURE (COMPOSITION);

DEPOLYMERIZERS; NUCLEOTIDE; PROTOFILAMENTS; TUBULIN;

NUCLEIC ACIDS;

DIMER; GUANOSINE DIPHOSPHATE MANNOSE; GUANOSINE TRIPHOSPHATE; GUANOSINE TRIPHOSPHATE DERIVATIVE; NUCLEOTIDE; TUBULIN; 5' GUANYLYLMETHYLENEBISPHOSPHONATE; 5'-GUANYLYLMETHYLENEBISPHOSPHONATE; DRUG DERIVATIVE; GUANOSINE DIPHOSPHATE;

CELLS AND CELL COMPONENTS;

ARTICLE; CELL CYCLE; CONFORMATIONAL TRANSITION; CRYSTALLOGRAPHY; DEPOLYMERIZATION; MICROTUBULE ASSEMBLY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN HYDROLYSIS; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; CHEMICAL STRUCTURE; CHEMISTRY; CRYOELECTRON MICROSCOPY; DIMERIZATION; HYDROLYSIS; METABOLISM; MICROTUBULE; PLIABILITY; ULTRASTRUCTURE;

CRYOELECTRON MICROSCOPY; DIMERIZATION; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; HYDROLYSIS; MICROTUBULES; MODELS, MOLECULAR; PLIABILITY; PROTEIN CONFORMATION; TUBULIN;

EID: 20544463212     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature03606     Document Type: Article

References (20)

1. Desai, A. & Mitchison, T. J. Microtubule polymerization dynamics. Annu. Rev. Cell Dev. Biol. 13, 83-117 (1997).
2. Jordan, M. A. Mechanism of action of antitumor drugs that interact with microtubules and tubulin. Curr. Med Chem. Anti-Cancer Agents 2, 1-17 (2002).
3. Heald, R. & Nogales, E. Microtubule dynamics. J. Cell Sci. 115, 3-4 (2002).
4. Nogales, E., Wolf, S. G. & Downing, K. H. Structure of the αβ tubulin dimer by electron crystallography. Nature 391,199-203 (1998).
5. Löwe, J., Li, H., Downing, K. H. & Nogales, E. Refined structure of αβ-tubulin at 3.5 Å resolution. J. Mol. Biol. 313, 1045-1057 (2001).
6. Li, H., DeRosier, D. J., Nicholson, W. V., Nogales, E. & Downing, K. H. Microtubule structure at 8 Å resolution. Structure 10, 1317-1328 (2002).
7. Ravelli, R. B. et al. Insight into tubulin regulation from a complex with colchicines and a stathmin-like domain. Nature 428, 198-202 (2004).
8. Chrétien, D., Fuller, S. D. & Karsenti, E. Structure of growing microtubule ends: two-dimensional sheets close into tubes at variable rates. J. Cell Biol. 129, 1311-1328 (1995).
9. Howard, W. D. & Timasheff, S. N. GDP state of tubulin: stabilization of double rings. Biochemistry 25, 8292-8300 (1986).
10. Nicholson, W. V., Lee, M., Downing, K. H. & Nogales, E. Cryo-electron microscopy of GDP-tubulin rings. Cell Biochem. Biophys. 31, 175-183 (1999).
11. Mandelkow, E. M., Mandelkow, E. & Milligan, R. A. Microtubule dynamics and microtubule caps: A time-resolved cryo-electron microscopy study. J. Cell Biol. 114, 977-991 (1991).
12. Tran, P. T., Joshi, P. & Salmon, E. D. How tubulin subunits are lost from the shortening ends of microtubules. J. Struct. Biol. 118, 107-118 (1997).
13. Wang, H.-W. & Nogales, E. An iterative Fourier-Bessel algorithm for reconstruction of helical structures with severe Bessel overlap. J. Struct. Biol. 149, 65-78 (2005).
14. Caplow, M., Ruhlen, R. L. & Shanks, J. The free energy for hydrolysis of a microtubule-bound nucleotide triphosphate is nearly zero: all of the free energy for hydrolysis is stored in the microtubule lattice. J. Cell Biol. 127, 779-788 (1994).
15. Mickey, B. & Howard, J. Rigidity of microtubules is increased by stabilizing agents. J. Cell Biol. 130, 909-917 (1995).
16. Hyman, A. A. & Karsenti, E. Morphogenetic properties of microtubules and mitotic spindle assembly. Cell 84, 401-410 (1996).
17. Andreu, J. M., Gorbunoff, M. J., Medrano, F. J. & Timasheff, S. N. Mechanism of colchicine binding to tubulin. Tolerance of constituents in ring C' of biphenyl analogues. Biochemistry 30, 3777-3786 (1991).
18. Jánosi, I. M., Chrétien, D. & Flyvbjerg, H. Modeling elastic properties of microtubule tips and walls. Eur. Biophys. J. 27, 501-513 (1998).
19. Hyman, A. A., Chrétien, D., Severin, F. & Wade, R. H. Structural changes accompanying GTP hydrolysis in microtubules: information from a slowly hydrolyzable analogue guanylyl-(α,β)-methylene- diphosphonate, J. Cell Biol. 128, 117-125 (1995).
20. Müller-Reichert, T., Chrétien, D., Severin, F. & Hyman, A. A. Structural changes at microtubule ends accompanying GTP hydrolysis: information from a slowly hydrolyzable analogue of GTP, guanylyl (α,β)methylenediphosphonate. Proc. Natl Acad. Sci. USA 95, 3661-3666 (1998).