Preparation of Pure Tyrosinated or Detyrosinated Tubulin Isoforms

Methods in Molecular Biology

Volumn 777, Issue , 2011, Pages 71-86

  Lafanechère, Laurence ^a   Job, Didier ^b,c,d  

^a INSTITUT ALBERT BONNIOT   (France)

^b INSERM   (France)

^c CEA GRENOBLE   (France)

^d UNIV GRENOBLE ALPES   (France)

Author keywords

D 2 tubulin; Detyrosination; Nontyro sinatable tubulin; Posttranslational modifications; Tubulin; Tubulin tyrosine ligase; Tyrosination cycle

Indexed keywords

ISOPROTEIN; TUBULIN; TYROSINE;

ANIMAL; ARTICLE; CHEMISTRY; HUMAN; ISOLATION AND PURIFICATION;

ANIMALS; HUMANS; PROTEIN ISOFORMS; TUBULIN; TYROSINE;

ANIMALIA;

EID: 79960930039     PISSN: 10643745     EISSN: 19406029     Source Type: Book Series    
DOI: 10.1007/978-1-61779-252-6_5     Document Type: Chapter

References (25)

1. Barra, H. S., Arce, C. A., and Argarana, C. E. (1988) Posttranslational tyrosination/detyro-sination of tubulin. Mol Neurobiol 2, 133–53.
2. Westermann, S., and Weber, K. (2003) Posttranslational modifications regulate microtubule function. Nat Rev Mol Cell Biol 4, 938–47.
3. MacRae, T. H. (1997) Tubulin post-translational modifications--enzymes and their mechanisms of action. Eur J Biochem 244, 265–78.
4. Lafanechere, L., Courtay-Cahen, C., Kawakami, T., Jacrot, M., Rudiger, M., Wehland, J., Job, D., and Margolis, R. L. (1998) Suppression of tubulin tyrosine ligase during tumor growth. J Cell Sci 111 (Pt 2), 171–81.
5. Mialhe, A., Lafanechere, L., Treilleux, I., Peloux, N., Dumontet, C., Bremond, A., Panh, M. H., Payan, R., Wehland, J., Margolis, R. L., and Job, D. (2001) Tubulin detyrosination is a frequent occurrence in breast cancers of poor prognosis. Cancer Res 61, 5024–7.
6. Erck, C., Peris, L., Andrieux, A., Meissirel, C., Gruber, A. D., Vernet, M., Schweitzer, A., Saoudi, Y., Pointu, H., Bosc, C., Salin, P. A., Job, D., and Wehland, J. (2005) A vital role of tubulin-tyrosine-ligase for neuronal organization. Proc Natl Acad Sci USA 102, 7853–8.
7. Peris, L., Thery, M., Faure, J., Saoudi, Y., Lafanechere, L., Chilton, J. K., Gordon-Weeks, P., Galjart, N., Bornens, M., Wordeman, L., Wehland, J., Andrieux, A., and Job, D. (2006) Tubulin tyrosination is a major factor affecting the recruitment of CAP-Gly proteins at microtubule plus ends. J Cell Biol 174, 839–49.
8. Badin-Larcon, A. C., Boscheron, C., Soleilhac, J. M., Piel, M., Mann, C., Denarier, E., Fourest-Lieuvin, A., Lafanechere, L., Bornens, M., and Job, D. (2004) Suppression of nuclear oscillations in Saccharomyces cerevisiae expressing Glu tubulin. Proc Natl Acad Sci USA 101, 5577–82.
9. Steinmetz, M. O., and Akhmanova, A. (2008) Capturing protein tails by CAP-Gly domains. Trends Biochem Sci 33, 535–45.
10. Weisbrich, A., Honnappa, S., Jaussi, R., Okhrimenko, O., Frey, D., Jelesarov, I., Akhmanova, A., and Steinmetz, M. O. (2007) Structure-function relationship of CAP-Gly domains. Nat Struct Mol Biol 14, 959–67.
11. Peris, L., Wagenbach, M., Lafanechere, L., Brocard, J., Moore, A. T., Kozielski, F., Job, D., Wordeman, L., and Andrieux, A. (2009) Motor-dependent microtubule disassembly driven by tubulin tyrosination. J Cell Biol 185, 1159–66.
12. Konishi, Y., and Setou, M. (2009) Tubulin tyrosination navigates the kinesin-1 motor domain to axons. Nat Neurosci 12, 559–67.
13. Cai, D., McEwen, D. P., Martens, J. R., Meyhofer, E., and Verhey, K. J. (2009) Single molecule imaging reveals differences in microtubule track selection between Kinesin motors. PLoS Biol 7, e1000216.
14. Roll-Mecak, A., and Vale, R. D. (2008) Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin. Nature 451, 363–7.
15. Paturle-Lafanechere, L., Edde, B., Denoulet, P., Van Dorsselaer, A., Mazarguil, H., Le Caer, J. P., Wehland, J., and Job, D. (1991) Characterization of a major brain tubulin variant which cannot be tyrosinated. Biochemistry 30, 10523–8.
16. Paturle-Lafanechere, L., Manier, M., Trigault, N., Pirollet, F., Mazarguil, H., and Job, D. (1994) Accumulation of delta 2-tubulin, a major tubulin variant that cannot be tyrosinated, in neuronal tissues and in stable microtubule assemblies. J Cell Sci 107 (Pt 6), 1529–43.
17. Lafanechere, L., and Job, D. (2000) The third tubulin pool. Neurochem Res 25, 11–8.
18. Paturle, L., Wehland, J., Margolis, R. L., and Job, D. (1989) Complete separation of tyrosinated, detyrosinated, and nontyrosinatable brain tubulin subpopulations using affinity chromatography. Biochemistry 28, 2698–704.
19. Banerjee, A. (1999) A monoclonal antibody to alpha-tubulin: purification of functionally active alpha-tubulin isoforms. Biochemistry 38, 5438–46.
20. Wehland, J., Schroder, H. C., and Weber, K. (1986) Isolation and purification of tubulin tyrosine ligase. Methods Enzymol 134, 170–9.
21. Schroder, H. C., Wehland, J., and Weber, K. (1985) Purification of brain tubulin-tyrosine ligase by biochemical and immunological methods. J Cell Biol 100, 276–81.
22. Weingarten, M. D., Lockwood, A. H., Hwo, S. Y., and Kirschner, M. W. (1975) A protein factor essential for microtubule assembly. Proc Natl Acad Sci USA 72, 1858–62.
23. Cuatrecasas, P. (1970) Protein purification by affinity chromatography. Derivatizations of agarose and polyacrylamide beads. J Biol Chem 245, 3059–65.
24. Sandoval, I. V., and Cuatrecasas, P. (1976) Protein kinase associated with tubulin: affinity chromatography and properties. Biochemistry 15, 3424–32.
25. Wehland, J., and Weber, K. (1987) Turnover of the carboxy-terminal tyrosine of alpha-tubulin and means of reaching elevated levels of detyrosination in living cells. J Cell Sci 88 (Pt 2), 185–203.