Post-translational modifications regulate microtubule function (original) (raw)

• Luduena, R. F. Multiple forms of tubulin: different gene products and covalent modifications. Int. Rev. Cytol. 178, 207–275 (1998).
  Article CAS PubMed Google Scholar
• MacRae, T. H. Tubulin post-translational modifications — enzymes and their mechanisms of action. Eur. J. Biochem. 244, 265–278 (1997).
  Article CAS PubMed Google Scholar
• Nogales, E., Whittaker, M., Milligan, R. A. & Downing, K. H. High-resolution model of the microtubule. Cell 96, 79–88 (1999).
  Article CAS PubMed Google Scholar
• Nogales, E., Wolf, S. G. & Downing, K. H. Structure of the αβ tubulin dimer by electron crystallography. Nature 391, 199–203 (1998).
  Article CAS PubMed Google Scholar
• Jimenez, M. A. et al. Helicity of α(404–451) and β(394–445) tubulin C-terminal recombinant peptides. Protein Sci. 8, 788–799 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Sullivan, K. F. & Cleveland, D. W. Identification of conserved isotype-defining variable region sequences for four vertebrate β tubulin polypeptide classes. Proc. Natl Acad. Sci. USA 83, 4327–4331 (1986).
  Article CAS PubMed PubMed Central Google Scholar
• Mejillano, M. R. & Himes, R. H. Assembly properties of tubulin after carboxyl group modification. J. Biol. Chem. 266, 657–664 (1991).
  Article CAS PubMed Google Scholar
• Mejillano, M. R., Tolo, E. T., Williams, R. C. Jr. & Himes, R. H. The conversion of tubulin carboxyl groups to amides has a stabilizing effect on microtubules. Biochemistry 31, 3478–3483 (1992).
  Article CAS PubMed Google Scholar
• Fackenthal, J. D., Turner, F. R. & Raff, E. C. Tissue-specific microtubule functions in Drosophila spermatogenesis require the β2-tubulin isotype-specific carboxy terminus. Dev. Biol. 158, 213–227 (1993).
  Article CAS PubMed Google Scholar
• Duan, J. & Gorovsky, M. A. Both carboxy-terminal tails of α- and β-tubulin are essential, but either one will suffice. Curr. Biol. 12, 313–316 (2002). Elegant genetic experiments identify essential functions for the tubulin carboxy-terminal tails in Tetrahymena.
  Article CAS PubMed Google Scholar
• Strahl, B. D. & Allis, C. D. The language of covalent histone modifications. Nature 403, 41–45 (2000).
  Article CAS PubMed Google Scholar
• L'Hernault, S. W. & Rosenbaum, J. L. Chlamydomonas α-tubulin is posttranslationally modified by acetylation on the ε-amino group of a lysine. Biochemistry 24, 473–478 (1985).
  Article CAS PubMed Google Scholar
• LeDizet, M. & Piperno, G. Identification of an acetylation site of Chlamydomonas α-tubulin. Proc. Natl Acad. Sci. USA 84, 5720–5724 (1987).
  Article CAS PubMed PubMed Central Google Scholar
• Sasse, R. & Gull, K. Tubulin post-translational modifications and the construction of microtubular organelles in Trypanosoma brucei. J. Cell Sci. 90, 577–589 (1988).
  Article CAS PubMed Google Scholar
• Weber, K., Schneider, A., Westermann, S., Muller, N. & Plessmann, U. Posttranslational modifications of α- and β-tubulin in Giardia lamblia, an ancient eukaryote. FEBS Lett. 419, 87–91 (1997).
  Article CAS PubMed Google Scholar
• Schneider, A., Plessmann, U., Felleisen, R. & Weber, K. Posttranslational modifications of trichomonad tubulins; identification of multiple glutamylation sites. FEBS Lett. 429, 399–402 (1998).
  Article CAS PubMed Google Scholar
• Schneider, A., Plessmann, U. & Weber, K. Subpellicular and flagellar microtubules of Trypanosoma brucei are extensively glutamylated. J. Cell Sci. 110, 431–437 (1997).
  Article CAS PubMed Google Scholar
• Maruta, H., Greer, K. & Rosenbaum, J. L. The acetylation of α-tubulin and its relationship to the assembly and disassembly of microtubules. J. Cell Biol. 103, 571–579 (1986).
  Article CAS PubMed Google Scholar
• Hubbert, C. et al. HDAC6 is a microtubule-associated deacetylase. Nature 417, 455–458 (2002).
  Article CAS PubMed Google Scholar
• Matsuyama, A. et al. In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation. EMBO J. 21, 6820–6831 (2002).
  Article CAS PubMed PubMed Central Google Scholar
• Zhang, Y. et al. HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo. EMBO J. 22, 1168–1179 (2003).
  Article CAS PubMed PubMed Central Google Scholar
• North, B. J., Marshall, B. L., Borra, M. T., Denu, J. M. & Verdin, E. The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol. Cell 11, 437–444 (2003). References 19–22 identify HDAC6 and SIRT2 as tubulin deacetylases and propose a role for tubulin acetylation in cell motility.
  Article CAS PubMed Google Scholar
• Kozminski, K. G., Diener, D. R. & Rosenbaum, J. L. High level expression of nonacetylatable α-tubulin in Chlamydomonas reinhardtii. Cell Motil. Cytoskeleton 25, 158–170 (1993).
  Article CAS PubMed Google Scholar
• Gaertig, J. et al. Acetylation of lysine 40 in α-tubulin is not essential in Tetrahymena thermophila. J. Cell Biol. 129, 1301–1310 (1995).
  Article CAS PubMed Google Scholar
• Haggarty, S. J., Koeller, K. M., Wong, J. C., Grozinger, C. M. & Schreiber, S. L. Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation. Proc. Natl Acad. Sci. USA 100, 4389–4394 (2003).
  Article CAS PubMed PubMed Central Google Scholar
• Palazzo, A., Ackerman, B. & Gundersen, G. G. Cell biology: tubulin acetylation and cell motility. Nature 421, 230 (2003).
  Article CAS PubMed Google Scholar
• Redeker, V. et al. Polyglycylation of tubulin: a posttranslational modification in axonemal microtubules. Science 266, 1688–1691 (1994).
  Article CAS PubMed Google Scholar
• Rudiger, M., Plessmann, U., Rudiger, A. H. & Weber, K. β tubulin of bull sperm is polyglycylated. FEBS Lett. 364, 147–151 (1995).
  Article CAS PubMed Google Scholar
• Plessmann, U. & Weber, K. Mammalian sperm tubulin: an exceptionally large number of variants based on several posttranslational modifications. J. Protein Chem. 16, 385–390 (1997).
  Article CAS PubMed Google Scholar
• Mary, J., Redeker, V., Le Caer, J. P., Rossier, J. & Schmitter, J. M. Posttranslational modifications of axonemal tubulin. J. Protein Chem. 16, 403–407 (1997).
  Article CAS PubMed Google Scholar
• Bre, M. H., Redeker, V., Vinh, J., Rossier, J. & Levilliers, N. Tubulin polyglycylation: differential posttranslational modification of dynamic cytoplasmic and stable axonemal microtubules in paramecium. Mol. Biol. Cell 9, 2655–2665 (1998).
  Article CAS PubMed PubMed Central Google Scholar
• Weber, K., Schneider, A., Muller, N. & Plessmann, U. Polyglycylation of tubulin in the diplomonad Giardia lamblia, one of the oldest eukaryotes. FEBS Lett. 393, 27–30 (1996).
  Article CAS PubMed Google Scholar
• Xia, L. et al. Polyglycylation of tubulin is essential and affects cell motility and division in Tetrahymena thermophila. J. Cell Biol. 149, 1097–1106 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Thazhath, R., Liu, C. & Gaertig, J. Polyglycylation domain of β-tubulin maintains axonemal architecture and affects cytokinesis in Tetrahymena. Nature Cell Biol. 4, 256–259 (2002). References 33 and 34 provide a careful analysis of tubulin polyglycylation in Tetrahymena and identify its essential functions in cell motility and cytokinesis.
  Article CAS PubMed Google Scholar
• Edde, B. et al. Posttranslational glutamylation of α-tubulin. Science 247, 83–85 (1990).
  Article CAS PubMed Google Scholar
• Mary, J., Redeker, V., Le Caer, J. P., Prome, J. C. & Rossier, J. Class I and IVa β-tubulin isotypes expressed in adult mouse brain are glutamylated. FEBS Lett. 353, 89–94 (1994).
  Article CAS PubMed Google Scholar
• Rudiger, M., Plessman, U., Kloppel, K. D., Wehland, J. & Weber, K. Class II tubulin, the major brain β tubulin isotype is polyglutamylated on glutamic acid residue 435. FEBS Lett. 308, 101–105 (1992).
  Article CAS PubMed Google Scholar
• Alexander, J. et al. Characterization of posttranslational modifications in neuron-specific class III β-tubulin by mass spectrometry. Proc. Natl Acad. Sci. USA 88, 4685–4689 (1991).
  Article CAS PubMed PubMed Central Google Scholar
• Redeker, V., Rossier, J. & Frankfurter, A. Posttranslational modifications of the C-terminus of α-tubulin in adult rat brain: α4 is glutamylated at two residues. Biochemistry 37, 14838–14844 (1998).
  Article CAS PubMed Google Scholar
• Bre, M. H., de Nechaud, B., Wolff, A. & Fleury, A. Glutamylated tubulin probed in ciliates with the monoclonal antibody GT335. Cell Motil. Cytoskeleton 27, 337–349 (1994).
  Article CAS PubMed Google Scholar
• Lechtreck, K. F. & Geimer, S. Distribution of polyglutamylated tubulin in the flagellar apparatus of green flagellates. Cell Motil. Cytoskeleton 47, 219–235 (2000).
  Article CAS PubMed Google Scholar
• Bobinnec, Y. et al. Glutamylation of centriole and cytoplasmic tubulin in proliferating non-neuronal cells. Cell Motil. Cytoskeleton 39, 223–232 (1998).
  Article CAS PubMed Google Scholar
• Regnard, C. et al. Polyglutamylation of nucleosome assembly proteins. J. Biol. Chem. 275, 15969–15976 (2000). Identifies the nucleosome assembly proteins NAP1 and NAP2 as substrates for polyglutamylation, indicating that this is a more general protein modification.
  Article CAS PubMed Google Scholar
• Regnard, C., Audebert, S., Desbruyeres Denoulet, P. & Edde, B. Tubulin polyglutamylase: partial purification and enzymatic properties. Biochemistry 37, 8395–8404 (1998).
  Article CAS PubMed Google Scholar
• Regnard, C. et al. Characterisation of PGs1, a subunit of a protein complex co-purifying with tubulin polyglutamylase. J. Cell Sci. 116, 4181–4190 (2003).
  Article CAS PubMed Google Scholar
• Regnard, C., Desbruyeres, E., Denoulet, P. & Edde, B. Tubulin polyglutamylase: isozymic variants and regulation during the cell cycle in HeLa cells. J. Cell Sci. 112, 4281–4289 (1999).
  Article CAS PubMed Google Scholar
• Westermann, S., Schneider, A., Horn, E. K. & Weber, K. Isolation of tubulin polyglutamylase from Crithidia; binding to microtubules and tubulin, and glutamylation of mammalian brain α- and β-tubulins. J. Cell Sci. 112, 2185–2193 (1999).
  Article CAS PubMed Google Scholar
• Westermann, S., Plessmann, U. & Weber, K. Synthetic peptides identify the minimal substrate requirements of tubulin polyglutamylase in side chain elongation. FEBS Lett. 459, 90–94 (1999).
  Article CAS PubMed Google Scholar
• Westermann, S. & Weber, K. Identification of CfNek, a novel member of the NIMA family of cell cycle regulators, as a polypeptide copurifying with tubulin polyglutamylation activity in Crithidia. J. Cell Sci. 115, 5003–5012 (2002). Identifies a kinase of the NIMA family as the first enzyme involved in tubulin polyglutamylation.
  Article CAS PubMed Google Scholar
• Liu, S. et al. A defect in a novel Nek-family kinase causes cystic kidney disease in the mouse and in zebrafish. Development 129, 5839–5846 (2002).
  Article CAS PubMed Google Scholar
• Pazour, G. J. & Rosenbaum, J. L. Intraflagellar transport and cilia-dependent diseases. Trends Cell Biol. 12, 551–555 (2002).
  Article CAS PubMed Google Scholar
• Manning, G., Whyte, D. B., Martinez, R., Hunter, T. & Sudarsanam, S. The protein kinase complement of the human genome. Science 298, 1912–1934 (2002).
  Article CAS PubMed Google Scholar
• Upadhya, P., Birkenmeier, E. H., Birkenmeier, C. S. & Barker, J. E. Mutations in a NIMA-related kinase gene, Nek1, cause pleiotropic effects including a progressive polycystic kidney disease in mice. Proc. Natl Acad. Sci. USA 97, 217–221 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Audebert, S. et al. Reversible polyglutamylation of α- and β-tubulin and microtubule dynamics in mouse brain neurons. Mol. Biol. Cell 4, 615–626 (1993).
  Article CAS PubMed PubMed Central Google Scholar
• Larcher, J. C., Boucher, D., Lazereg, S., Gros, F. & Denoulet, P. Interaction of kinesin motor domains with α- and β-tubulin subunits at a tau-independent binding site. Regulation by polyglutamylation. J. Biol. Chem. 271, 22117–22124 (1996).
  Article CAS PubMed Google Scholar
• Bonnet, C. et al. Differential binding regulation of microtubule-associated proteins MAP1A, MAP1B, and MAP2 by tubulin polyglutamylation. J. Biol. Chem. 276, 12839–12848 (2001).
  Article CAS PubMed Google Scholar
• Okada, Y. & Hirokawa, N. Mechanism of the single-headed processivity: diffusional anchoring between the K-loop of kinesin and the C terminus of tubulin. Proc. Natl Acad. Sci. USA 97, 640–645 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Thorn, K. S., Ubersax, J. A. & Vale, R. D. Engineering the processive run length of the kinesin motor. J. Cell Biol. 151, 1093–1100 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Gagnon, C. et al. The polyglutamylated lateral chain of α-tubulin plays a key role in flagellar motility. J. Cell Sci. 109, 1545–1553 (1996).
  Article CAS PubMed Google Scholar
• Million, K. et al. Polyglutamylation and polyglycylation of α- and β-tubulins during in vitro ciliated cell differentiation of human respiratory epithelial cells. J. Cell Sci. 112, 4357–4366 (1999).
  Article CAS PubMed Google Scholar
• Bobinnec, Y. et al. Centriole disassembly in vivo and its effect on centrosome structure and function in vertebrate cells. J. Cell Biol. 143, 1575–1589 (1998). Antibody-microinjection studies identify tubulin polyglutamylation as being essential for centriole stability and centrosome structure.
  Article CAS PubMed PubMed Central Google Scholar
• Bornens, M. Centrosome composition and microtubule anchoring mechanisms. Curr. Opin. Cell Biol. 14, 25–34 (2002).
  Article CAS PubMed Google Scholar
• Argarana, C. E., Barra, H. S. & Caputto, R. Release of [14C]tyrosine from tubulinyl-[14C]tyrosine by brain extract. Separation of a carboxypeptidase from tubulin-tyrosine ligase. Mol. Cell. Biochem. 19, 17–21 (1978).
  Article CAS PubMed Google Scholar
• Barra, H. S., Rodriguez, J. A., Arce, C. A. & Caputto, R. A soluble preparation from rat brain that incorporates into its own proteins (14C)arginine by a ribonuclease-sensitive system and (14C)tyrosine by a ribonuclease-insensitive system. J. Neurochem. 20, 97–108 (1973).
  Article CAS PubMed Google Scholar
• Arce, C. A., Rodriguez, J. A., Barra, H. S. & Caputo, R. Incorporation of L-tyrosine, L-phenylalanine and L-3,4-dihydroxyphenylalanine as single units into rat brain tubulin. Eur. J. Biochem. 59, 145–149 (1975).
  Article CAS PubMed Google Scholar
• Argarana, C. E., Arce, C. A., Barra, H. S. & Caputto, R. In vivo incorporation of [14C]tyrosine into the C-terminal position of the α subunit of tubulin. Arch. Biochem. Biophys. 180, 264–268 (1977).
  Article CAS PubMed Google Scholar
• Paturle-Lafanechere, L. et al. Characterization of a major brain tubulin variant which cannot be tyrosinated. Biochemistry 30, 10523–10528 (1991).
  Article CAS PubMed Google Scholar
• Rudiger, M., Wehland, J. & Weber, K. The carboxy-terminal peptide of detyrosinated α tubulin provides a minimal system to study the substrate specificity of tubulin-tyrosine ligase. Eur. J. Biochem. 220, 309–320 (1994).
  Article CAS PubMed Google Scholar
• Banerjee, A. Coordination of posttranslational modifications of bovine brain α-tubulin. Polyglycylation of δ2 tubulin. J. Biol. Chem. 277, 46140–46144 (2002).
  Article CAS PubMed Google Scholar
• Multigner, L. et al. The A and B tubules of the outer doublets of sea urchin sperm axonemes are composed of different tubulin variants. Biochemistry 35, 10862–10871 (1996).
  Article CAS PubMed Google Scholar
• Johnson, K. A. The axonemal microtubules of the Chlamydomonas flagellum differ in tubulin isoform content. J. Cell Sci. 111, 313–320 (1998).
  Article CAS PubMed Google Scholar
• Bre, M. H. et al. Axonemal tubulin polyglycylation probed with two monoclonal antibodies: widespread evolutionary distribution, appearance during spermatozoan maturation and possible function in motility. J. Cell Sci. 109, 727–738 (1996).
  Article CAS PubMed Google Scholar
• Huitorel, P. et al. Differential distribution of glutamylated tubulin isoforms along the sea urchin sperm axoneme. Mol. Reprod. Dev. 62, 139–148 (2002).
  Article CAS PubMed Google Scholar
• Murofushi, H. Purification and characterization of tubulin-tyrosine ligase from porcine brain. J. Biochem. 87, 979–984 (1980).
  Article CAS PubMed Google Scholar
• Ersfeld, K. et al. Characterization of the tubulin-tyrosine ligase. J. Cell Biol. 120, 725–732 (1993).
  Article CAS PubMed Google Scholar
• Galperin, M. Y. & Koonin, E. V. A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity. Protein Sci. 6, 2639–2643 (1997).
  Article CAS PubMed PubMed Central Google Scholar
• Argarana, C. E., Barra, H. S. & Caputto, R. Tubulinyl-tyrosine carboxypeptidase from chicken brain: properties and partial purification. J. Neurochem. 34, 114–118 (1980).
  Article CAS PubMed Google Scholar
• Wehland, J. & Weber, K. Turnover of the carboxy-terminal tyrosine of α-tubulin and means of reaching elevated levels of detyrosination in living cells. J. Cell Sci. 88, 185–203 (1987).
  Article CAS PubMed Google Scholar
• Webster, D. R., Gundersen, G. G., Bulinski, J. C. & Borisy, G. G. Assembly and turnover of detyrosinated tubulin in vivo. J. Cell Biol. 105, 265–276 (1987).
  Article CAS PubMed Google Scholar
• Webster, D. R., Wehland, J., Weber, K. & Borisy, G. G. Detyrosination of α tubulin does not stabilize microtubules in vivo. J. Cell Biol. 111, 113–122 (1990).
  Article CAS PubMed Google Scholar
• Cook, T. A., Nagasaki, T. & Gundersen, G. G. Rho guanosine triphosphatase mediates the selective stabilization of microtubules induced by lysophosphatidic acid. J. Cell Biol. 141, 175–185 (1998).
  Article CAS PubMed PubMed Central Google Scholar
• Palazzo, A. F., Cook, T. A., Alberts, A. S. & Gundersen, G. G. mDia mediates Rho-regulated formation and orientation of stable microtubules. Nature Cell Biol. 3, 723–729 (2001).
  Article CAS PubMed Google Scholar
• Infante, A. S., Stein, M. S., Zhai, Y., Borisy, G. G. & Gundersen, G. G. Detyrosinated (Glu) microtubules are stabilized by an ATP-sensitive plus-end cap. J. Cell Sci. 113, 3907–3919 (2000).
  Article CAS PubMed Google Scholar
• Gurland, G. & Gundersen, G. G. Stable, detyrosinated microtubules function to localize vimentin intermediate filaments in fibroblasts. J. Cell Biol. 131, 1275–1290 (1995).
  Article CAS PubMed Google Scholar
• Liao, G. & Gundersen, G. G. Kinesin is a candidate for cross-bridging microtubules and intermediate filaments. Selective binding of kinesin to detyrosinated tubulin and vimentin. J. Biol. Chem. 273, 9797–9803 (1998).
  Article CAS PubMed Google Scholar
• Kreitzer, G., Liao, G. & Gundersen, G. G. Detyrosination of tubulin regulates the interaction of intermediate filaments with microtubules in vivo via a kinesin-dependent mechanism. Mol. Biol. Cell 10, 1105–1118 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Lafanechere, L. et al. Suppression of tubulin tyrosine ligase during tumor growth. J. Cell Sci. 111, 171–181 (1998).
  Article CAS PubMed Google Scholar
• Mialhe, A. et al. Tubulin detyrosination is a frequent occurrence in breast cancers of poor prognosis. Cancer Res. 61, 5024–5027 (2001).
  CAS PubMed Google Scholar
• Eiserich, J. P. et al. Microtubule dysfunction by posttranslational nitrotyrosination of α-tubulin: a nitric oxide-dependent mechanism of cellular injury. Proc. Natl Acad. Sci. USA 96, 6365–6370 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Kalisz, H. M., Erck, C., Plessmann, U. & Wehland, J. Incorporation of nitrotyrosine into α-tubulin by recombinant mammalian tubulin-tyrosine ligase. Biochim. Biophys. Acta 1481, 131–138 (2000).
  Article CAS PubMed Google Scholar
• Chang, W. et al. Alteration of the C-terminal amino acid of tubulin specifically inhibits myogenic differentiation. J. Biol. Chem. 277, 30690–30698 (2002).
  Article CAS PubMed Google Scholar
• Eipper, B. A. Properties of rat brain tubulin. J. Biol. Chem. 249, 1407–1416 (1974).
  Article CAS PubMed Google Scholar
• Gard, D. L. & Kirschner, M. W. A polymer-dependent increase in phosphorylation of β-tubulin accompanies differentiation of a mouse neuroblastoma cell line. J. Cell Biol. 100, 764–774 (1985).
  Article CAS PubMed Google Scholar
• Caron, J. M. Posttranslational modification of tubulin by palmitoylation: I. In vivo and cell-free studies. Mol. Biol. Cell 8, 621–636 (1997).
  Article CAS PubMed PubMed Central Google Scholar
• Ozols, J. & Caron, J. M. Posttranslational modification of tubulin by palmitoylation: II. Identification of sites of palmitoylation. Mol. Biol. Cell 8, 637–645 (1997).
  Article CAS PubMed PubMed Central Google Scholar
• Caron, J. M., Vega, L. R., Fleming, J., Bishop, R. & Solomon, F. Single site α-tubulin mutation affects astral microtubules and nuclear positioning during anaphase in Saccharomyces cerevisiae: possible role for palmitoylation of α-tubulin. Mol. Biol. Cell 12, 2672–2687 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Sisson, J. C., Ho, K. S., Suyama, K. & Scott, M. P. Costal2, a novel kinesin-related protein in the Hedgehog signaling pathway. Cell 90, 235–245 (1997).
  Article CAS PubMed Google Scholar
• Nogales, E., Downing, K. H., Amos, L. A. & Lowe, J. Tubulin and FtsZ form a distinct family of GTPases. Nature Struct. Biol. 5, 451–458 (1998).
  Article CAS PubMed Google Scholar
• McKean, P. G., Vaughan, S. & Gull, K. The extended tubulin superfamily. J. Cell Sci. 114, 2723–2733 (2001).
  Article CAS PubMed Google Scholar
• Dupuis-Williams, P. et al. Functional role of ε-tubulin in the assembly of the centriolar microtubule scaffold. J. Cell Biol. 158, 1183–1193 (2002).
  Article CAS PubMed PubMed Central Google Scholar
• Vinh, J. et al. Structural characterization by tandem mass spectrometry of the posttranslational polyglycylation of tubulin. Biochemistry 38, 3133–3139 (1999).
  Article CAS PubMed Google Scholar
• Vinh, J., Loyaux, D., Redeker, V. & Rossier, J. Sequencing branched peptides with CID/PSD MALDI-TOF in the low–picomole range: application to the structural study of the posttranslational polyglycylation of tubulin. Anal. Chem. 69, 3979–3985 (1997).
  Article CAS PubMed Google Scholar