Polyglutamylation des microtubules et neurodégénérescence

Marie-Jo Moutin; Annie Andrieux; Carsten Janke

doi:10.1051/medsci/2011275006

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Volume 27 / Numéro 5 (Mai 2011)

Med Sci (Paris), 27 5 (2011) 464-467

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Numéro		Med Sci (Paris) Volume 27, Numéro 5, Mai 2011


Page(s)		464 - 467
Section		Nouvelles
DOI		https://doi.org/10.1051/medsci/2011275006
Publié en ligne		25 mai 2011

Edde B, Rossier J, Le Caer JP, et al. Posttranslational glutamylation of alpha-tubulin. Science 1990 ; 247 : 83-85. [CrossRef] [PubMed] [Google Scholar]
Janke C, Rogowski K, Wloga D, et al. Tubulin polyglutamylase enzymes are members of the TTL domain protein family. Science 2005 ; 308 : 1758-1762. [CrossRef] [PubMed] [Google Scholar]
Van Dijk J, Rogowski K, Miro J, et al. A targeted multienzyme mechanism for selective microtubule polyglutamylation. Mol Cell 2007 ; 26 : 437-448. [CrossRef] [PubMed] [Google Scholar]
Ersfeld K, Wehland J, Plessmann U, et al. Characterization of the tubulin-tyrosine ligase. J Cell Biol 1993 ; 120 : 725-732. [CrossRef] [PubMed] [Google Scholar]
Rogowski K, Juge F, van Dijk J, et al. Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation. Cell 2009 ; 137 : 1076-1087. [CrossRef] [PubMed] [Google Scholar]
Wloga D, Webster DM, Rogowski K, et al. TTLL3 Is a tubulin glycine ligase that regulates the assembly of cilia. Dev Cell 2009 ; 16 : 867-876. [CrossRef] [PubMed] [Google Scholar]
Kalinina E, Biswas R, Berezniuk I, et al. A novel subfamily of mouse cytosolic carboxypeptidases. Faseb J 2007 ; 21 : 836-850. [CrossRef] [PubMed] [Google Scholar]
Rodriguez de la Vega M, Sevilla RG, Hermoso A, et al. Nna1-like proteins are active metallocarboxypeptidases of a new and diverse M14 subfamily. Faseb J 2007 ; 21 : 851-865. [CrossRef] [PubMed] [Google Scholar]
Rogowski K, van Dijk J, Magiera MM, et al. A family of protein-deglutamylating enzymes associated with neurodegeneration. Cell 2010 ; 143 : 564-578. [CrossRef] [PubMed] [Google Scholar]
Erck C, Peris L, Andrieux A, et al. A vital role of tubulin-tyrosine-ligase for neuronal organization. Proc Natl Acad Sci USA 2005 ; 102 : 7853-7858. [CrossRef] [Google Scholar]
Lafanechere L, Courtay-Cahen C, Kawakami T, et al. Suppression of tubulin tyrosine ligase during tumor growth. J Cell Sci 1998 ; 111 : 171-181. [PubMed] [Google Scholar]
Peris L, Thery M, Faure J, et al. Tubulin tyrosination is a major factor affecting the recruitment of CAP-Gly proteins at microtubule plus ends. J Cell Biol 2006 ; 174 : 839-849. [CrossRef] [PubMed] [Google Scholar]
Peris L, Wagenbach M, Lafanechere L, et al. Motor-dependent microtubule disassembly driven by tubulin tyrosination. J Cell Biol 2009 ; 185 : 1159-1166. [CrossRef] [PubMed] [Google Scholar]
Janke C, Rogowski K, van Dijk J. Polyglutamylation: a fine-regulator of protein function ? Protein modifications: beyond the usual suspects. EMBO Rep 2008 ; 9 : 636-641. [CrossRef] [PubMed] [Google Scholar]

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[1] Edde B, Rossier J, Le Caer JP, et al. Posttranslational glutamylation of alpha-tubulin. Science 1990 ; 247 : 83-85. [CrossRef] [PubMed] [Google Scholar]

[2] Janke C, Rogowski K, Wloga D, et al. Tubulin polyglutamylase enzymes are members of the TTL domain protein family. Science 2005 ; 308 : 1758-1762. [CrossRef] [PubMed] [Google Scholar]

[3] Van Dijk J, Rogowski K, Miro J, et al. A targeted multienzyme mechanism for selective microtubule polyglutamylation. Mol Cell 2007 ; 26 : 437-448. [CrossRef] [PubMed] [Google Scholar]

[4] Ersfeld K, Wehland J, Plessmann U, et al. Characterization of the tubulin-tyrosine ligase. J Cell Biol 1993 ; 120 : 725-732. [CrossRef] [PubMed] [Google Scholar]

[5] Rogowski K, Juge F, van Dijk J, et al. Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation. Cell 2009 ; 137 : 1076-1087. [CrossRef] [PubMed] [Google Scholar]

[6] Wloga D, Webster DM, Rogowski K, et al. TTLL3 Is a tubulin glycine ligase that regulates the assembly of cilia. Dev Cell 2009 ; 16 : 867-876. [CrossRef] [PubMed] [Google Scholar]

[7] Kalinina E, Biswas R, Berezniuk I, et al. A novel subfamily of mouse cytosolic carboxypeptidases. Faseb J 2007 ; 21 : 836-850. [CrossRef] [PubMed] [Google Scholar]

[8] Rodriguez de la Vega M, Sevilla RG, Hermoso A, et al. Nna1-like proteins are active metallocarboxypeptidases of a new and diverse M14 subfamily. Faseb J 2007 ; 21 : 851-865. [CrossRef] [PubMed] [Google Scholar]

[9] Rogowski K, van Dijk J, Magiera MM, et al. A family of protein-deglutamylating enzymes associated with neurodegeneration. Cell 2010 ; 143 : 564-578. [CrossRef] [PubMed] [Google Scholar]

[10] Erck C, Peris L, Andrieux A, et al. A vital role of tubulin-tyrosine-ligase for neuronal organization. Proc Natl Acad Sci USA 2005 ; 102 : 7853-7858. [CrossRef] [Google Scholar]

[11] Lafanechere L, Courtay-Cahen C, Kawakami T, et al. Suppression of tubulin tyrosine ligase during tumor growth. J Cell Sci 1998 ; 111 : 171-181. [PubMed] [Google Scholar]

[12] Peris L, Thery M, Faure J, et al. Tubulin tyrosination is a major factor affecting the recruitment of CAP-Gly proteins at microtubule plus ends. J Cell Biol 2006 ; 174 : 839-849. [CrossRef] [PubMed] [Google Scholar]

[13] Peris L, Wagenbach M, Lafanechere L, et al. Motor-dependent microtubule disassembly driven by tubulin tyrosination. J Cell Biol 2009 ; 185 : 1159-1166. [CrossRef] [PubMed] [Google Scholar]

[14] Janke C, Rogowski K, van Dijk J. Polyglutamylation: a fine-regulator of protein function ? Protein modifications: beyond the usual suspects. EMBO Rep 2008 ; 9 : 636-641. [CrossRef] [PubMed] [Google Scholar]