Evidence for new C-terminally truncated variants of α- and β-tubulins
Aillaud, Chrystelle (Université Grenoble Alpes. Grenoble Institut des Neurosciences)
Bosc, Christophe (Université Grenoble Alpes. Grenoble Institut des Neurosciences)
Saoudi, Yasmina (Université Grenoble Alpes. Grenoble Institut des Neurosciences)
Denarier, Eric (Université Grenoble Alpes. Grenoble Institut des Neurosciences)
Peris, Leticia (Université Grenoble Alpes. Grenoble Institut des Neurosciences)
Sago, Laila (Centre national de la recherche scientifique. Service d'Identification et de Caractérisation des Protéines par Spectrométrie de masse)
Taulet, Nicolas (Centre national de la recherche scientifique. Centre de Recherche de Biochimie Macromoléculaire)
Cieren, Adeline (Université Grenoble Alpes. Grenoble Institut des Neurosciences)
Tort, Olívia (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Magiera, Maria M. (Institut Curie)
Janke, Carsten (Institut Curie)
Redeker, Virginie (Paris-Saclay Institute of Neuroscience)
Andrieux, Annie (Université Grenoble Alpes. Grenoble Institut des Neurosciences)
Moutin, Marie-Jo (Université Grenoble Alpes. Grenoble Institut des Neurosciences)

Data:	2016
Resum:	New C-terminally truncated α- and β-tubulin variants, both ending with an -EEEG sequence, are identified in vivo: αΔ3-tubulin, which has a specific neuronal distribution pattern (distinct from that of αΔ2-tubulin) and seems to be related to dynamic microtubules, and βΔ4-tubulin, corresponding to β2A/B-tubulin modified by truncation of four C-terminal residues, which is ubiquitously present in cells and tissues. Cellular α-tubulin can bear various carboxy-terminal sequences: full-length tubulin arising from gene neosynthesis is tyrosinated, and two truncated variants, corresponding to detyrosinated and Δ2 α‑tubulin, result from the sequential cleavage of one or two C-terminal residues, respectively. Here, by using a novel antibody named 3EG that is highly specific to the -EEEG C-terminal sequence, we demonstrate the occurrence in neuronal tissues of a new αΔ3‑tubulin variant corresponding to α1A/B‑tubulin deleted of its last three residues (EEY). αΔ3‑tubulin has a specific distribution pattern: its quantity in the brain is similar to that of αΔ2-tubulin around birth but is much lower in adult tissue. This truncated α1A/B-tubulin variant can be generated from αΔ2-tubulin by the deglutamylases CCP1, CCP4, CCP5, and CCP6 but not by CCP2 and CCP3. Moreover, using 3EG antibody, we identify a C‑terminally truncated β-tubulin form with the same -EEEG C-terminal sequence. Using mass spectrometry, we demonstrate that β2A/B-tubulin is modified by truncation of the four C-terminal residues (EDEA). We show that this newly identified βΔ4-tubulin is ubiquitously present in cells and tissues and that its level is constant throughout the cell cycle. These new C-terminally truncated α- and β-tubulin variants, both ending with -EEEG sequence, are expected to regulate microtubule physiology. Of interest, the αΔ3-tubulin seems to be related to dynamic microtubules, resembling tyrosinated-tubulin rather than the other truncated variants, and may have critical function(s) in neuronal development.
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Llengua:	Anglès
Document:	Article ; recerca ; Versió publicada
Publicat a:	Molecular biology of the cell, Vol. 27, issue 4 (Feb. 2016) , p. 640-653, ISSN 1939-4586

DOI: 10.1091/mbc.E15-03-0137
PMID: 26739754

14 p, 3.3 MB

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Documents de recerca > Documents dels grups de recerca de la UAB > Centres i grups de recerca (producció científica) > Ciències de la salut i biociències > Institut de Biotecnologia i de Biomedicina (IBB)
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