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Functional role of ɛ-tubulin in the assembly of the centriolar microtubule scaffold

Centrioles and basal bodies fascinate by their spectacular architecture, featuring an arrangement of nine microtubule triplets into an axial symmetry, whose biogenesis relies on yet elusive mechanisms. However, the recent discovery of new tubulins, such as δ-, ɛ-, or η-tubulin, could constitute a br...

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Detalles Bibliográficos
Autores principales: Dupuis-Williams, Pascale, Fleury-Aubusson, Anne, de Loubresse, Nicole Garreau, Geoffroy, Hélène, Vayssié, Laurence, Galvani, Angélique, Espigat, Aude, Rossier, Jean
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2002
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173240/
https://www.ncbi.nlm.nih.gov/pubmed/12356863
http://dx.doi.org/10.1083/jcb.200205028
Descripción
Sumario:Centrioles and basal bodies fascinate by their spectacular architecture, featuring an arrangement of nine microtubule triplets into an axial symmetry, whose biogenesis relies on yet elusive mechanisms. However, the recent discovery of new tubulins, such as δ-, ɛ-, or η-tubulin, could constitute a breakthrough for deciphering the assembly steps of this unconventional microtubule scaffold. Here, we report the functional analysis in vivo of ɛ-tubulin, based on gene silencing in Paramecium, which demonstrates that this protein, which localizes at the basal bodies, is essential for the assembly and anchorage of the centriolar microtubules.