The C. elegans deglutamylase CCPP-6 does not operate redundantly with CCPP-1 in gross cilia integrity

Tubulin glutamylation is a reversible modification of the microtubules that regulates cilia stability and function. The addition of glutamates to the microtubule is catalyzed by members of the TTLL family of enzymes, while the removal is carried out by a family of cytosolic carboxypeptidase (CCP) en...

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Detalles Bibliográficos
Autores principales: Klimas, Abigail S, Dominguez, Jessica, Shah, Bhumi P, Lee, Zion Y, Peel, Nina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Caltech Library 2023
Materias:
New Finding
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10242412/
https://www.ncbi.nlm.nih.gov/pubmed/37287505
http://dx.doi.org/10.17912/micropub.biology.000740
Descripción
Sumario:Tubulin glutamylation is a reversible modification of the microtubules that regulates cilia stability and function. The addition of glutamates to the microtubule is catalyzed by members of the TTLL family of enzymes, while the removal is carried out by a family of cytosolic carboxypeptidase (CCP) enzymes. C. elegans has two deglutamylating enzymes, CCPP-1 and CCPP-6 . CCPP-1 is required for ciliary stability and function in the worm, however CCPP-6 is dispensable for cilia integrity. To investigate redundancy between the two deglutamylating enzymes we made a ccpp-1 ( ok1821 ); ccpp-6 ( ok382 ) double mutant. The double mutant shows normal viability, and the dye-filling phenotypes are not worse than the ccpp-1 single mutant, suggesting that CCPP-1 and CCPP-6 do not function redundantly in C. elegans cilia .

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