Caenorhabditis elegansglutamylating enzymes function redundantly in male mating

Autor: Timothy P. Salmon, Zachary K. Barth, Nina Peel, Jessica D. Lee, Ruchi V. Shah, Anar Naik, Megan M. Brewster, Daniel G. Chawla, Katherine E. Badecker
Rok vydání: 2016
Předmět:
Zdroj: Biology Open, Vol 5, Iss 9, Pp 1290-1298 (2016)
Biology Open
ISSN: 2046-6390
DOI: 10.1242/bio.017442
Popis: Microtubule glutamylation is an important modulator of microtubule function and has been implicated in the regulation of centriole stability, neuronal outgrowth and cilia motility. Glutamylation of the microtubules is catalyzed by a family of tubulin tyrosine ligase-like (TTLL) enzymes. Analysis of individual TTLL enzymes has led to an understanding of their specific functions, but how activities of the TTLL enzymes are coordinated to spatially and temporally regulate glutamylation remains relatively unexplored. We have undertaken an analysis of the glutamylating TTLL enzymes in C. elegans. We find that although all five TTLL enzymes are expressed in the embryo and adult worm, loss of individual enzymes does not perturb microtubule function in embryonic cell divisions. Moreover, normal dye-filling, osmotic avoidance and male mating behavior indicate the presence of functional amphid cilia and male-specific neurons. A ttll-4(tm3310); ttll-11(tm4059); ttll-5(tm3360) triple mutant, however, shows reduced male mating efficiency due to a defect in the response step, suggesting that these three enzymes function redundantly, and that glutamylation is required for proper function of the male-specific neurons.
Summary: Although mutations in individual microtubule glutamylating enzymes do not disrupt essential microtubule functions in C. elegans, combining mutations in three enzymes uncovers a redundant function for glutamylation in male mating.
Databáze: OpenAIRE