Brokate Llanos, Ana MaríaMonje, José Manueldel Socorro Murdoch, PiedadMuñoz Ruiz, Manuel Jesús2025-04-212025-04-212014-10-08Genetics, Volume 198, Issue 4, 1 December 2014, Pages 1559–1569,10.1534/genetics.114.170084https://hdl.handle.net/10433/23795This work was supported by the Junta de Andalucía (P07-CVI-02697) and the Spanish Ministry of Science and Innovation (BFU2006-07391/BMC) and Ministry of Economy and Competitiveness (BFU2013-46923-P). A.M.B.-L. was supported by a Plan Propio de Investigación fellowship from the Universidad Pablo de Olavide. J.M.M. was supported by the Formación del personal Universitario program of the Spanish Ministry of Science and Innovation.Type III galactosemia is a metabolic disorder caused by reduced activity of UDP-galactose-4-epimerase, which participates in galactose metabolism and the generation of various UDP-sugar species. We characterized gale-1 in Caenorhabditis elegans and found that a complete loss-of-function mutation is lethal, as has been hypothesized for humans, whereas a nonlethal partial loss-of-function allele causes a variety of developmental abnormalities, likely resulting from the impairment of the glycosylation process. We also observed that gale-1 mutants are hypersensitive to galactose as well as to infections. Interestingly, we found interactions between gale-1 and the unfolded protein response.application/pdfenAttribution-NonCommercial-NoDerivatives 4.0 Internationalhttp://creativecommons.org/licenses/by-nc-nd/4.0/Caenorhabditis elegansGalactosemia type IIIGlycosylationGALEUnfolded protein responsejournal articlerestricted access