par Ngale Njume, Ferdinand;Razzauti Sanfeliu, Adrià
;Soler García, Miguel
;Perschin, Veronika;Fazeli, Gholamreza;Bourez, Axelle
;Delporte, Cédric
;Ghogomu Mbigha, Stephen
;Poelvoorde, Philippe
;Pichard, Simon;Birck, Catherine;Poterszman, Arnaud;Souopgui, Jacob
;Van Antwerpen, Pierre
;Stigloher, Christian;Vanhamme, Luc
;Laurent, Patrick 
Référence iScience, 25, 11, page (105357)
Publication Publié, 2022-11-01










Référence iScience, 25, 11, page (105357)
Publication Publié, 2022-11-01
Article révisé par les pairs
Résumé : | The cuticle of C. elegans is impermeable to chemicals, toxins, and pathogens. However, increased permeability is a desirable phenotype because it facilitates chemical uptake. Surface lipids contribute to the permeability barrier. Here, we identify the lipid transfer protein GMAP-1 as a critical element setting the permeability of the C. elegans cuticle. A gmap-1 deletion mutant increases cuticular permeability to sodium azide, levamisole, Hoechst, and DiI. Expressing GMAP-1 in the hypodermis or transiently in the adults is sufficient to rescue this gmap-1 permeability phenotype. GMAP-1 protein is secreted from the hypodermis to the aqueous fluid filling the space between collagen fibers of the cuticle. In vitro, GMAP-1 protein binds phosphatidylserine and phosphatidylcholine while in vivo, GMAP-1 sets the surface lipid composition and organization. Altogether, our results suggest GMAP-1 secreted by hypodermis shuttles lipids to the surface to form the permeability barrier of C. elegans. |