Evidence for the major role of PH4αEFB in the prolyl 4-hydroxylation of <i>Drosophila</i> collagen IV.

ABSTRACT: Collagens are fundamental components of extracellular matrices, requiring precise intracellular post-translational modifications for proper function. Among the modifications, prolyl 4-hydroxylation is critical to stabilise the collagen triple helix. In humans, this reaction is mediated by collagen prolyl 4-hydroxylases (P4Hs). While humans possess three genes encoding these enzymes (P4Hαs), Drosophila melanogaster harbour at least 26 candidates for collagen P4Hαs despite its simple genome, and it is poorly understood which of them are actually working on collagen in the fly. In this study, we addressed this question by carrying out thorough bioinformatic and biochemical analyses. We demonstrate that among the 26 potential collagen P4Hαs, PH4αEFB shares the highest homology with vert

SUBMITTER: Ishikawa Y 

PROVIDER: S-EPMC12340787 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature