O₂ sensing-associated glycosylation exposes the F-box-combining site of the Dictyostelium Skp1 subunit in E3 ubiquitin ligases.

ABSTRACT: Skp1 is a conserved protein linking cullin-1 to F-box proteins in SCF (Skp1/Cullin-1/F-box protein) E3 ubiquitin ligases, which modify protein substrates with polyubiquitin chains that typically target them for 26S proteasome-mediated degradation. In Dictyostelium (a social amoeba), Toxoplasma gondii (the agent for human toxoplasmosis), and other protists, Skp1 is regulated by a unique pentasaccharide attached to hydroxylated Pro-143 within its C-terminal F-box-binding domain. Prolyl hydroxylation of Skp1 contributes to O₂-dependent Dictyostelium development, but full glycosylation at that position is required for optimal O₂ sensing. Previous studies have shown that the glycan promotes organization of the F-box-binding region

SUBMITTER: Sheikh MO 

PROVIDER: S-EPMC5704474 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature