Glycosylation Weakens Skp1 Homodimerization in <i>Toxoplasma gondii</i> by Interrupting a Fuzzy Interaction.

ABSTRACT: Skp1/Cullin-1/F-Box protein (SCF) complexes represent a major class of E3 ubiquitin ligases responsible for proteomic control throughout eukaryotes. Target specificity is mediated by a large set of F-box proteins (FBPs) whose F-box domains interact with Skp1 in a conserved, well-organized fashion. In the social amoeba Dictyostelium, Skp1 is regulated by oxygen-dependent glycosylation which alters Skp1's FBP interactome and inhibits homodimerization that is mediated in part by an ordered interface which overlaps with that of FBPs. Based on sedimentation velocity experiments, Skp1 from the intracellular pathogen Toxoplasma gondii exhibits a homodimerization K_d comparable to that of a previously measured FBP/Skp1 interaction. Glycosylation of Skp1's disordered

SUBMITTER: Cantrell DA 

PROVIDER: S-EPMC12101541 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature