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Tag: Glycosylation

Glycoregulation of E3(SCF) ubiquitin ligases in unicellular eukaryotes

Skp1 is an essential adaptor within the Skp1/Cul1/F-box (SCF) class of E3 polyubiquitin ligases that regulate protein degradation in all eukaryotes. Skp1 is also a target of a 5-enzyme glycosylation pathway in parasites and other unicellular eukaryotes. Glycosylation of Skp1 is contingent upon oxygen-dependent hydroxylation of a critical Pro residue by a homolog of the …

UGA biochemists create new tool to study biological process in parasites

Click on image below to view photo gallery with captions. Researchers in the University of Georgia’s West Laboratory are interested in how unicellular parasites thrive in their environments. Focusing on post-translational modifications of proteins, particularly a crucial process called glycosylation, researchers are gaining insights into how this basic life process in parasites can lead to better …

Oxygen-dependent regulation of F-box proteins in Toxoplasma gondii is mediated by Skp1 glycosylation

  A dynamic proteome is required for cellular adaption to changing environments including levels of O2, and the SKP1/CULLIN-1/F-box protein/RBX1 (SCF) family of E3 ubiquitin ligases contributes importantly to proteasome-mediated degradation. We examine, in the apicomplexan parasite Toxoplasma gondii, the influence on the interactome of SKP1 by its novel glycan attached to a hydroxyproline generated …

Glycomics, Glycoproteomics and Glycogenomics: an Inter-Taxa Evolutionary Perspective

Glycosylation is a highly diverse set of co- and post-translational modification of proteins. For mammalian glycoproteins, glycosylation is often site-, tissue- and species-specific, and diversified by microheterogeneity. Multitudinous biochemical, cellular, physiological and organismic effects of their glycans have been revealed, either intrinsic to the carrier proteins or mediated by endogenous reader proteins with carbohydrate recognition …