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Skp1 isoforms are differentially modified by a dual function prolyl 4-hydroxylase/N-acety lglucosaminyltransferase in a plant pathogen

Skp1 is hydroxylated by an O(2)-dependent prolyl hydroxylase (PhyA) that contributes to O(2)-sensing in the social amoeba Dictyostelium and the mammalian pathogen Toxoplasma gondii. HO-Skp1 is subject to glycosylation and the resulting pentasaccharide affects Skp1 conformation in a way that influenc...

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Publicat a:Glycobiology
Autors principals: van der Wel, Hanke, Gas-Pascual, Elisabet, West, Christopher M
Format: Artigo
Idioma:Inglês
Publicat: Oxford University Press 2019
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Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC6774341/
https://ncbi.nlm.nih.gov/pubmed/31281925
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/glycob/cwz049
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