RFT1 Protein Affects Glycosylphosphatidylinositol (GPI) Anchor Glycosylation.

ABSTRACT: The membrane protein RFT1 is essential for normal protein N-glycosylation, but its precise function is not known. RFT1 was originally proposed to translocate the glycolipid Man₅GlcNAc₂-PP-dolichol (needed to synthesize N-glycan precursors) across the endoplasmic reticulum membrane, but subsequent studies showed that it does not play a direct role in transport. In contrast to the situation in yeast, RFT1 is not essential for growth of the parasitic protozoan Trypanosoma brucei, enabling the study of its function in a null background. We now report that lack of T. brucei RFT1 (TbRFT1) not only affects protein N-glycosylation but also glycosylphosphatidylinositol (GPI) anchor side-chain modification. Analysis by immunoblotting, metabolic labeling, and mass spectrometry d

SUBMITTER: Gottier P 

PROVIDER: S-EPMC5247644 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature