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St3gal6 and
St6gal1. Increased percentages of core-fucosylated and triantennary glycan moieties were seen in LDKO livers, and proteins with the “hyperglycoforms” preferentially localized to exosomes and lysosomes. This up-regulation of N-glycosylation machinery was specific to the Golgi apparatus and not the endoplasmic reticulum. The increased glycan complexity in the LDKO correlated well with dilated unstacked Golgi ribbons and alterations in the secretion of albumin, cholesterol, and triglycerides. Our findings demonstrate a role for the FXR-SHP axis in maintaining glycoprotein diversity in the liver.
INTRODUCTION
N-Glycosylation is a key posttranslational modification that decides the fate of several liver proteins, including their targeting to the plasma membrane or for secretion. Briefly, various combinations of sugar molecules (glycan moieties) attach covalently to the nitrogen of asparagine residues of a protein ( ....

United States , Miltenyi Biotec , Envigo Harlan , Trizol Invitrogen , Milliporesigma Amicon , Vectashield Hardset , Institute For Genomic Biology , Carbohydrate Research Center , Royj Carver Biotechnology Center , National Glycoscience Resource , Perelman School Of Medicine , University Of Illinois , National Academy Of Sciences , Cell Signaling Technology , Material Sciences Laboratory For Electron , Cor Image Studio Software , American Cancer Society , Laboratory Animals , Institute For Genomic Biology Core , Committee At University Of Illinois Urbana Champaign , University Of Georgia , Biosciences Histology Laboratory , University Of Pennsylvania , University Of Illinois At Urbana Champaign , National Academy , Institutional Animal Care ,