title: Activity Detection of GalNAc Transferases by Protein-Based Fluorescence Sensors In Vivo.
abstract: Mucin-type O-glycosylation occurring in the Golgi apparatus is an important protein posttranslational modification initiated by up to 20 GalNAc-transferase isozymes with largely distinct substrate specificities. Regulation of this enzyme family affects a vast array of proteins transiting the secretory pathway and misregulation causes human diseases. Here we describe the use of protein-based fluorescence sensors that traffic in the secretory pathway to monitor GalNAc-transferase activity in living cells. The sensors can either be "pan" or isozyme specific.
authors.affiliation: Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA, 15213, USA.
authors.forename: Lina
authors.initials: L
authors.lastname: Song
authors.affiliation: Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA, 15213, USA.
authors.forename: Collin
authors.initials: C
authors.lastname: Bachert
authors.affiliation: Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA, 15213, USA. linstedt@cmu.edu.
authors.forename: Adam D
authors.initials: AD
authors.lastname: Linstedt
mesh_terms: D015374:Biosensing Techniques / Q000379:methods*; D057809:HEK293 Cells; D006801:Humans; D008856:Microscopy, Fluorescence / Q000379:methods; D017350:N-Acetylgalactosaminyltransferases / Q000235:genetics / Q000378:metabolism*; D000097763:Polypeptide N-acetylgalactosaminyltransferase
chemical_list: D017350:N-Acetylgalactosaminyltransferases; D000097763:Polypeptide N-acetylgalactosaminyltransferase
keywords: Fluorescence-activating protein; Fluorescent biosensor; GalNAc transferase; O-glycosylation