Regulated N-glycosylation controls chaperone function and receptor trafficking

One-fifth of human proteins are N-glycosylated in the endoplasmic reticulum (ER) by two oligosaccharyltransferases, OST-A and OST-B. Contrary to the prevailing view of N-glycosylation as a housekeeping function, we identified an ER pathway that modulates the activity of OST-A. Genetic analyses linke...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Science (American Association for the Advancement of Science) 2024-11, Vol.386 (6722), p.667-672
Hauptverfasser:	Ma, Mengxiao, Dubey, Ramin, Jen, Annie, Pusapati, Ganesh V, Singal, Bharti, Shishkova, Evgenia, Overmyer, Katherine A, Cormier-Daire, Valérie, Fedry, Juliette, Aravind, L, Coon, Joshua J, Rohatgi, Rajat
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Asparagine Cell surface Cell surface receptors Control stability Endoplasmic reticulum Endoplasmic Reticulum - metabolism Folding Glycosylation HEK293 Cells Hexosyltransferases - genetics Hexosyltransferases - metabolism HSP90 Heat-Shock Proteins - genetics HSP90 Heat-Shock Proteins - metabolism Humans Membrane proteins Membrane Proteins - genetics Membrane Proteins - metabolism Membrane trafficking Mice Molecular Chaperones - metabolism Phosphorylation Protein Folding Protein Transport Proteins Quality control Receptor mechanisms Receptor, IGF Type 1 - metabolism Receptors Signal quality Ubiquitination Wnt Signaling Pathway
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!