Location, location, location: new insights into O-GalNAc protein glycosylation

TY - JOUR

T1 - Location, location, location: new insights into O-GalNAc protein glycosylation

AU - Gill, David J

AU - Clausen, Henrik

AU - Bard, Frederic

N1 - Copyright © 2010 Elsevier Ltd. All rights reserved.

PY - 2011/3/1

Y1 - 2011/3/1

N2 - O-GalNAc glycosylation of proteins confers essential structural, protective and signaling roles in eumetazoans. Addition of O-glycans onto proteins is an extremely complex process that regulates both sites of attachment and the types of oligosaccharides added. Twenty distinct polypeptide GalNAc-transferases (GalNAc-Ts) initiate O-glycosylation and fine-tuning their expression provides a mechanism for regulating this action. Recently, a new mode of regulation has emerged where activation of Src kinase selectively redistributes Golgi-localized GalNAc-Ts to the ER. This relocalization results in a strong increase in the density of O-glycan decoration. In this review, we discuss how different mechanisms can regulate the number and the types of O-glycans decorating proteins. In addition, we speculate how Src-dependent relocation of GalNAc-Ts could play an important role in cancerous cellular transformation.

AB - O-GalNAc glycosylation of proteins confers essential structural, protective and signaling roles in eumetazoans. Addition of O-glycans onto proteins is an extremely complex process that regulates both sites of attachment and the types of oligosaccharides added. Twenty distinct polypeptide GalNAc-transferases (GalNAc-Ts) initiate O-glycosylation and fine-tuning their expression provides a mechanism for regulating this action. Recently, a new mode of regulation has emerged where activation of Src kinase selectively redistributes Golgi-localized GalNAc-Ts to the ER. This relocalization results in a strong increase in the density of O-glycan decoration. In this review, we discuss how different mechanisms can regulate the number and the types of O-glycans decorating proteins. In addition, we speculate how Src-dependent relocation of GalNAc-Ts could play an important role in cancerous cellular transformation.

KW - Animals

KW - Glycoproteins

KW - Glycosylation

KW - Humans

KW - N-Acetylgalactosaminyltransferases

KW - Polysaccharides

KW - Protein Transport

KW - Substrate Specificity

U2 - 10.1016/j.tcb.2010.11.004

DO - 10.1016/j.tcb.2010.11.004

M3 - Review

C2 - 21145746

SN - 0962-8924

VL - 21

SP - 149

EP - 158

JO - Trends in Cell Biology

JF - Trends in Cell Biology

IS - 3

ER -