Artículos de revistas
Glycoprotein reglucosylation
Date
2005-04Registration in:
Trombetta, E. Sergio; Parodi, Armando José A.; Glycoprotein reglucosylation; Academic Press Inc Elsevier Science; Methods; 35; 4; 4-2005; 328-337
1046-2023
1095-9130
CONICET Digital
CONICET
Author
Trombetta, E. Sergio
Parodi, Armando José A.
Abstract
Proteins following the secretory pathway acquire their proper tertiary and in certain cases also quaternary structures in the endoplasmic reticulum (ER). Incompletely folded species are retained in the ER and eventually degraded. One of the molecular mechanisms by which cells achieve this conformational sorting is based on monoglucosylated N-glycans (Glc1Man5-9GlcNAc2) present on nascent glycoproteins in the ER. This chapter discusses two of the steps that regulate the abundance of such N-glycan structures, including glycoprotein deglucosylation (by glucosidase II) and reglucosylation (by the UDP-Glc:glycoprotein glucosyltransferase), as well as an overview of methods to evaluate the N-glycans prevalent during glycoprotein biogenesis in the ER.