Signal recognition particle receptor-ß (SR-ß) coordinates cotranslational N-glycosylation.
Sci Adv
; 9(11): eade8079, 2023 03 17.
Article
in En
| MEDLINE
| ID: mdl-36921042
ABSTRACT
Proteins destined for the secretory compartment of the cell are cotranslationally translocated into the endoplasmic reticulum. The majority of these proteins are N-glycosylated, a co- and posttranslational modification that ensures proper protein folding, stability, solubility, and cellular localization. Here, we show that the [Formula see text] subunit of the signal recognition particle receptor (SR) is required for assembly of the N-glycosylation-competent translocon. We report that guanine analog chemical probes identified by high-throughput screening or mutation of the SR-[Formula see text] guanosine triphosphate binding site cause an N-glycosylation-deficient phenotype. Neither method alters the association of SR-[Formula see text] with SR-[Formula see text], but both approaches reduce the association of SR-[Formula see text] with the oligosaccharyltransferase complex. These experiments demonstrate that SR-[Formula see text] has a previously unrecognized function coordinating endoplasmic reticulum translation with N-glycosylation.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Receptors, Cytoplasmic and Nuclear
/
Endoplasmic Reticulum
Language:
En
Journal:
Sci Adv
Year:
2023
Document type:
Article
Affiliation country:
United States
Publication country:
EEUU
/
ESTADOS UNIDOS
/
ESTADOS UNIDOS DA AMERICA
/
EUA
/
UNITED STATES
/
UNITED STATES OF AMERICA
/
US
/
USA