AI Article Synopsis
- * The study reveals that the [Formula: see text] subunit of the signal recognition particle receptor (SR) is essential for creating a translocon that can facilitate N-glycosylation.
- * Chemical probes and mutations affecting the SR-[Formula: see text] binding site lead to a lack of N-glycosylation without disrupting its connection to other SR subunits, highlighting the SR-[Formula: see text]'s new role in linking protein translation with glycosylation within the endoplasmic ret
Article 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.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10017033 | PMC |
| http://dx.doi.org/10.1126/sciadv.ade8079 | DOI Listing |
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