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Signal recognition particle receptor-β (SR-β) coordinates cotranslational N-glycosylation.

Chatchai PhoomakNatalie RinisMarta BaroShiteshu ShrimalDaniel BennettScott A ShafferMark LehrmanReid GilmoreJoseph N Contessa
Published in: Science advances (2023)
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.
Keyphrases
  • endoplasmic reticulum
  • smoking cessation
  • human milk
  • small molecule
  • single molecule
  • low birth weight
  • preterm infants
  • cell therapy
  • protein protein