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TitleStructural basis of regulated N-glycosylation at the secretory translocon.
Journal, issue, pagesNature, Vol. 649, Issue 8097, Page 777-784, Year 2026
Publish dateNov 19, 2025
AuthorsMelvin Yamsek / Mengxiao Ma / Roshan Jha / Yu Wan / Qianru Li / Frank Zhong / Katherine DeLong / Zhe Ji / Rajat Rohatgi / Robert J Keenan /
PubMed AbstractMost human secretory pathway proteins are N-glycosylated by oligosaccharyltransferase (OST) complexes as they enter the endoplasmic reticulum (ER). Recent work revealed a substrate-assisted mechanism ...Most human secretory pathway proteins are N-glycosylated by oligosaccharyltransferase (OST) complexes as they enter the endoplasmic reticulum (ER). Recent work revealed a substrate-assisted mechanism by which N-glycosylation of the chaperone glucose-regulated protein 94 (GRP94) is regulated to control cell surface receptor signalling. Here we report the structure of a natively isolated GRP94 folding intermediate tethered to a specialized CCDC134-bound translocon. Together with functional analysis, the data reveal how a conserved N-terminal extension in GRP94 inhibits OST-A and how structural rearrangements within the translocon shield the tethered nascent chain from inappropriate OST-B glycosylation. These interactions depend on a hydrophobic CCDC134 groove, which recognizes a non-native conformation of nascent GRP94. Our results define a mechanism of regulated N-glycosylation and illustrate how the nascent chain remodels the translocon to facilitate its own biogenesis.
External linksNature / PubMed:41261126 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 4.1 Å
Structure data

49171

9n9j

EMDB-49171, PDB-9n9j:
Structure of a GRP94 folding intermediate engaged with a CCDC134- and FKBP11-bound secretory translocon
Method: EM (single particle) / Resolution: 3.2 Å

72945

9ygy

EMDB-72945, PDB-9ygy:
Structure of a GRP94 folding intermediate engaged with a CCDC134- and FKBP11-bound secretory translocon
Method: EM (single particle) / Resolution: 4.1 Å

Chemicals

ChemComp-ELU:
phosphono [(3~{R},6~{E},10~{E})-3,7,11,15-tetramethylhexadeca-6,10,14-trienyl] hydrogen phosphate

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsRIBOSOME / Membrane protein / Translocon / Transport / N-Glycosylation

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