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PXD060914

PXD060914 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleSND3 is the membrane insertase within a distinct SEC61 translocon complex
DescriptionDuring the biogenesis of most eukaryotic integral membrane proteins (IMPs), transmembrane domains are inserted into the endoplasmic reticulum membrane by a dedicated insertase or the SEC61 translocon. The SRP-independent (SND) pathway is the least understood route into the membrane, despite catering for a broad range of IMP types. Here, we show that Chaetomium thermophilum SND3 is a membrane insertase with an atypical fold. We further present a cryo-electron microscopy structure of a ribosome-associated SND3 translocon complex involved in co-translational IMP insertion. The structure reveals that the SND3 translocon additionally comprises the complete SEC61 translocon, CCDC47 and TRAPɑ. Here, the SEC61β N-terminus works together with CCDC47 to prevent substrate access to the translocon. Instead, molecular dynamics simulations show that SND3 disrupts the lipid bilayer to promote IMP insertion via its membrane-embedded hydrophilic groove. Structural and sequence comparisons indicate that the SND3 translocon is a distinct multipass translocon in fungi, euglenozoan parasites and other eukaryotic taxa.
HostingRepositoryPRIDE
AnnounceDate2025-09-24
AnnouncementXMLSubmission_2025-09-24_09:21:07.297.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterJulian Langer
SpeciesList scientific name: Chaetomium thermophilum; NCBI TaxID: 209285;
ModificationListmonohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
InstrumentOrbitrap Eclipse; timsTOF HT
Dataset History
RevisionDatetimeStatusChangeLog Entry
02025-02-18 03:09:09ID requested
12025-09-24 09:21:07announced
Publication List
Dataset with its publication pending
Keyword List
submitter keyword: proteomics, multipass translocon, membrane insertase,SND3
Contact List
Julian Langer
contact affiliationMax Planck Institute of Biophysics
contact emailjulian.langer@biophys.mpg.de
lab head
Julian Langer
contact affiliationMPIs for Biophysics and Brain Research
contact emailjulian.langer@biophys.mpg.de
dataset submitter
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Dataset FTP location
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