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ProteomicsA novel translocon for biogenesis of multi-pass membrane proteins
A novel 370 kDa translocon comprising Sec61 and five accessory factors acting co-translationally with ribosomes to fold and insert multi-pass membrane proteins was identified, purified and analyzed structurally by single particle cryo-EM and cross-linking mass spectrometry. The purified ribosome-tr...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2019-07-08 | MSV000084065 | MassIVE
ProteomicsLipid Scrambling Pathways in the Sec61 Translocon Complex
Maintenance of cellular homeostasis and functionality requires rapid translocation of newly synthesized lipids across the membrane leaflets of the endoplasmic reticulum (ER) where majority of cellular lipid biosynthesis takes place. This process is facilitated without the need for ATP by specific me...
ORGANISM(S): Ovis canadensis sierrae 
2025-05-26 | PXD062310 | Pride
Translocon complex Sec61 
GenomicsTranslocon remodeling during protein synthesis at the ER
Translocon remodeling during protein synthesis at the ER
PRJNA1265091 | ENA
ProteomicsSND3 is the membrane insertase within a distinct SEC61 translocon complex
During 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...
ORGANISM(S): Chaetomium thermophilum 
2025-09-24 | PXD060914 | Pride
Proteomics Multipass translocon Membrane insertase Snd3 
GenomicsStructural basis of regulated N-glycosylation at the secretory translocon
Structural basis of regulated N-glycosylation at the secretory translocon
PRJNA1295541 | ENA
ProteomicsStructural basis of gate dynamics at the outer membrane lipopolysaccharide holo-translocon
Gram-negative bacteria resist many harmful chemicals, protected by an asymmetric outer membrane (OM) containing lipopolysaccharide (LPS) in its external leaflet. Leaflet-selective assembly of LPS is an essential, yet mechanistically elusive process. This reaction is mediated by the OM LPS core trans...
ORGANISM(S): Escherichia coli 
2025-12-01 | PXD068376 | Pride
Lps translocon Native ms Gel digestion 
OtherTranslocon remodeling during protein synthesis at the ER
Protein biogenesis at the endoplasmic reticulum (ER) is coordinated by the Sec61 translocon whose dynamic subunit composition is essential for maintaining a functional proteome. How nascent secretory and membrane proteins recruit accessory factors to the translocon, and what controls the interplay b...
ORGANISM(S): Homo sapiens 
2025-08-30 | GSE297497 | GEO
ProteomicsFlavobacterium T9SS Extended Translocon
Secretion Systems are protein export machines that enable bacteria to exploit their environment through the release of protein effectors. The Type 9 Secretion System (T9SS) is responsible for protein export across the outer membrane (OM) of bacteria of the phylum Bacteroidota. Here we use deletion o...
ORGANISM(S): Flavobacterium johnsoniae UW101 
2024-03-05 | PXD049165 | Pride
Bacteroidetes Type 9 secretion system 
ProteomicsThe SecYEG interactome of E. coli: non-competitive binding of PpiD and YidC to the SecYEG translocon
The SecYEG translocon constitutes the major protein transporting channel in bacteria and transports an enormous variety of different secretory and inner membrane proteins. The minimal core of the SecYEG translocon consists of the three inner membrane proteins SecY, SecE and SecG, which together with...
ORGANISM(S): Escherichia coli 
2019-11-07 | PXD015974 | Pride
Yidc Ppid Label-free proteomics Secyeg translocon Protein cross-linking 
OtherStructural basis of regulated N-glycosylation at the secretory translocon
Most human secretory pathway proteins are N-glycosylated by oligosaccharyltransferase complexes as they enter the endoplasmic reticulum. Recent work revealed a substrate-assisted mechanism by which N-glycosylation of the chaperone GRP94 is regulated to control cell surface receptor signaling. Here w...
ORGANISM(S): Homo sapiens 
2025-09-27 | GSE303507 | GEO
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