ReviewOpen biology2020
Understanding the mammalian TRAP complex function(s).
Review in Open biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- The TRAP complex (SSR1-SSR4): mechanistic roles and therapeutic opportunities.Annals of medicine · 2026Review
- SSR4 Sustains Tertiary Lymphoid Structures by Regulation Quality Control of N-linked Glycosylation During B-cell Differentiation Into Plasmacyte in Colorectal Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Early neonatal diagnosis of SSR4-related congenital disorder of glycosylation with severe congenital heart defects: a case report and systematic review.Frontiers in pediatrics · 2026Article
- Article
- Lipid Scrambling Pathways in the Sec61 Translocon Complex.Journal of the American Chemical Society · 2025Article
- Toward Understanding the Mechanism of Client-Selective Small Molecule Inhibitors of the Sec61 Translocon.Journal of molecular recognition : JMR · 2025Review
- Identification of Translocon-associated Protein Delta as An Oncogene in Human Colorectal Cancer Cells.Journal of cancer prevention · 2024Article
- Article
- Combining causal and correlative approaches to discover biomarkers of response to paclitaxel.Oncotarget · 2024Article
- Functional unknomics: Systematic screening of conserved genes of unknown function.PLoS biology · 2023Article
- ΔInternational journal of molecular sciences · 2023Article
- Structural insights into TRAP association with ribosome-Sec61 complex and translocon inhibition by a CADA derivative.Science advances · 2023Article
- Inhibitors of the Sec61 Complex and Novel High Throughput Screening Strategies to Target the Protein Translocation Pathway.International journal of molecular sciences · 2021Review
- Intermedilysin cytolytic activity depends on heparan sulfates and membrane composition.PLoS genetics · 2021Article
Corrections and comments
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In eukaryotic cells, about one-third of the synthesized proteins are translocated into the endoplasmic reticulum; they are membrane or lumen resident proteins and proteins direct to the Golgi apparatus. The co-translational translocation takes place through the heterotrimeric protein-conducting channel Sec61 which is associated with the ribosome and many accessory components, such as the heterotetrameric translocon-associated protein (TRAP) complex. Recently, microscopic techniques, such as cryo-electron microscopy and cryo-electron tomography, have enabled the determination of the translocation machinery structure. However, at present, there is a lack of understanding regarding the roles of some of its components; indeed, the TRAP complex function during co-translational translocation needs to be established. In addition, TRAP may play a role during unfolded protein response, endoplasmic-reticulum-associated protein degradation and congenital disorder of glycosylation (ssr4 CDG). In this article, I describe the current understanding of the TRAP complex in the light of its possible function(s).
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.