ArticleScience (New York, N.Y.)2024
Identification of a factor that accelerates substrate release from the signal recognition particle.
Article in Science (New York, N.Y.), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- GTPase cycle and ER membrane regulate cargo handover during cotranslational protein targeting.Science advances · 2026Article
- HSP47 in Mitochondria: Roles in Apoptosis, Signal Transduction, and Protein and Virus Transportation.Cells · 2026Review
- Pairwise transmembrane domain insertion during multipass protein biogenesis.Molecular cell · 2026Article
- Global analysis of translocon remodeling during protein synthesis at the ER.Nature structural & molecular biology · 2025Article
- Mechanistic Insights into Protein Biogenesis and Maturation on the Ribosome.Journal of molecular biology · 2025Review
- SND3 is the membrane insertase within a distinct SEC61 translocon complex.Nature communications · 2025Article
- Navigating lipid droplet proteins - part I: ER targeting routes of lipid droplet-destined membrane proteins.Biochemical Society transactions · 2025Review
- Rules of Engagement for Components of Membrane Protein Biogenesis at the Human Endoplasmic Reticulum.International journal of molecular sciences · 2025Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The eukaryotic signal recognition particle (SRP) cotranslationally recognizes the first hydrophobic segment of nascent secretory and membrane proteins and delivers them to a receptor at the endoplasmic reticulum (ER). How substrates are released from SRP at the ER to subsequently access translocation factors is not well understood. We found that TMEM208 can engage the substrate binding domain of SRP to accelerate release of its bound cargo. Without TMEM208, slow cargo release resulted in excessive synthesis of downstream polypeptide before engaging translocation factors. Delayed access to translocation machinery caused progressive loss of insertion competence, particularly for multipass membrane proteins, resulting in their impaired biogenesis. Thus, TMEM208 facilitates prompt cargo handover from the targeting to translocation machinery to minimize biogenesis errors and maintain protein homeostasis.
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Registered trials
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