ArticleNature chemical biology2016
YidC assists the stepwise and stochastic folding of membrane proteins.
Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 78 citations in OpenAlex.
- The Shape of Things to Come: α-Helical Membrane Protein Folding on the Ribosome.Chemical reviews · 2026Review
- Membrane Protein Folding and Biogenesis: Insights from Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- Monitoring Membrane Protein Folding Assisted by Insertases and Translocases Using AFM-Based Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- Membrane Protein Insertion in Cells: Principles, Pathways, and Quality Control.Chemical reviews · 2026Review
- Single Molecule Force Spectroscopy to Probe Intermediates and Energetics of Membrane Protein Folding.Chemical reviews · 2026Review
- Article
- Deciphering the Interdomain Coupling in a Gram-Negative Bacterial Membrane Insertase.The journal of physical chemistry. B · 2024Article
- Folding speeds of helical membrane proteins.Biochemical Society transactions · 2024Review
- The insertase YidC chaperones the polytopic membrane protein MelB inserting and folding simultaneously from both termini.Structure (London, England : 1993) · 2023Article
- ER-localized Shr3 is a selective co-translational folding chaperone necessary for amino acid permease biogenesis.The Journal of cell biology · 2023Article
- The Biogenesis of Multipass Membrane Proteins.Cold Spring Harbor perspectives in biology · 2023Review
- Single-molecule mechanical studies of chaperones and their clients.Biophysics reviews · 2022Review
- Article
- Methods to study folding of alpha-helical membrane proteins in lipids.Open biology · 2022Review
- Evolutionary balance between foldability and functionality of a glucose transporter.Nature chemical biology · 2022Article
- The ER membrane complex (EMC) can functionally replace the Oxa1 insertase in mitochondria.PLoS biology · 2022Article
- How physical forces drive the process of helical membrane protein folding.EMBO reports · 2022Review
- Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022Review
- An investigation of the YidC-mediated membrane insertion of Pf3 coat protein using molecular dynamics simulations.Frontiers in molecular biosciences · 2022Article
- A unified evolutionary origin for the ubiquitous protein transporters SecY and YidC.BMC biology · 2021Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
How chaperones, insertases and translocases facilitate insertion and folding of complex cytoplasmic proteins into cellular membranes is not fully understood. Here we utilize single-molecule force spectroscopy to observe YidC, a transmembrane chaperone and insertase, sculpting the folding trajectory of the polytopic α-helical membrane protein lactose permease (LacY). In the absence of YidC, unfolded LacY inserts individual structural segments into the membrane; however, misfolding dominates the process so that folding cannot be completed. YidC prevents LacY from misfolding by stabilizing the unfolded state from which LacY inserts structural segments stepwise into the membrane until folding is completed. During stepwise insertion, YidC and the membrane together stabilize the transient folds. Remarkably, the order of insertion of structural segments is stochastic, indicating that LacY can fold along variable pathways toward the native structure. Since YidC is essential in membrane protein biogenesis and LacY is a model for the major facilitator superfamily, our observations have general relevance.
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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.