ArticleProtein science : a publication of the Protein Society2014
Folding of Aquaporin 1: multiple evidence that helix 3 can shift out of the membrane core.
Article in Protein science : a publication of the Protein Society, 2014. 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.
- Feedback from the Nascent Chain Triggers Ribosomal Frameshifting and Transcript Decay.bioRxiv : the preprint server for biology · 2025Article
- Cotranslational folding stimulates programmed ribosomal frameshifting in the alphavirus structural polyprotein.The Journal of biological chemistry · 2020Article
- Lipid-Assisted Membrane Protein Folding and Topogenesis.The protein journal · 2019Review
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
- A network of chaperones prevents and detects failures in membrane protein lipid bilayer integration.Nature communications · 2019Article
- Contribution of Cotranslational Folding Defects to Membrane Protein Homeostasis.Journal of the American Chemical Society · 2019Article
- Grafting Charged Species to Membrane-Embedded Scaffolds Dramatically Increases the Rate of Bilayer Flipping.ACS central science · 2017Article
- NMR Investigation of Structures of G-protein Coupled Receptor Folding Intermediates.The Journal of biological chemistry · 2016Article
- Article
- Marginally hydrophobic transmembrane α-helices shaping membrane protein folding.Protein science : a publication of the Protein Society · 2015Review
- Influence of Pathogenic Mutations on the Energetics of Translocon-Mediated Bilayer Integration of Transmembrane Helices.The Journal of membrane biology · 2015Article
- Protein Science Best Paper awards to Chih-Chia (Jack) Su and Minttu Virkki.Protein science : a publication of the Protein Society · 2015Article
- The safety dance: biophysics of membrane protein folding and misfolding in a cellular context.Quarterly reviews of biophysics · 2015Article
- Disease-linked supertrafficking of a potassium channel.The Journal of biological chemistryArticle
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Authors and funding
6 authors.
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Abstract
The folding of most integral membrane proteins follows a two-step process: initially, individual transmembrane helices are inserted into the membrane by the Sec translocon. Thereafter, these helices fold to shape the final conformation of the protein. However, for some proteins, including Aquaporin 1 (AQP1), the folding appears to follow a more complicated path. AQP1 has been reported to first insert as a four-helical intermediate, where helix 2 and 4 are not inserted into the membrane. In a second step, this intermediate is folded into a six-helical topology. During this process, the orientation of the third helix is inverted. Here, we propose a mechanism for how this reorientation could be initiated: first, helix 3 slides out from the membrane core resulting in that the preceding loop enters the membrane. The final conformation could then be formed as helix 2, 3, and 4 are inserted into the membrane and the reentrant regions come together. We find support for the first step in this process by showing that the loop preceding helix 3 can insert into the membrane. Further, hydrophobicity curves, experimentally measured insertion efficiencies and MD-simulations suggest that the barrier between these two hydrophobic regions is relatively low, supporting the idea that helix 3 can slide out of the membrane core, initiating the rearrangement process.
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