ArticleProceedings of the National Academy of Sciences of the United States of America2008
Molecular code for protein insertion in the endoplasmic reticulum membrane is similar for N(in)-C(out) and N(out)-C(in) transmembrane helices.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. 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.
- Membrane-embedded polar residues target membrane proteins for degradation by the quality control protease FtsH.Nature communications · 2026Article
- Lipid bilayer thinning near a ubiquitin ligase selects ER membrane proteins for degradation.bioRxiv : the preprint server for biology · 2025Article
- Spiers Memorial Lecture: Analysis andFaraday discussions · 2021Article
- Efficient integration of transmembrane domains depends on the folding properties of the upstream sequences.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Spc1 regulates the signal peptidase-mediated processing of membrane proteins.Journal of cell science · 2021Article
- Harmonizing Experimental Data with Modeling to Predict Membrane Protein Insertion in Yeast.Biophysical journal · 2019Article
- Membrane Protein Integration and Topogenesis at the ER.The protein journal · 2019Review
- Murine astrotactins 1 and 2 have a similar membrane topology and mature via endoproteolytic cleavage catalyzed by a signal peptidase.The Journal of biological chemistry · 2019Article
- Applications of Single-Molecule Methods to Membrane Protein Folding Studies.Journal of molecular biology · 2018Review
- Gene Duplication Leads to Altered Membrane Topology of a Cytochrome P450 Enzyme in Seed Plants.Molecular biology and evolution · 2017Article
- Refined topology model of the STT3/Stt3 protein subunit of the oligosaccharyltransferase complex.The Journal of biological chemistry · 2017Article
- Mycolactone subverts immunity by selectively blocking the Sec61 translocon.The Journal of experimental medicine · 2016Article
- Folding and Intramembraneous BRICHOS Binding of the Prosurfactant Protein C Transmembrane Segment.The Journal of biological chemistry · 2015Article
- Marginally hydrophobic transmembrane α-helices shaping membrane protein folding.Protein science : a publication of the Protein Society · 2015Review
- Review
- Thermodynamics of Membrane Insertion and Refolding of the Diphtheria Toxin T-Domain.The Journal of membrane biology · 2015Article
- Differential repositioning of the second transmembrane helices from E. coli Tar and EnvZ upon moving the flanking aromatic residues.Biochimica et biophysica acta · 2015Article
- Folding of Aquaporin 1: multiple evidence that helix 3 can shift out of the membrane core.Protein science : a publication of the Protein Society · 2014Article
- Structural and functional profiling of the lateral gate of the Sec61 translocon.The Journal of biological chemistry · 2014Article
- Changed membrane integration and catalytic site conformation are two mechanisms behind the increased Aβ42/Aβ40 ratio by presenilin 1 familial Alzheimer-linked mutations.FEBS open bio · 2014Article
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5 authors.
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Abstract
Transmembrane alpha-helices in integral membrane proteins can have two orientations in the membrane: N(in)-C(out) or N(out)-C(in). Previous studies of model N(out)-C(in) transmembrane segment have led to a detailed, quantitative picture of the "molecular code" that relates amino acid sequence to membrane insertion efficiency in vivo [Hessa T, et al. (2007) Molecular code for transmembrane helix recognition by the Sec61 translocon. Nature 450:1026-1030], but whether the same code applies also to N(in)-C(out) transmembrane helices is unknown. Here, we show that the contributions of individual amino acids to the overall efficiency of membrane insertion are similar for the two kinds of helices and that the threshold hydrophobicity for membrane insertion can be up to approximately 1 kcal/mol lower for N(in)-C(out) compared with N(out)-C(in) transmembrane helices, depending on the neighboring helices.
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