ArticleMolecular biology of the cell2004
Interactions between Sec complex and prepro-alpha-factor during posttranslational protein transport into the endoplasmic reticulum.
Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 63 citations in OpenAlex.
- The MFα signal sequence in yeast-based protein secretion: challenges and innovations'.Applied microbiology and biotechnology · 2025Review
- A diversified and segregated mRNA spliced-leader system in the parasitic Perkinsozoa.Open biology · 2022Article
- Molecular Modeling of Signal Peptide Recognition by Eukaryotic Sec Complexes.International journal of molecular sciences · 2021Review
- Analysis of the Putative Nucleoporin POM33 in the Filamentous FungusJournal of fungi (Basel, Switzerland) · 2021Article
- How does Sec63 affect the conformation of Sec61 in yeast?PLoS computational biology · 2021Article
- Architecture of the active post-translational Sec translocon.The EMBO journal · 2021Article
- The P5A ATPase Spf1p is stimulated by phosphatidylinositol 4-phosphate and influences cellular sterol homeostasis.Molecular biology of the cell · 2019Article
- Determination of the Oligomeric State of SecYEG Protein Secretion Channel Complex Using in Vivo Photo- and Disulfide Cross-linking.The Journal of biological chemistry · 2016Article
- Membrane Protein Structure, Function, and Dynamics: a Perspective from Experiments and Theory.The Journal of membrane biology · 2015Review
- Co-translational protein targeting to the bacterial membrane.Biochimica et biophysica acta · 2014Review
- Sec62 protein mediates membrane insertion and orientation of moderately hydrophobic signal anchor proteins in the endoplasmic reticulum (ER).The Journal of biological chemistry · 2013Article
- Efficient secretion of small proteins in mammalian cells relies on Sec62-dependent posttranslational translocation.Molecular biology of the cell · 2012Article
- The bacterial Sec-translocase: structure and mechanism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Article
- Preferential targeting of a signal recognition particle-dependent precursor to the Ssh1p translocon in yeast.The Journal of biological chemistry · 2011Article
- Structural studies and the assembly of the heptameric post-translational translocon complex.The Journal of biological chemistry · 2011Article
- Membrane protein insertion at the endoplasmic reticulum.Annual review of cell and developmental biology · 2011Review
- Sss1p is required to complete protein translocon activation.The Journal of biological chemistry · 2010Article
- Structure of monomeric yeast and mammalian Sec61 complexes interacting with the translating ribosome.Science (New York, N.Y.) · 2009Article
- The lateral gate of SecYEG opens during protein translocation.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Posttranslational translocation of prepro-alpha-factor (ppalphaF) across the yeast endoplasmic reticulum membrane begins with the binding of the signal sequence to the Sec complex, a membrane component consisting of the trimeric Sec61p complex and the tetrameric Sec62p/63p complex. We show by photo-cross-linking that the signal sequence is bound directly to a site where it contacts simultaneously Sec61p and Sec62p, suggesting that there is a single signal sequence recognition step. We found no evidence for the simultaneous contact of the signal sequence with two Sec61p molecules. To identify transmembrane segments of Sec61p that line the actual translocation pore, a late translocation intermediate of ppalphaF was generated with photoreactive probes incorporated into the mature portion of the polypeptide. Cross-linking to multiple regions of Sec61p was observed. In contrast to the signal sequence, neighboring positions of the mature portion of ppalphaF had similar interactions with Sec61p. These data suggest that the channel pore is lined by several transmembrane segments, which have no significant affinity for the translocating polypeptide chain.
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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.