ArticleThe Journal of biological chemistry2013
Sec62 protein mediates membrane insertion and orientation of moderately hydrophobic signal anchor proteins in the endoplasmic reticulum (ER).
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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Who cites it
22 citing papers in PubMed, 44 citations in OpenAlex.
- The Sec11 C-terminal short helix promotes productive engagement of internal signal sequences with the signal peptidase complex.The Journal of biological chemistry · 2026Article
- Protein secretion routes in fungi are predicted by the length of the hydrophobic helix in the signal sequence.G3 (Bethesda, Md.) · 2026Article
- Review
- Targeting of Proteins for Translocation at the Endoplasmic Reticulum.International journal of molecular sciences · 2022Review
- Signal Peptide Features Determining the Substrate Specificities of Targeting and Translocation Components in Human ER Protein Import.Frontiers in physiology · 2022Review
- Emerging View on the Molecular Functions of Sec62 and Sec63 in Protein Translocation.International journal of molecular sciences · 2021Review
- Complexity and Specificity of Sec61-Channelopathies: Human Diseases Affecting Gating of the Sec61 Complex.Cells · 2021Review
- Predicating the Effector Proteins Secreted byFrontiers in microbiology · 2020Article
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
- The Best for the Most Important: Maintaining a Pristine Proteome in Stem and Progenitor Cells.Stem cells international · 2019Review
- Chaperone-Mediated Sec61 Channel Gating during ER Import of Small Precursor Proteins Overcomes Sec61 Inhibitor-Reinforced Energy Barrier.Cell reports · 2018Article
- Inhibitors of protein translocation across membranes of the secretory pathway: novel antimicrobial and anticancer agents.Cellular and molecular life sciences : CMLS · 2018Review
- Refined topology model of the STT3/Stt3 protein subunit of the oligosaccharyltransferase complex.The Journal of biological chemistry · 2017Article
- An Update on Sec61 Channel Functions, Mechanisms, and Related Diseases.Frontiers in physiology · 2017Review
- Identification of SEC62 as a potential marker for 3q amplification and cellular migration in dysplastic cervical lesions.BMC cancer · 2016Article
- Initial evidence for Sec62 as a prognostic marker in advanced head and neck squamous cell carcinoma.Oncology letters · 2016Article
- Cotranslational stabilization of Sec62/63 within the ER Sec61 translocon is controlled by distinct substrate-driven translocation events.Molecular cell · 2015Article
- Signal peptide-binding drug as a selective inhibitor of co-translational protein translocation.PLoS biology · 2014Article
- Type II transmembrane domain hydrophobicity dictates the cotranslational dependence for inversion.Molecular biology of the cell · 2014Article
- Structural and functional profiling of the lateral gate of the Sec61 translocon.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nascent chains are known to be targeted to the endoplasmic reticulum membrane either by a signal recognition particle (SRP)-dependent co-translational or by an SRP-independent post-translational translocation route depending on signal sequences. Using a set of model and cellular proteins carrying an N-terminal signal anchor sequence of controlled hydrophobicity and yeast mutant strains defective in SRP or Sec62 function, the hydrophobicity-dependent targeting efficiency and targeting pathway preference were systematically evaluated. Our results suggest that an SRP-dependent co-translational and an SRP-independent post-translational translocation are not mutually exclusive for signal anchor proteins and that moderately hydrophobic ones require both SRP and Sec62 for proper targeting and translocation to the endoplasmic reticulum. Further, defect in Sec62 selectively reduced signal sequences inserted in an N(in)-C(out) (type II) membrane topology, implying an undiscovered role of Sec62 in regulating the orientation of the signal sequence in an early stage of translocation.
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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.