The DOI matches its Crossref record; 432 of the 433 references it cites were found in a registry or an index, and 1 are not checked yet.
The Sec translocon mediated protein transport in prokaryotes and eukaryotes.
Open accessAbstract
Protein transport via the Sec translocon represents an evolutionary conserved mechanism for delivering cytosolically-synthesized proteins to extra-cytosolic compartments. The Sec translocon has a three-subunit core, termed Sec61 in Eukaryotes and SecYEG in Bacteria. It is located in the endoplasmic reticulum of Eukaryotes and in the cytoplasmic membrane of Bacteria where it constitutes a channel that can be activated by multiple partner proteins. These partner proteins determine the mechanism of polypeptide movement across the channel. During SRP-dependent co-translational targeting, the ribosome threads the nascent protein directly into the Sec channel. This pathway is in Bacteria mainly dedicated for membrane proteins but in Eukaryotes also employed by secretory proteins. The alternative pathway, leading to post-translational translocation across the Sec translocon engages an ATP-dependent pushing mechanism by the motor protein SecA in Bacteria and a ratcheting mechanism by the lumenal chaperone BiP in Eukaryotes. Protein transport and biogenesis is also assisted by additional proteins at the lateral gate of SecY/Sec61α and in the lumen of the endoplasmic reticulum or in the periplasm of bacterial cells. The modular assembly enables the Sec complex to transport a vast array of substrates. In this review we summarize recent biochemical and structural information on the prokaryotic and eukaryotic Sec translocons and we describe the remarkably complex interaction network of the Sec complexes.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“The universally conserved SecYEG translocon acts at the center of bacterial protein transport and mediates the translocation of newly synthesized proteins into and across the cytoplasmic membrane.”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Denks et al., 2014
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Membrane lipids: where they are and how they behave
van Meer, G., Voelker, D. R., & Feigenson, G. W. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2330 · Cited by 7,157
A new method for predicting signal sequence cleavage sites
von HEIJNE, G. (1986) · Nucleic Acids Research · doi:10.1093/nar/14.11.4683 · Cited by 4,473
Genome-Wide Analysis in Vivo of Translation with Nucleotide Resolution Using Ribosome Profiling
Ingolia, N. T., Ghaemmaghami, S., Newman, J. R. S., & Weissman, J. S. (2009) · Science · doi:10.1126/science.1168978 · Cited by 3,853
von HEIJNE, G. (1985) · Journal of Molecular Biology · doi:10.1016/0022-2836(85)90046-4 · Cited by 2,176
Lee, A., Iwakoshi, N. N., & Glimcher, L. H. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.21.7448-7459.2003 · Cited by 2,099
Deshaies, R., Koch, B., Werner-Washburne, M., Craig, E., & Schekman, R. (1988) · Nature · doi:10.1038/332800a0 · Cited by 1,368
X-ray structure of a protein-conducting channel
van den Berg, B., Clemons, W., Collinson, I. R., Modis, Y., Hartmann, E., Harrison, S. C., & Rapoport, T. A. (2003) · Nature · doi:10.1038/nature02218 · Cited by 1,236
70K heat shock related proteins stimulate protein translocation into microsomes
Chirico, W. J., Waters, M. G., & Blobel, G. (1988) · Nature · doi:10.1038/332805a0 · Cited by 1,232
von HEIJNE, G. (1990) · The Journal of Membrane Biology · doi:10.1007/bf01868635 · Cited by 1,140
Recognition of transmembrane helices by the endoplasmic reticulum translocon
Hessa, T., Kim, H., Bihlmaier, K., Lundin, C., Boekel, J., Andersson, H. M., Nilsson, I., White, S. H., & von HEIJNE, G. (2005) · Nature · doi:10.1038/nature03216 · Cited by 996
Research works printed but not linked: 4
- Castanié-Cornet M-P, 2013, Biochim Biophys Acta – Mol Cell Res
- Keller RCA, 2011, Cell Mol Biol Lett, 16, 40
- Nakashima K, 2012, J Bacteriol, 152, 27
- Tseng TT, 1999, J Mol MicroBio Biotechnol, 1, 107
Cited by
Sorted by citations
Mechanisms of Integral Membrane Protein Insertion and Folding
Cymer, F., von HEIJNE, G., & White, S. H. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.09.014 · Cited by 367
The Type IX Secretion System (T9SS): Highlights and Recent Insights into Its Structure and Function
Lasica, A. M., Ksiazek, M., Madej, M., & Potempa, J. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00215 · Cited by 312
Signal. peptides for recombinant protein secretion in bacterial expression systems
Freudl, R. (2018) · Microbial Cell Factories · doi:10.1186/s12934-018-0901-3 · Cited by 312
Bahr, G., González, L. J., & Vila, A. J. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00138 · Cited by 288
Johnson, L. R., Lee, D. Y., Eacret, J. S., Ye, D., June, C. H., & Minn, A. J. (2021) · Cell · doi:10.1016/j.cell.2021.08.004 · Cited by 190
Metadata
- Authors
- Denks, K., Vogt, A., Sachelaru, I., Petriman, N.-A., Kudva, R., & Koch, H.-G.
- Affiliations
- University of Freiburg (DE)
- Corresponding author
- Koch, Hans-Georg
- Venue
- Molecular Membrane Biology
- Publisher
- Informa UK Limited
- Published
- 2014-03
- Volume
- 31
- Issue
- 2-3
- Pages
- 58-84
- ISSN
- 0968-7688 (ISSN-L)
- 1464-5203
- OpenAlex
- W1978110792
- Cited by
- 170
- References
- 431
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 18 · 2023: 10 · 2022: 16 · 2021: 18 · 2020: 17 · 2019: 15 · 2018: 7 · 2017: 22 · 2016: 9 · 2015: 21 · 2014: 6
- FWCI
- 2.56
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Membrane Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- Sec translocon, Sec61, SecYEG, protein translocation, SRP, post-translational translocation, SecA, BiP, endoplasmic reticulum, bacterial cytoplasmic membrane, membrane protein biogenesis, protein secretion, evolutionary conservation
- MeSH terms
- SEC Translocation Channels, Cell Membrane, Endoplasmic Reticulum, Membrane Proteins, Models, Molecular, Prokaryotic Cells, Signal Recognition Particle, Protein Transport, Eukaryota
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review