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
Items 401–433 of 433
The SecY Protein Family: Comparative Analysis and Phylogenetic Relationships
Rensing, S. A., & Maier, U. (1994) · Molecular Phylogenetics and Evolution · doi:10.1006/mpev.1994.1021 · Cited by 25
CK2 phosphorylation of human Sec63 regulates its interaction with Sec62
Ampofo, E., Welker, S., Jung, M., Müller, L., Greiner, M., Zimmermann, R., & Montenarh, M. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.12.020 · Cited by 25
Conservation of components of theEscherichia coliexport machinery in prokaryotes
Cook, H., & Tommassen, J. (1991) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1991.tb04660.x · Cited by 25
GTPases and the origin of the ribosome
Hartman, H., & Smith, T. F. (2010) · Biology Direct · doi:10.1186/1745-6150-5-36 · Cited by 24
[35] SeeB: A chaperone from Escherichia coli
Randall, L. L., Topping, T., Smith, V. F., Diamond, D. L., & HARDY, S. J. S. (1998) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(98)90037-4 · Cited by 23
Biogenesis of the signal recognition particle
Leung, E., & Brown, J. D. (2010) · Biochemical Society Transactions · doi:10.1042/bst0381093 · Cited by 22
Topologically Fixed SecG Is Fully Functional
van der Sluis, E. O., van der Vries, E., Berrelkamp, G., Nouwen, N. P., & Driessen, A. J. M. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.3.1188-1190.2006 · Cited by 22
Keller, R. C. A. (2010) · Cellular & Molecular Biology Letters · doi:10.2478/s11658-010-0036-y · Cited by 21
Loibl, M., Wunderle, L., Hutzler, J., Schulz, B. L., Aebi, M., & Strahl, S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.543116 · Cited by 20
Eichler, J. (2003) · Molecular Phylogenetics and Evolution · doi:10.1016/s1055-7903(03)00015-0 · Cited by 20
Nearest Neighbor Analysis of the SecYEG Complex. 1. Identification of a SecY−SecG Interface
Satoh, Y., Matsumoto, G., Mori, H., & Ito, K. (2003) · Biochemistry · doi:10.1021/bi034331a · Cited by 20
Multiple SecA Molecules Drive Protein Translocation across a Single Translocon with SecG Inversion
Morita, K., Tokuda, H., & Nishiyama, K. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.301754 · Cited by 20
Characterization of the supporting role of SecE in protein translocation
Nijeholt, J. A. L. A., de Keyzer, J., Prabudiansyah, I., & Driessen, A. J. M. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.07.046 · Cited by 20
Archaea Signal Recognition Particle Shows the Way
Zwieb, C. W., & Bhuiyan, S. (2010) · Archaea · doi:10.1155/2010/485051 · Cited by 20
Boisramé, A., Chasles, M., Babour, A., Beckerich, J.-M., & Gaillardin, C. M. (2002) · Journal of Cell Science · doi:10.1242/jcs.00187 · Cited by 19
Liang, H., VanValkenburgh, C., Chen, X., Mullins, C., Kaer, L. V., Green, N., & Fang, H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307542200 · Cited by 18
Nouwen, N. P., KRUIJFF, B. D., & Tommassen, J. (1996) · Molecular Microbiology · doi:10.1111/j.1365-2958.1996.tb02466.x · Cited by 18
N-acetylation and phosphorylation of Sec complex subunits in the ER membrane
Soromani, C., Zeng, N., Hollemeyer, K., Heinzle, E., Klein, M.-C., Tretter, T., Seaman, M. N. J., & Römisch, K. (2012) · BMC Cell Biology · doi:10.1186/1471-2121-13-34 · Cited by 18
Crossing the membrane in Archaea, the third domain of life
Calo, D., & Eichler, J. (2010) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2010.03.020 · Cited by 18
Zhao, X., & Jäntti, J. (2009) · BMC Cell Biology · doi:10.1186/1471-2121-10-76 · Cited by 17
The ER-membrane-resident Hsp40 ERj1 is a novel substrate for protein kinase CK2
Götz, C., Müller, A., Montenarh, M., Zimmermann, R., & Dudek, J. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.07.146 · Cited by 16
Structure and function of signal recognition particle (SRP)
Römisch, K., Ribes, V., High, S., L�tcke, H., Tollervey, D. W., & Dobberstein, B. (1990) · Molecular Biology Reports · doi:10.1007/bf00360420 · Cited by 16
Role of Human Sec63 in Modulating the Steady-State Levels of Multi-Spanning Membrane Proteins
Mades, A., Gotthardt, K., Awe, K., Stieler, J., Döring, T., Füser, S., & Prange, R. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049243 · Cited by 16
The signal recognition particle database (SRPDB)
Larsen, N., & Zwieb, C. W. (1993) · Nucleic Acids Research · doi:10.1093/nar/21.13.3019 · Cited by 14
Computational analysis reveals abundance of potential glycoproteins in Archaea, Bacteria and Eukarya
Zafar, S., Nasir, A., & Bokhari, H. (2011) · Bioinformation · doi:10.6026/97320630006352 · Cited by 11
Conservation of components of the export machinery in prokaryotes
DECOOK, H., & Tommassen, J. (1991) · FEMS Microbiology Letters · doi:10.1016/0378-1097(91)90594-z · Cited by 8
Yamamoto, H., Fujita, H., Kida, Y., & Sakaguchi, M. (2012) · Biochemistry · doi:10.1021/bi2018915 · Cited by 8
Nam, S.-E., & Paetzel, M. (2013) · Biochemistry · doi:10.1021/bi4011489 · Cited by 6
BIP: A low molecular weight protein coisolated with beta-2 microglublin
Gordon, S. M., & Kindt, T. J. (1976) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(76)80228-8 · Cited by 5
Single rRNA Helices Bind Independently to the Protein‐Conducting Channel SecYEG
Behrens, C., Hartmann, E., & Kalies, K. (2012) · Traffic · doi:10.1111/tra.12033 · Cited by 3
Nakashima, K., Ishida, H., Nakatomi, A., & Yazawa, M. (2012) · The Journal of Biochemistry · doi:10.1093/jb/mvs048 · Cited by 3
Phosphatidylserine-binding protein lactadherin inhibits protein translocation across the ER membrane
Yamamoto, H., Kida, Y., & Sakaguchi, M. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.03.131 · Cited by 2
Seaside transportation—from structure to function of translocation machines
Lithgow, T. J., & Waksman, G. (2013) · EMBO Reports · doi:10.1038/embor.2013.79 · Cited by 1
Flagged first, then by citations
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
