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Mechanisms of Sec61/SecY-Mediated Protein Translocation Across Membranes

https://doi.org/10.1146/annurev-biophys-050511-102312

103/103 checkable references clean · checked 2026-07-22

Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.

The 103 checked references that resolve

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Reconstitution of a protein translocation system containing purified SecY, SecE, and SecA from Escherichia coli.

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Mapping polypeptide interactions of the SecA ATPase during translocation

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Structure of Monomeric Yeast and Mammalian Sec61 Complexes Interacting with the Translating Ribosome

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Architecture of the Protein-Conducting Channel Associated with the Translating 80S Ribosome

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The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure

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Atomic Model of the E.coli Membrane-bound Protein Translocation Complex SecYEG

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Three-dimensional structure of the bacterial protein-translocation complex SecYEG

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The purified E. coli integral membrane protein is sufficient for reconstitution of SecA-dependent precursor protein translocation

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Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY

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Formation of a functional ribosome-membrane junction during translocation requires the participation of a GTP-binding protein.

resolves10.1038/nrm2657

Delivering proteins for export from the cytosol

resolves10.1016/0092-8674(94)90424-3

Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore

resolves10.1016/0092-8674(93)90640-C

The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation

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A Dual Function for SecA in the Assembly of Single Spanning Membrane Proteins in Escherichia coli

resolves10.1016/j.molcel.2006.03.036

Central Pore Residues Mediate the p97/VCP Activity Required for ERAD

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A signal sequence is not required for protein export in prlA mutants of Escherichia coli.

resolves10.1016/j.cell.2011.06.004

Stepwise Insertion and Inversion of a Type II Signal Anchor Sequence in the Ribosome-Sec61 Translocon Complex

resolves10.1074/jbc.M110.175638

The Oligomeric State and Arrangement of the Active Bacterial Translocon

resolves10.1021/bi0342057

Bacillus subtilis SecA ATPase Exists as an Antiparallel Dimer in Solution

resolves10.1146/annurev.biochem.77.061606.160747

Protein Translocation Across the Bacterial Cytoplasmic Membrane

resolves10.1093/emboj/16.16.4871

The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling

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Sec‐dependent membrane protein biogenesis: SecYEG, preprotein hydrophobicity and translocation kinetics control the stop‐transfer function

resolves10.1073/pnas.1012556107

Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes

resolves10.1038/nature07439

A role for the two-helix finger of the SecA ATPase in protein translocation

resolves10.1083/jcb.126.4.935

Sec72p contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex.

resolves10.1091/mbc.4.9.931

Structural and functional characterization of Sec66p, a new subunit of the polypeptide translocation apparatus in the yeast endoplasmic reticulum.

resolves10.1038/nsmb.2026

Cryo-EM structure of the ribosome–SecYE complex in the membrane environment

resolves10.1016/0092-8674(94)90155-4

Topological ?frustration? in multispanning E. coli inner membrane proteins

resolves10.1083/jcb.147.2.257

Glycosylation Can Influence Topogenesis of Membrane Proteins and Reveals Dynamic Reorientation of Nascent Polypeptides within the Translocon

resolves10.1074/jbc.M702066200

Allosteric Regulation of SecA

resolves10.1016/0092-8674(93)90483-7

Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane

resolves10.1038/nature08559

Signal peptides are allosteric activators of the protein translocase

resolves10.1515/BC.2009.102

Protein targeting by the signal recognition particle

resolves10.1529/biophysj.105.075291

Molecular Dynamics Studies of the Archaeal Translocon

resolves10.1021/bi061013d

Simulations of a Protein Translocation Pore: SecY

resolves10.1016/j.sbi.2005.01.013

The signal recognition particle and its interactions during protein targeting

resolves10.1016/S0092-8674(00)80235-4

The Aqueous Pore through the Translocon Has a Diameter of 40–60 Å during Cotranslational Protein Translocation at the ER Membrane

resolves10.1016/S0092-8674(00)81403-8

BiP Maintains the Permeability Barrier of the ER Membrane by Sealing the Lumenal End of the Translocon Pore before and Early in Translocation

resolves10.1016/S0092-8674(00)81391-4

Oligomeric Rings of the Sec61p Complex Induced by Ligands Required for Protein Translocation

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Predicting the orientation of eukaryotic membrane-spanning proteins.

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The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans‐membrane topology

resolves10.1016/S0092-8674(00)00028-3

The Sec61p Complex Mediates the Integration of a Membrane Protein by Allowing Lipid Partitioning of the Transmembrane Domain

resolves10.1038/nature03216

Recognition of transmembrane helices by the endoplasmic reticulum translocon

resolves10.1016/j.cell.2005.04.012

Loops in the Central Channel of ClpA Chaperone Mediate Protein Binding, Unfolding, and Translocation

resolves10.1016/j.molcel.2010.12.028

SecA Interacts with Ribosomes in Order to Facilitate Posttranslational Translocation in Bacteria

resolves10.1126/science.1074424

Nucleotide Control of Interdomain Interactions in the Conformational Reaction Cycle of SecA

resolves10.1074/jbc.M210762200

Post-translational Secretion of Fusion Proteins in the Halophilic Archaea Haloferax volcanii

resolves10.1073/pnas.0502774102

Dimeric SecA is essential for protein translocation

resolves10.1091/mbc.E10-01-0060

The Hydrophobic Core of the Sec61 Translocon Defines the Hydrophobicity Threshold for Membrane Integration

resolves10.1038/emboj.2011.314

A single copy of SecYEG is sufficient for preprotein translocation

resolves10.1016/S1097-2765(02)00685-8

Protein Folding during Cotranslational Translocation in the Endoplasmic Reticulum

resolves10.1016/j.str.2010.12.016

Quaternary Structure of SecA in Solution and Bound to SecYEG Probed at the Single Molecule Level

resolves10.1091/mbc.E03-05-0325

The Endoplasmic Reticulum Membrane Is Permeable to Small Molecules

resolves10.1016/j.molcel.2007.05.002

The Plug Domain of the SecY Protein Stabilizes the Closed State of the Translocation Channel and Maintains a Membrane Seal

resolves10.1016/S0092-8674(00)80311-6

Both Lumenal and Cytosolic Gating of the Aqueous ER Translocon Pore Are Regulated from Inside the Ribosome during Membrane Protein Integration

resolves10.1083/jcb.201103117

Transmembrane segments of nascent polytopic membrane proteins control cytosol/ER targeting during membrane integration

resolves10.1083/jcb.201103118

Polytopic membrane protein folding at L17 in the ribosome tunnel initiates cyclical changes at the translocon

resolves10.1016/S0021-9258(19)36699-2

Membrane assembly of the triple-spanning coronavirus M protein. Individual transmembrane domains show preferred orientation.

resolves10.1016/S0092-8674(00)80767-9

BiP Acts as a Molecular Ratchet during Posttranslational Transport of Prepro-α Factor across the ER Membrane

resolves10.1016/j.str.2008.05.003

Single Copies of Sec61 and TRAP Associate with a Nontranslating Mammalian Ribosome

resolves10.1016/j.molcel.2007.10.034

Ribosome Binding of a Single Copy of the SecY Complex: Implications for Protein Translocation

resolves10.1016/S1097-2765(00)80158-6

J Proteins Catalytically Activate Hsp70 Molecules to Trap a Wide Range of Peptide Sequences

resolves10.1074/jbc.M300230200

Fluorescence Resonance Energy Transfer Analysis of Protein Translocase

resolves10.1002/j.1460-2075.1994.tb06713.x

Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane.

resolves10.1038/nature01050

Crystal structure of bacterial multidrug efflux transporter AcrB

resolves10.1074/jbc.M413947200

The Bacterial ATPase SecA Functions as a Monomer in Protein Translocation

resolves10.1074/jbc.M908916199

Evidence for Post-translational Membrane Insertion of the Integral Membrane Protein Bacterioopsin Expressed in the Heterologous Halophilic Archaeon Haloferax volcanii

resolves10.1073/pnas.0401742101

A large conformational change of the translocation ATPase SecA

resolves10.1016/j.cell.2007.02.036

Protein Translocation Is Mediated by Oligomers of the SecY Complex with One SecY Copy Forming the Channel

resolves10.1146/annurev.cellbio.21.012704.133214

PROTEIN TRANSLOCATION BY THE SEC61/SECY CHANNEL

resolves10.1016/j.jmb.2006.12.049

Structure of Dimeric SecA, the Escherichia coli Preprotein Translocase Motor

resolves10.1038/nature10014

Preserving the membrane barrier for small molecules during bacterial protein translocation

resolves10.1074/jbc.M500035200

Role of the GYVG Pore Motif of HslU ATPase in Protein Unfolding and Translocation for Degradation by HslV Peptidase

resolves10.1016/S0092-8674(00)81738-9

Signal Sequence Recognition in Posttranslational Protein Transport across the Yeast ER Membrane

resolves10.1083/jcb.151.1.167

Spontaneous Release of Cytosolic Proteins from Posttranslational Substrates before Their Transport into the Endoplasmic Reticulum

resolves10.1002/j.1460-2075.1994.tb06293.x

SecD and SecF facilitate protein export in Escherichia coli.

resolves10.1038/nature06384

Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes

resolves10.1016/j.tcb.2004.09.002

Membrane-protein integration and the role of the translocation channel

resolves10.1016/j.molcel.2007.03.022

Determining the Conductance of the SecY Protein Translocation Channel for Small Molecules

resolves10.1111/j.1600-0854.2011.01171.x

Molecular Mechanism of Co‐translational Protein Targeting by the Signal Recognition Particle

resolves10.1091/mbc.E06-05-0439

Ribosome Binding to and Dissociation from Translocation Sites of the Endoplasmic Reticulum Membrane

resolves10.1016/j.jmb.2005.09.058

The Oligomeric Distribution of SecYEG is Altered by SecA and Translocation Ligands

resolves10.1126/science.1188950

Control of Membrane Protein Topology by a Single C-Terminal Residue

resolves10.1073/pnas.85.20.7592

Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum.

resolves10.1101/gad.1170304

Role of the processing pore of the ClpX AAA+ ATPase in the recognition and engagement of specific protein substrates

resolves10.1016/0092-8674(91)90455-8

A protein-conducting channel in the endoplasmic reticulum

resolves10.1128/JB.187.18.6454-6465.2005

Modeling the Effects of prl Mutations on the Escherichia coli SecY Complex

resolves10.1083/jcb.200312079

The organization of engaged and quiescent translocons in the endoplasmic reticulum of mammalian cells

resolves10.1529/biophysj.105.073304

Size, Motion, and Function of the SecY Translocon Revealed by Molecular Dynamics Simulations with Virtual Probes

resolves10.1091/mbc.E11-01-0070

Translocation channel gating kinetics balances protein translocation efficiency with signal sequence recognition fidelity

resolves10.1038/nature09980

Structure and function of a membrane component SecDF that enhances protein export

resolves10.1038/nature07421

Conformational transition of Sec machinery inferred from bacterial SecYE structures

resolves10.1038/nature02218

X-ray structure of a protein-conducting channel

resolves10.1016/j.jmb.2006.09.061

Crystal Structure of the Translocation ATPase SecA from Thermus thermophilus Reveals a Parallel, Head-to-Head Dimer

resolves10.1074/jbc.M103912200

Mapping the Sites of Interaction between SecY and SecE by Cysteine Scanning Mutagenesis

resolves10.1038/nrm2063

Membrane-protein topology

resolves10.1126/science.1070925

Identification of Signal Peptide Peptidase, a Presenilin-Type Aspartic Protease

resolves10.1110/ps.4090102

Complex behavior in solution of homodimeric SecA

resolves10.1038/nrmicro1845

Mathematical models of infectious disease transmission

resolves10.1074/jbc.M308327200

Conserved Pore Residues in the AAA Protease FtsH Are Important for Proteolysis and Its Coupling to ATP Hydrolysis

resolves10.1016/j.jmb.2006.08.044

A Novel Dimer Interface and Conformational Changes Revealed by an X-ray Structure of B. subtilis SecA

resolves10.1038/nature07335

Structure of a complex of the ATPase SecA and the protein-translocation channel

resolves10.1016/j.jmb.2009.10.024

Conformational Flexibility and Peptide Interaction of the Translocation ATPase SecA

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