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Protein translocation across the ER membrane

https://doi.org/10.1016/j.bbamem.2010.06.015

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marked retracted — notice via Crossref, record curated by Retraction Watch10.1038/sj.embor.7400551

L25 functions as a conserved ribosomal docking site shared by nascent chain‐associated complex and signal‐recognition particle

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Sec61p Is Required for ERAD-L

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Sec61p is part of the endoplasmic reticulum‐associated degradation machinery

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ERdj5 Is Required as a Disulfide Reductase for Degradation of Misfolded Proteins in the ER

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YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism

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Roles of Cytosolic Hsp70 and Hsp40 Molecular Chaperones in Post-translational Translocation of Presecretory Proteins into the Endoplasmic Reticulum

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Seventy‐kilodalton heat shock proteins and an additional component from reticulocyte lysate stimulate import of M13 procoat protein into microsomes.

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Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein.

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A membrane component essential for vectorial translocation of nascent proteins across the endoplasmic reticulum: requirements for its extraction and reassociation with the membrane.

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Distinct Modes of Signal Recognition Particle Interaction with the Ribosome

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Endoplasmic Reticulum-bound Ribosomes Reside in Stable Association with the Translocon following Termination of Protein Synthesis

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The Crystal Structure of Archaeal Nascent Polypeptide-associated Complex (NAC) Reveals a Unique Fold and the Presence of a Ubiquitin-associated Domain

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Role of Protein Translocation Pathways across the Endoplasmic Reticulum in Trypanosoma brucei

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A large presecretory protein translocates both cotranslationally, using signal recognition particle and ribosome, and post-translationally, without these ribonucleoparticles, when synthesized in the presence of mammalian microsomes.

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RNA Interference of Signal Peptide-binding Protein SRP54 Elicits Deleterious Effects and Protein Sorting Defects in Trypanosomes

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Differential Regulation of the TRAIL Death Receptors DR4 and DR5 by the Signal Recognition Particle

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SRP Keeps Polypeptides Translocation-Competent by Slowing Translation to Match Limiting ER-Targeting Sites

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The signal recognition particle in S. cerevisiae

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SEC65 gene product is a subunit of the yeast signal recognition particle required for its integrity

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The S. cerevisiae SEC65 gene encodes a component of yeast signal recognition particle with homology to human SRP19

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An in Vitro Assay Using Overexpressed Yeast SRP Demonstrates that Cotranslational Translocation Is Dependent upon the J-Domain of Sec63p

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SEC62 encodes a putative membrane protein required for protein translocation into the yeast endoplasmic reticulum.

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Mutants in three novel complementation groups inhibit membrane protein insertion into and soluble protein translocation across the endoplasmic reticulum membrane of Saccharomyces cerevisiae.

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The yeast SSS1 gene is essential for secretory protein translocation and encodes a conserved protein of the endoplasmic reticulum.

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Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p

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A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae.

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Ssh1p Determines the Translocation and Dislocation Capacities of the Yeast Endoplasmic Reticulum

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BiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum.

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Sec63p and Kar2p are required for the translocation of SRP‐dependent precursors into the yeast endoplasmic reticulum in vivo

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Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae.

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Structural evidence for consecutive Hel308-like modules in the spliceosomal ATPase Brr2

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Binding of Secretory Precursor Polypeptides to a Translocon Subcomplex Is Regulated by BiP

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Protein Transport by Purified Yeast Sec Complex and Kar2p Without Membranes

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

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A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursors.

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Coordinated Activation of Hsp70 Chaperones

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LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum

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Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

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Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK

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Nuclear Magnetic Resonance Solution Structure of the Human Hsp40 (HDJ-1) J-domain

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Structural Basis for the Cooperation of Hsp70 and Hsp110 Chaperones in Protein Folding

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Structure of the Hsp110:Hsc70 Nucleotide Exchange Machine

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A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation

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Evolutionary conservation of components of the protein translocation complex

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

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A microsomal protein is involved in ATP‐dependent transport of presecretory proteins into mammalian microsomes.

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Lumenal proteins of the mammalian endoplasmic reticulum are required to complete protein translocation

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A microsomal ATP‐binding protein involved in efficient protein transport into the mammalian endoplasmic reticulum.

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

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A new role for BiP

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Polypeptide‐binding proteins mediate completion of co‐translational protein translocation into the mammalian endoplasmic reticulum

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The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum

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Mammalian Sec61 Is Associated with Sec62 and Sec63

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Homologs of the yeast Sec complex subunits Sec62p and Sec63p are abundant proteins in dog pancreas microsomes

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A novel type of co‐chaperone mediates transmembrane recruitment of DnaK‐like chaperones to ribosomes

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ERj1p has a basic role in protein biogenesis at the endoplasmic reticulum

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ERj1p uses a universal ribosomal adaptor site to coordinate the 80S ribosome at the membrane

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Evolutionary Gain of Function for the ER Membrane Protein Sec62 from Yeast to Humans

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A protein of the endoplasmic reticulum involved early in polypeptide translocation

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Signal sequence-dependent function of the TRAM protein during early phases of protein transport across the endoplasmic reticulum membrane.

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TRAM Regulates the Exposure of Nascent Secretory Proteins to the Cytosol during Translocation into the Endoplasmic Reticulum

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A tetrameric complex of membrane proteins in the endoplasmic reticulum

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Substrate-specific function of the translocon-associated protein complex during translocation across the ER membrane

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Stress-Associated Endoplasmic Reticulum Protein 1 (Serp1)/Ribosome-Associated Membrane Protein 4 (Ramp4) Stabilizes Membrane Proteins during Stress and Facilitates Subsequent Glycosylation

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Control of glycosylation of MHC class II‐associated invariant chain by translocon‐associated RAMP4

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Different Transmembrane Domains Associate with Distinct Endoplasmic Reticulum Components during Membrane Integration of a Polytopic Protein

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Role of the Cytoplasmic Segments of Sec61α in the Ribosome-Binding and Translocation-Promoting Activities of the Sec61 Complex

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

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

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Alignment of Conduits for the Nascent Polypeptide Chain in the Ribosome-Sec61 Complex

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The Structure of Ribosome-Channel Complexes Engaged in Protein Translocation

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

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

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

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X-ray structure of a protein-conducting channel

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The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer

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Large aqueous channels in membrane vesicles derived from the rough endoplasmic reticulum of canine pancreas or the plasma membrane of Escherichia coli.

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A protein-conducting channel in the endoplasmic reticulum

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The Sec61p Complex Is a Dynamic Precursor Activated Channel

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Lanthanum ions inhibit the mammalian Sec61 complex in its channel dynamics and protein transport activity

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

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

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Bidirectional movement of a nascent polypeptide across microsomal membranes reveals requirements for vectorial translocation of proteins

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Protein Disulphide Isomerase and a Lumenal Cyclophilin-Type Peptidyl Prolyl Cis-Trans Isomerase are in Transient Contact with Secretory Proteins During Late Stages of Translocation

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Pancreas specific protein disulfide isomerase, PDIp, is in transient contact with secretory proteins during late stages of translocation

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The Role of ATP in the Functional Cycle of the DnaK Chaperone System

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The Second Step of ATP Binding to DnaK Induces Peptide Release

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Identification of the peptide binding domain of hsc70. 18-Kilodalton fragment located immediately after ATPase domain is sufficient for high affinity binding.

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Peptide-binding specificity of the molecular chaperone BiP

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Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP

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Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function

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Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ

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Eukaryotic DnaJ homologs and the specificity of Hsp70 activity

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A Bipartite Signaling Mechanism Involved in DnaJ-mediated Activation of the Escherichia coli DnaK Protein

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Mechanism of regulation of Hsp70 chaperones by DnaJ cochaperones

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An Essential Role for the Substrate-Binding Region of Hsp40s in Saccharomyces cerevisiae

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Not all J domains are created equal: Implications for the specificity of Hsp40–Hsp70 interactions

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Chaperone action in the posttranslational topological reorientation of the hepatitis B virus large envelope protein: Implications for translocational regulation

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Mammalian BiP controls posttranslational ER translocation of the hepatitis B virus large envelope protein

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Topology of the Membrane-Associated Hepatitis C Virus Protein NS4B

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The Adenovirus E3-6.7K Protein Adopts Diverse Membrane Topologies following Posttranslational Translocation

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Reorientation of Aquaporin-1 Topology during Maturation in the Endoplasmic Reticulum

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Membrane protein topology: effects of delta mu H+ on the translocation of charged residues explain the ‘positive inside’ rule.

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Co- and Posttranslational Translocation Mechanisms Direct Cystic Fibrosis Transmembrane Conductance Regulator N Terminus Transmembrane Assembly

resolves10.1091/mbc.9.9.2681

Coupled Translocation Events Generate Topological Heterogeneity at the Endoplasmic Reticulum Membrane

resolves10.1007/s00232-004-0715-6

Biogenesis of CFTR and other Polytopic Membrane Proteins: New Rolesfor the Ribosome-Translocon Complex

resolves10.1083/jcb.200711107

The expanding role of the ER translocon in membrane protein folding

resolves10.1016/j.cub.2005.02.043

Polytopic Proteins: Preventing Aggregation in the Membrane

resolves10.1074/jbc.M410329200

Ribophorin I Associates with a Subset of Membrane Proteins after Their Integration at the Sec61 Translocon

resolves10.1038/nsmb1005-834

Helices on the move

resolves10.1038/nature03216

Recognition of transmembrane helices by the endoplasmic reticulum translocon

resolves10.1126/science.1109176

Membrane Insertion of a Potassium-Channel Voltage Sensor

resolves10.1038/nature06387

Molecular code for transmembrane-helix recognition by the Sec61 translocon

resolves10.1073/pnas.0711151105

Prediction of membrane-protein topology from first principles

resolves10.1093/bioinformatics/btn114

Prediction of the translocon-mediated membrane insertion free energies of protein sequences

resolves10.1093/bioinformatics/btn255

MINS2: Revisiting the molecular code for transmembrane-helix recognition by the Sec61 translocon

resolves10.1021/bi991740r

Transmembrane Biogenesis of Kv1.3

resolves10.1016/j.jmb.2009.02.035

Membrane-integration Characteristics of Two ABC Transporters, CFTR and P-glycoprotein

resolves10.1099/vir.0.81140-0

Contribution of the charged residues of hepatitis C virus glycoprotein E2 transmembrane domain to the functions of the E1E2 heterodimer

resolves10.1128/JVI.02198-06

Transmembrane Domains of Hepatitis C Virus Envelope Glycoproteins: Residues Involved in E1E2 Heterodimerization and Involvement of These Domains in Virus Entry

resolves10.1007/s00894-010-0672-1

Contribution of charged and polar residues for the formation of the E1–E2 heterodimer from Hepatitis C Virus

resolves10.1073/pnas.0905394106

Protein contents in biological membranes can explain abnormal solvation of charged and polar residues

resolves10.1038/nature03821

A substrate-specific inhibitor of protein translocation into the endoplasmic reticulum

resolves10.1038/nature03670

Selective inhibition of cotranslational translocation of vascular cell adhesion molecule 1

resolves10.1242/jcs.054494

Eeyarestatin I inhibits Sec61-mediated protein translocation at the endoplasmic reticulum

resolves10.1074/jbc.M404857200

Small Molecule Modulators of Endogenous and Co-chaperone-stimulated Hsp70 ATPase Activity

resolves10.1042/BJ20081787

Post-translational import of protein into the endoplasmic reticulum of a trypanosome: an in vitro system for discovery of anti-trypanosomal chemical entities

resolves10.2337/db08-1362

A Point Mutation in Sec61α1 Leads to Diabetes and Hepatosteatosis in Mice

resolves10.1158/0008-5472.CAN-09-2775

Glioblastoma Proto-oncogene SEC61γ Is Required for Tumor Cell Survival and Response to Endoplasmic Reticulum Stress

resolves10.1158/1541-7786.MCR-05-0165

Genomic and Expression Analysis of the 3q25-q26 Amplification Unit Reveals TLOC1/SEC62 as a Probable Target Gene in Prostate Cancer

resolves10.1053/j.gastro.2004.12.051

HNPCC-associated small bowel cancer: Clinical and molecular characteristics

resolves10.1200/JCO.2005.00.695

Molecular Staging for Survival Prediction of Colorectal Cancer Patients

resolves10.1038/ng1357

Mutations in SEC63 cause autosomal dominant polycystic liver disease

resolves10.1016/j.molmed.2004.11.004

Polycystic liver disease is a disorder of cotranslational protein processing

resolves10.1038/ng1677

The gene disrupted in Marinesco-Sjögren syndrome encodes SIL1, an HSPA5 cochaperone

resolves10.1038/ng1678

Mutations in SIL1 cause Marinesco-Sjögren syndrome, a cerebellar ataxia with cataract and myopathy

resolves10.1038/ng1620

Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP

resolves10.1038/nature05124

AB5 subtilase cytotoxin inactivates the endoplasmic reticulum chaperone BiP

The 8 references without a DOI — listed, not checked

no DOI — not checkedGpi19, the Saccharomyces cerevisiae homologue of mammalian PIG-P, is a subunit of the initial enzyme for glyco-sylphosphatidylinositol anchor biosynthesis

no DOI — not checkedRNA translation on the endoplasmic reticulum: kinetic advantages to protein synthesis on the ER

no DOI — not checkedSec complexes in the yeast ER

no DOI — not checkedRegulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange

no DOI — not checkedMembrane protein biosynthesis at the endoplasmic reticulum

no DOI — not checkedApraxotin A reversibly inhibits the secretory pathway by preventing cotranslational translocation

no DOI — not checkedInstabilotyping reveals unique mutational spectra in microsatellite-unstable gastric cancers

no DOI — not checkedMembrane insertion of tail-anchored proteins

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