Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation

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Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation is …
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scholarly articleQ13442814

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P356DOI10.1083/JCB.153.5.1061
P3181OpenCitations bibliographic resource ID3843289
P932PMC publication ID2174341
P698PubMed publication ID11381090
P5875ResearchGate publication ID11957990

P2093author name stringY Kato
T Endo
J L Brodsky
S I Nishikawa
S W Fewell
P2860cites workSec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destructionQ24324602
Rapid and efficient site-specific mutagenesis without phenotypic selectionQ27860628
A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiaeQ27860636
A role for the DnaJ homologue Scj1p in protein folding in the yeast endoplasmic reticulumQ27929932
Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradationQ27930550
Genetic interactions between KAR7/SEC71, KAR8/JEM1, KAR5, and KAR2 during nuclear fusion in Saccharomyces cerevisiaeQ27930560
Ubiquitin-dependent protein degradationQ27931143
SSI1 encodes a novel Hsp70 of the Saccharomyces cerevisiae endoplasmic reticulum.Q27932136
The engagement of Sec61p in the ER dislocation processQ27932365
ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathwayQ27932376
A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursorsQ27932477
BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membraneQ27932673
A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70sQ27935309
Functional interaction of cytosolic hsp70 and a DnaJ-related protein, Ydj1p, in protein translocation in vivoQ27935347
The yeast JEM1p is a DnaJ-like protein of the endoplasmic reticulum membrane required for nuclear fusionQ27936580
SSS1 encodes a stabilizing component of the Sec61 subcomplex of the yeast protein translocation apparatus.Q27936612
Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulumQ27937605
The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogeneQ27937937
Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolasesQ27937990
Sec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membraneQ27938591
Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway.Q27939649
Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradationQ28131669
Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradationQ28247695
A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposomeQ28257113
BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeastQ28303811
Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeastQ29618500
Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaKQ29618850
Setting the standards: quality control in the secretory pathwayQ29620321
Yeast Saccharomyces cerevisiae selectable markers in pUC18 polylinkersQ29620747
Tackling the protease problem in Saccharomyces cerevisiaeQ29620845
Retrograde protein translocation: ERADication of secretory proteins in health and diseaseQ33676998
Surfing the Sec61 channel: bidirectional protein translocation across the ER membrane.Q33774962
ER protein quality control and proteasome-mediated protein degradationQ33794243
A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptidesQ34172156
Degradation of unassembled Vph1p reveals novel aspects of the yeast ER quality control systemQ34663301
A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulumQ34687189
Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fateQ35931446
Gene dosage-dependent secretion of yeast vacuolar carboxypeptidase Y.Q36214972
70-kD heat shock-related protein is one of at least two distinct cytosolic factors stimulating protein import into mitochondriaQ36220955
A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an Escherichia coli heat shock proteinQ36222319
Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiaeQ36236192
Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP.Q36236461
The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiaeQ36266890
Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeastQ36280501
Ste6p mutants defective in exit from the endoplasmic reticulum (ER) reveal aspects of an ER quality control pathway in Saccharomyces cerevisiaeQ36912883
Genetic interactions between KAR2 and SEC63, encoding eukaryotic homologues of DnaK and DnaJ in the endoplasmic reticulumQ37376425
Endoplasmic reticulum degradation of a mutated ATP-binding cassette transporter Pdr5 proceeds in a concerted action of Sec61 and the proteasome.Q38330998
Intracellular disposal of incompletely folded human alpha1-antitrypsin involves release from calnexin and post-translational trimming of asparagine-linked oligosaccharidesQ38347593
Determination of the transmembrane topology of yeast Sec61p, an essential component of the endoplasmic reticulum translocation complexQ38352353
A hitchhiker's guide to analysis of the secretory pathway in yeastQ38751290
Inhibition of endoplasmic reticulum (ER)-to-Golgi transport induces relocalization of binding protein (BiP) within the ER to form the BiP bodiesQ40366396
Role of the proteasome in membrane extraction of a short-lived ER-transmembrane proteinQ42646222
The Hsp70 homologue Lhs1p is involved in a novel function of the yeast endoplasmic reticulum, refolding and stabilization of heat-denatured protein aggregatesQ42837194
The J-domain family and the recruitment of chaperone powerQ45068628
Sec61p and BiP directly facilitate polypeptide translocation into the ER.Q45975576
70K heat shock related proteins stimulate protein translocation into microsomesQ49486847
The GTP-binding Sar1 protein is localized to the early compartment of the yeast secretory pathway.Q54694535
Oligomeric Rings of the Sec61p Complex Induced by Ligands Required for Protein TranslocationQ57189552
Binding of mitochondrial presequences to yeast cytosolic heat shock protein 70 depends on the amphiphilicity of the presequenceQ71070590
Degradation of a mutant secretory protein, alpha1-antitrypsin Z, in the endoplasmic reticulum requires proteasome activityQ71514672
Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cerevisiaeQ71762925
Cer1p, a novel Hsp70-related protein required for posttranslational endoplasmic reticulum translocation in yeastQ71825363
Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeastQ72679083
Distinct domains within yeast Sec61p involved in post-translational translocation and protein dislocationQ73316838
Degradation of proteins from the ER of S. cerevisiae requires an intact unfolded protein response pathwayQ73958524
BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocationQ74405725
Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY speciesQ74456148
Calnexin and BiP interact with acid phosphatase independently of glucose trimming and reglucosylation in Schizosaccharomyces pombeQ77710332
The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinctQ77912013
P433issue5
P407language of work or nameEnglishQ1860
P921main subjectendoplasmic reticulumQ79927
molecular chaperonesQ422496
Scj1p YMR214WQ27548925
Jem1p YJL073WQ27549562
Hsp70 family ATPase KAR2 YJL034WQ27551305
P304page(s)1061-70
P577publication date2001-05-28
P1433published inJournal of Cell BiologyQ1524550
P1476titleMolecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation
P478volume153

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