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A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery
by
Hirsch, Christian
, Gauss, Robert
, Jarosch, Ernst
, Sommer, Thomas
in
Biomedical and Life Sciences
/ Blotting, Western
/ Cancer Research
/ Carrier Proteins - chemistry
/ Carrier Proteins - genetics
/ Carrier Proteins - metabolism
/ Cell Biology
/ Control systems
/ Developmental Biology
/ Endoplasmic reticulum
/ Endoplasmic Reticulum - metabolism
/ Hydrolysis
/ Immunoprecipitation
/ Lectins
/ letter
/ Life Sciences
/ Ligases
/ Membrane Glycoproteins - chemistry
/ Membrane Glycoproteins - genetics
/ Membrane Glycoproteins - metabolism
/ Physiological aspects
/ Plasmids - genetics
/ Polypeptides
/ Protein Binding
/ Protein Conformation
/ Protein Folding
/ Proteins
/ Quality control
/ Saccharomyces cerevisiae - genetics
/ Saccharomyces cerevisiae - metabolism
/ Saccharomyces cerevisiae Proteins - chemistry
/ Saccharomyces cerevisiae Proteins - genetics
/ Saccharomyces cerevisiae Proteins - metabolism
/ Stem Cells
/ Ubiquitin-proteasome system
/ Ubiquitin-Protein Ligases - chemistry
/ Ubiquitin-Protein Ligases - genetics
/ Ubiquitin-Protein Ligases - metabolism
2006
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A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery
by
Hirsch, Christian
, Gauss, Robert
, Jarosch, Ernst
, Sommer, Thomas
in
Biomedical and Life Sciences
/ Blotting, Western
/ Cancer Research
/ Carrier Proteins - chemistry
/ Carrier Proteins - genetics
/ Carrier Proteins - metabolism
/ Cell Biology
/ Control systems
/ Developmental Biology
/ Endoplasmic reticulum
/ Endoplasmic Reticulum - metabolism
/ Hydrolysis
/ Immunoprecipitation
/ Lectins
/ letter
/ Life Sciences
/ Ligases
/ Membrane Glycoproteins - chemistry
/ Membrane Glycoproteins - genetics
/ Membrane Glycoproteins - metabolism
/ Physiological aspects
/ Plasmids - genetics
/ Polypeptides
/ Protein Binding
/ Protein Conformation
/ Protein Folding
/ Proteins
/ Quality control
/ Saccharomyces cerevisiae - genetics
/ Saccharomyces cerevisiae - metabolism
/ Saccharomyces cerevisiae Proteins - chemistry
/ Saccharomyces cerevisiae Proteins - genetics
/ Saccharomyces cerevisiae Proteins - metabolism
/ Stem Cells
/ Ubiquitin-proteasome system
/ Ubiquitin-Protein Ligases - chemistry
/ Ubiquitin-Protein Ligases - genetics
/ Ubiquitin-Protein Ligases - metabolism
2006
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A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery
by
Hirsch, Christian
, Gauss, Robert
, Jarosch, Ernst
, Sommer, Thomas
in
Biomedical and Life Sciences
/ Blotting, Western
/ Cancer Research
/ Carrier Proteins - chemistry
/ Carrier Proteins - genetics
/ Carrier Proteins - metabolism
/ Cell Biology
/ Control systems
/ Developmental Biology
/ Endoplasmic reticulum
/ Endoplasmic Reticulum - metabolism
/ Hydrolysis
/ Immunoprecipitation
/ Lectins
/ letter
/ Life Sciences
/ Ligases
/ Membrane Glycoproteins - chemistry
/ Membrane Glycoproteins - genetics
/ Membrane Glycoproteins - metabolism
/ Physiological aspects
/ Plasmids - genetics
/ Polypeptides
/ Protein Binding
/ Protein Conformation
/ Protein Folding
/ Proteins
/ Quality control
/ Saccharomyces cerevisiae - genetics
/ Saccharomyces cerevisiae - metabolism
/ Saccharomyces cerevisiae Proteins - chemistry
/ Saccharomyces cerevisiae Proteins - genetics
/ Saccharomyces cerevisiae Proteins - metabolism
/ Stem Cells
/ Ubiquitin-proteasome system
/ Ubiquitin-Protein Ligases - chemistry
/ Ubiquitin-Protein Ligases - genetics
/ Ubiquitin-Protein Ligases - metabolism
2006
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A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery
Journal Article
A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery
2006
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Overview
A quality-control system surveys the lumen of the endoplasmic reticulum for terminally misfolded proteins. Polypeptides singled out by this system are ultimately degraded by the cytosolic ubiquitin-proteasome pathway. Key components of both the endoplasmic reticulum quality-control system and the degradation machinery have been identified, but a connection between the two systems has remained elusive. Here, we report an association between the endoplasmic reticulum quality-control lectin Yos9p and Hrd3p, a component of the ubiquitin-proteasome system that links these pathways. We identify designated regions in the luminal domain of Hrd3p that interact with Yos9p and the ubiquitin ligase Hrd1p. Binding of misfolded proteins occurs through Hrd3p, suggesting that Hrd3p recognises proteins that deviate from their native conformation, whereas Yos9p ensures that only terminally misfolded polypeptides are degraded.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ Carrier Proteins - chemistry
/ Carrier Proteins - metabolism
/ Endoplasmic Reticulum - metabolism
/ Lectins
/ letter
/ Ligases
/ Membrane Glycoproteins - chemistry
/ Membrane Glycoproteins - genetics
/ Membrane Glycoproteins - metabolism
/ Proteins
/ Saccharomyces cerevisiae - genetics
/ Saccharomyces cerevisiae - metabolism
/ Saccharomyces cerevisiae Proteins - chemistry
/ Saccharomyces cerevisiae Proteins - genetics
/ Saccharomyces cerevisiae Proteins - metabolism
/ Ubiquitin-Protein Ligases - chemistry
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