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Nucleotide Binding by Lhs1p Is Essential for Its Nucleotide Exchange Activity and for Function in Vivo
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EDEM1 Recognition and Delivery of Misfolded Proteins to the SEL1L-Containing ERAD Complex
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ALS-linked mutant SOD1 induces ER stress- and ASK1-dependent motor neuron death by targeting Derlin-1
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Derlin-1 facilitates the retro-translocation of cholera toxin
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OS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
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SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins
Britta Mueller et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2008)
ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER
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O-mannosylation is required for degradation of the endoplasmic reticulum-associated degradation substrate Gas1*p via the ubiquitin/proteasome pathway in Saccharomyces cerevisiae
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Characterization of an ERAD pathway for nonglyclosylated BiP substrates, which require Herp
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Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6α and XBP1
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Derlin-1 promotes the efficient degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) and CFTR folding mutants
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Man2C1, an α-mannosidase, is involved in the trimming of free oligosaccharides in the cytosol
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EDEM1 regulates ER-associated degradation by accelerating de-mannosylation of folding-defective polypeptides and by inhibiting their covalent aggregation
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SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER
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Yeast Derlin Dfm1 interacts with Cdc48 and functions in ER homeostasis
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Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator
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A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery
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Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins
Pedro Carvalho et al.
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A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation
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The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptor
Guangtao Li et al.
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The MRH protein Erlectin is a member of the endoplasmic reticulum synexpression group and functions in N-glycan recognition
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The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitment
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EDEM3, a soluble EDEM homolog, enhances glycoprotein endoplasmic reticulum-associated degradation and mannose trimming
K Hirao et al.
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Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum
BM Wilkinson et al.
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Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI)
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Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways
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Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation
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Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane
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Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation
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NATURE CELL BIOLOGY (2005)
Ubx2 links the Cdc48 complex to ER-associated protein degradation
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NATURE CELL BIOLOGY (2005)
Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen
A Bhamidipati et al.
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Yos9p detects and targets misfolded glycoproteins for ER-associated degradation
W Kim et al.
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Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase
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Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD
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More than one glycan is needed for ER glucosidase II to allow entry of glycoproteins into the calnexin/calreticulin cycle
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TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum
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Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins
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Importance of carbohydrate positioning in the recognition of mutated CPY for ER-associated degradation
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Essential role of synoviolin in embryogenesis
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A novel stress-induced EDEM variant regulating endoplasmic reticulum-associated glycoprotein degradation
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ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates
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Der1p, a protein required for degradation of malfolded soluble proteins of the endoplasmic reticulum: topology and Der1-like proteins
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Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control
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Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum
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DER7, encoding α-glucosidase I is essential for degradation of malfolded glycoproteins of the endoplasmic reticulum
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A foldable CFTRΔF508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase
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P-domain and lectin site are involved in the chaperone function of Saccharomyces cerevisiae calnexin homologue
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Roles of O-mannosylation of aberrant proteins in reduction of the load for endoplasmic reticulum chaperones in yeast
K Nakatsukasa et al.
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The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum
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A genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins
BA Buschhorn et al.
FEBS LETTERS (2004)
A membrane protein required for dislocation of misfolded proteins from the ER
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A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
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Enhancement of endoplasmic reticulum (ER) degradation of misfolded null Hong Kong α1-antitrypsin by human ER mannosidase I
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Ngly1, a mouse gene encoding a deglycosylating enzyme implicated in proteasomal degradation:: expression, genomic organization, and chromosomal mapping
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EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin
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Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb)
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Identification and characterization of a novel endoplasmic reticulum (ER) DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is induced by ER stress
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JOURNAL OF BIOLOGICAL CHEMISTRY (2002)
Different effects of calnexin deletion in Saccharomyces cerevisiae on the secretion of two glycosylated amyloidogenic lysozymes
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FEBS LETTERS (2002)
Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48
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The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
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PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2001)
Effects of calnexin deletion in Saccharomyces cerevisiae on the secretion of glycosylated lysozymes
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Rad23 provides a link between the Png1 deglycosylating enzyme and the 26 S proteasome in yeast
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Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation
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Functional differences in yeast protein disulfide isomerases
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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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