GRP 94 in ER Quality Control and Stress Responses

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  2013

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• Glucose regulated protein 94 is required for muscle differentiation through its control of the autocrine production of insulin-like growth factors.

  2010cited by this paper
• Gp93, the Drosophila GRP94 ortholog, is required for gut epithelial homeostasis and nutrient assimilation-coupled growth control.

  2010cited by this paper
• Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates

  2010cited by this paper
• Drosophila Glycoprotein 93 Is an Ortholog of Mammalian Heat Shock Protein gp96 (grp94, HSP90b1, HSPC4) and Retains Disulfide Bond-Independent Chaperone Function for TLRs and Integrins1

  2009cited by this paper
• An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells

  2009cited by this paper
• Efficient Cross-Priming of Antiviral CD8+ T Cells by Antigen Donor Cells Is GRP94 Independent1

  2009cited by this paper
• pH-dependent conformational changes in bacterial Hsp90 reveal a Grp94-like conformation at pH 6 that is highly active in suppression of citrate synthase aggregation.

  2009cited by this paper
• Grp 78 Heterozygosity Promotes Adaptive Unfolded Protein Response and Attenuates Diet-Induced Obesity and Insulin Resistance

  2009cited by this paper
• The chaperone activity of GRP94 toward insulin-like growth factor II is necessary for the stress response to serum deprivation.

  2009influential reference
• Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90

  2009cited by this paper
• Cell-surface Processing of the Metalloprotease Pro-ADAMTS9 Is Influenced by the Chaperone GRP94/gp96*

  2009cited by this paper
• Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide

  2009influential reference
• Mammalian OS-9 is upregulated in response to endoplasmic reticulum stress and facilitates ubiquitination of misfolded glycoproteins.

  2009cited by this paper
• Endoplasmic reticulum HSP90b1 (gp96, grp94) optimizes B-cell function via chaperoning integrin and TLR but not immunoglobulin.

  2008cited by this paper
• Subtilase cytotoxin activates PERK, IRE1 and ATF6 endoplasmic reticulum stress‐signalling pathways

  2008cited by this paper
• A Dual Task for the Xbp1-responsive OS-9 Variants in the Mammalian Endoplasmic Reticulum

  2008cited by this paper
• Endoplasmic Reticulum Chaperones Are Involved in the Morphogenesis of Rotavirus Infectious Particles

  2008influential reference
• OS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1–SEL1L ubiquitin ligase complex for ERAD

  2008influential reference
• Loss of the tuberous sclerosis complex tumor suppressors triggers the unfolded protein response to regulate insulin signaling and apoptosis.

  2008cited by this paper
• Insulin-like growth factor-I protects cells from ER stress-induced apoptosis via enhancement of the adaptive capacity of endoplasmic reticulum

  2008cited by this paper
• The peptide-binding activity of GRP94 is regulated by calcium.

  2007influential reference
• The ATPase Cycle of the Endoplasmic Chaperone Grp94*

  2007cited by this paper
• Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones.

  2007influential reference
• ER E3 ubiquitin ligase HRD‐1 and its specific partner chaperone BiP play important roles in ERAD and developmental growth in Caenorhabditis elegans

  2007cited by this paper
• GRP94 is essential for mesoderm induction and muscle development because it regulates insulin-like growth factor secretion.

  2007influential reference
• Altered Quality Control in the Endoplasmic Reticulum Causes Cortical Dysplasia in Knock-In Mice Expressing a Mutant BiP

  2007cited by this paper
• XBP-1, a key regulator of unfolded protein response, activates transcription of IGF1 and Akt phosphorylation in zebrafish embryonic cell line.

  2007cited by this paper
• Aberrant quality control in the endoplasmic reticulum impairs the biosynthesis of pulmonary surfactant in mice expressing mutant BiP

  2007cited by this paper
• Structure and mechanism of the Hsp90 molecular chaperone machinery.

  2006cited by this paper
• The N-terminal fragment of GRP94 is sufficient for peptide presentation via professional antigen-presenting cells.

  2006cited by this paper
• Therapeutic cancer vaccines.

  2006cited by this paper
• Endoplasmic Reticulum Stress Induction of Insulin-like Growth Factor-binding Protein-1 Involves ATF4*

  2006cited by this paper
• Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94

  2006cited by this paper
• Control of MyoD Function during Initiation of Muscle Differentiation by an Autocrine Signaling Pathway Activated by Insulin-like Growth Factor-II*

  2006cited by this paper
• Design, synthesis, and biological evaluation of hydroquinone derivatives of 17-amino-17-demethoxygeldanamycin as potent, water-soluble inhibitors of Hsp90.

  2006cited by this paper
• Monitoring chaperone engagement of substrates in the endoplasmic reticulum of live cells.

  2006cited by this paper
• Endoplasmic reticulum stress signaling transmitted by ATF6 mediates apoptosis during muscle development

  2005cited by this paper
• Yos9p detects and targets misfolded glycoproteins for ER-associated degradation.

  2005cited by this paper
• Compensatory regulation among ER chaperones in C. elegans

  2005cited by this paper
• Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD.

  2005cited by this paper
• Roles of heat shock protein gp96 in the ER quality control: redundant or unique function?

  2005cited by this paper
• Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen.

  2005cited by this paper
• Structure of Unliganded GRP94, the Endoplasmic Reticulum Hsp90

  2005cited by this paper
• Identification of the N-terminal Peptide Binding Site of Glucose-regulated Protein 94*

  2004cited by this paper
• Ligand-induced Conformational Shift in the N-terminal Domain of GRP94, an Hsp90 Chaperone*

  2004influential reference
• Independent ATPase activity of Hsp90 subunits creates a flexible assembly platform.

  2004cited by this paper
• XBP-1 Regulates a Subset of Endoplasmic Reticulum Resident Chaperone Genes in the Unfolded Protein Response

  2003cited by this paper
• ISO: a critical evaluation of the role of peptides in heat shock/chaperone protein-mediated tumor rejection.

  2003cited by this paper
• Structure of the N-terminal Domain of GRP94

  2003cited by this paper
• Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP-1

  2003cited by this paper
• Folding of thyroglobulin in the calnexin/calreticulin pathway and its alteration by loss of Ca2+ from the endoplasmic reticulum.

  2003cited by this paper
• Scavenger receptor‐A mediates gp96/GRP94 and calreticulin internalization by antigen‐presenting cells

  2003cited by this paper
• Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion.

  2003cited by this paper
• Overexpression of the stress‐protein Grp94 reduces cardiomyocyte necrosis due to calcium overload and simulated ischemia

  2003influential reference
• A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.

  2002cited by this paper
• Cutting Edge: CD91-Independent Cross-Presentation of GRP94(gp96)-Associated Peptides1

  2002cited by this paper
• Radicicol-sensitive Peptide Binding to the N-terminal Portion of GRP94*

  2002cited by this paper
• IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA

  2002cited by this paper
• SHEPHERD is the Arabidopsis GRP94 responsible for the formation of functional CLAVATA proteins

  2002cited by this paper
• Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability

  2001cited by this paper
• Reduced amount of the glucose‐regulated protein GRP94 in skeletal myoblasts results in loss of fusion competence

  2000cited by this paper
• GHKL, an emergent ATPase/kinase superfamily.

  2000cited by this paper
• Chaperone selection during glycoprotein translocation into the endoplasmic reticulum.

  2000cited by this paper
• Ligand Interactions in the Adenosine Nucleotide-binding Domain of the Hsp90 Chaperone, GRP94

  2000influential reference
• Calreticulin Is Essential for Cardiac Development

  1999cited by this paper
• GRP94, an ER chaperone with protein and peptide binding properties.

  1999cited by this paper
• Interaction of radicicol with members of the heat shock protein 90 family of molecular chaperones.

  1999cited by this paper
• Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin.

  1998cited by this paper
• Ca2+ and Receptor-associated Protein Are Independently Required for Proper Folding and Disulfide Bond Formation of the Low Density Lipoprotein Receptor-related Protein*

  1998cited by this paper
• The endoplasmic reticulum Ca2+ store: a view from the lumen.

  1998cited by this paper
• BiP (GRP78) and Endoplasmin (GRP94) Are Induced following Rotavirus Infection and Bind Transiently to an Endoplasmic Reticulum-Localized Virion Component

  1998cited by this paper
• Multiple Molecular Chaperones Interact with Apolipoprotein B during Its Maturation

  1998cited by this paper
• Participation of GRP94-related protein in secretion of pancreatic bile salt-dependent lipase and in its internalization by the intestinal epithelium.

  1998cited by this paper
• Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone.

  1997cited by this paper
• Thyroglobulin Transport along the Secretory Pathway

  1997cited by this paper
• An atypical topoisomerase II from archaea with implications for meiotic recombination

  1997cited by this paper
• Interaction of Endoplasmic Reticulum Chaperone GRP94 with Peptide Substrates Is Adenine Nucleotide-independent*

  1997cited by this paper
• Endoplasmic reticulum chaperone GRP94 subunit assembly is regulated through a defined oligomerization domain.

  1996cited by this paper
• Dimerization characteristics of the 94-kDa glucose-regulated protein.

  1996cited by this paper
• Tumor‐specific cell surface expression of the ‐KDEL containing endoplasmic reticular heat shock protein gp96

  1996cited by this paper
• GRP94 resides within cardiac sarcoplasmic reticulum vesicles and is phosphorylated by casein kinase II.

  1994cited by this paper
• Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum

  1994influential reference
• Expression of calreticulin in Escherichia coli and identification of its Ca2+ binding domains.

  1991cited by this paper
• Characterization and purification of the 94-kDa glucose-regulated protein.

  1991cited by this paper
• Membrane biogenesis during B cell differentiation: most endoplasmic reticulum proteins are expressed coordinately

  1990cited by this paper
• Four intracisternal calcium-binding glycoproteins from rat liver microsomes with high affinity for calcium. No indication for calsequestrin-like proteins in inositol 1,4,5-trisphosphate-sensitive calcium sequestering rat liver vesicles.

  1989cited by this paper
• Glucose-regulated protein (GRP94 and GRP78) genes share common regulatory domains and are coordinately regulated by common trans-acting factors

  1989influential reference
• Identification of a set of calcium-binding proteins in reticuloplasm, the luminal content of the endoplasmic reticulum.

  1988cited by this paper
• Coordinated regulation of a set of genes by glucose and calcium ionophores in mammalian cells

  1987influential reference
• Depletion of intracellular calcium stores by calcium ionophore A23187 induces the genes for glucose-regulated proteins in hamster fibroblasts.

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• Glucose depletion accounts for the induction of two transformation-sensitive membrane proteins in Rous sarcoma virus-transformed chick embryo fibroblasts ( glucose starvation / membrane proteins )

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• ER stress activation in the intestinal mucosa but not in mesenteric adipose tissue is associated with inflammation in Crohn’s disease patients

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• Modulation of the unfolded protein response by the human hepatitis B virus

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• Modelling the effect of GRP78 on anti-oestrogen sensitivity and resistance in breast cancer

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• Modelling the effect of GRP 78 on anti-oestrogen sensitivity and resistance in breast cancer

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• Effects of ubiquitin C-terminal hydrolase L1 deficiency on mouse ova.

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