Cited by 209

The DOI matches its Crossref record.

GRP94 in ER quality control and stress responses

Eletto, Davide, Dersh, Devin, Argon, Yair·2010·Seminars in Cell & Developmental Biology

Verifying this paper

8 of 9 steps done · this page updates itself — you can leave and come back

  1. Registry recordVerified
  2. Full textFetching the open-access text — a few minutes for a paper we haven’t read before
  3. Reference listNot fetched yet
  4. Reference checkNot run yet for this paper
  5. StatisticsNeeds the full text
  6. ClaimsNeeds the full text
  7. Cited sourcesNeeds claims to check
  8. Self-checkNeeds the full text
  9. VerificationFindings verified

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/j.semcdb.2010.03.004

Cites

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

No references could be resolved yet.

Research works printed but not linked: 92

  1. Shiu, 1977, Glucose depletion accounts for the induction of two transformation-sensitive membrane proteins in Rous sarcoma virus-transformed chick embryo fibroblasts, Proc Natl Acad Sci USA, 74, 3840, 10.1073/pnas.74.9.3840 · DOI
  2. Kang, 1991, Characterization and purification of the 94-kDa glucose-regulated protein, J Biol Chem, 266, 5643, 10.1016/S0021-9258(19)67643-X · DOI
  3. Argon, 1999, GRP94, an ER chaperone with protein and peptide binding properties, Semin Cell Dev Biol, 10, 495, 10.1006/scdb.1999.0320 · DOI
  4. Srivastava, 2006, Therapeutic cancer vaccines, Curr Opin Immunol, 18, 201, 10.1016/j.coi.2006.01.009 · DOI
  5. Baker-LePain, 2003, ISO: a critical evaluation of the role of peptides in heat shock/chaperone protein-mediated tumor rejection, Curr Opin Immunol, 15, 89, 10.1016/S0952791502000067 · DOI
  6. Nemoto, 1996, Dimerization characteristics of the 94-kDa glucose-regulated protein, J Biochem (Tokyo), 120, 249, 10.1093/oxfordjournals.jbchem.a021406 · DOI
  7. Wearsch, 1996, Endoplasmic reticulum chaperone GRP94 subunit assembly is regulated through a defined oligomerization domain, Biochemistry, 35, 16760, 10.1021/bi962068q · DOI
  8. Dollins, 2007, Structures of GRP94–nucleotide complexes reveal mechanistic differences between the hsp90 chaperones, Mol Cell, 28, 41, 10.1016/j.molcel.2007.08.024 · DOI
  9. Immormino, 2004, Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone, J Biol Chem, 279, 46162, 10.1074/jbc.M405253200 · DOI
  10. Krukenberg, 2009, Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide, Protein Sci, 10.1002/pro.191 · DOI
  11. Soldano, 2003, Structure of the N-terminal domain of GRP94: basis for ligand specificity and regulation, J Biol Chem, 278, 48330, 10.1074/jbc.M308661200 · DOI
  12. Krukenberg, 2009, 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, J Mol Biol, 390, 278, 10.1016/j.jmb.2009.04.080 · DOI
  13. Gidalevitz, 2004, Identification of the N-terminal peptide binding site of glucose-regulated protein 94, J Biol Chem, 279, 16543, 10.1074/jbc.M313060200 · DOI
  14. Biswas, 2006, The N-terminal fragment of GRP94 is sufficient for peptide presentation via professional APCs, Int Immunol, 18, 1147, 10.1093/intimm/dxl049 · DOI
  15. Berwin, 2002, CD91-independent cross-presentation of GRP94(gp96)-associated peptides, J Immunol, 168, 4282, 10.4049/jimmunol.168.9.4282 · DOI
  16. Berwin, 2003, Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells, EMBO J, 22, 6127, 10.1093/emboj/cdg572 · DOI
  17. Schulte, 1999, Interaction of radicicol with members of the heat shock protein 90 family of molecular chaperones, Mol Endocrinol, 13, 1435, 10.1210/me.13.9.1435 · DOI
  18. Schulte, 1998, Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin, Cell Stress Chaperones, 3, 100, 10.1379/1466-1268(1998)003<0100:ARBTTN>2.3.CO;2 · DOI
  19. Ostrovsky, 2009, The chaperone activity of GRP94 towards of insulin-like growth factor II is necessary for the stress response to serum deprivation, Mol Biol Cell, 20, 1855, 10.1091/mbc.E08-04-0346 · DOI · Paper page
  20. Vogen, 2002, Radicicol-sensitive peptide binding to the N-terminal portion of GRP94, J Biol Chem, 277, 40742, 10.1074/jbc.M205323200 · DOI
  21. Rosser, 2000, Ligand interactions in the adenosine nucleotide binding domain of the Hsp90 chaperone, GRP94. I. Evidence for allosteric regulation of ligand binding, J Biol Chem, 275, 22798, 10.1074/jbc.M001477200 · DOI
  22. Wearsch, 1997, Interaction of endoplasmic reticulum chaperone GRP94 with peptide substrates is adenine nucleotide-independent, J Biol Chem, 272, 5152, 10.1074/jbc.272.8.5152 · DOI
  23. Frey, 2007, The ATPase cycle of the endoplasmic chaperone Grp94, J Biol Chem, 282, 35612, 10.1074/jbc.M704647200 · DOI
  24. Ostrovsky, 2009, An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells, Proc Natl Acad Sci USA, 106, 11600, 10.1073/pnas.0902626106 · DOI
  25. Bergerat, 1997, An atypical topoisomerase II from Archaea with implications for meiotic recombination, Nature, 386, 414, 10.1038/386414a0 · DOI
  26. Dutta, 2000, GHKL, an emergent ATPase/kinase superfamily, Trends Biochem Sci, 25, 24, 10.1016/S0968-0004(99)01503-0 · DOI
  27. Richter, 2006, hsp90: twist and fold, Cell, 127, 251, 10.1016/j.cell.2006.10.004 · DOI
  28. Biswas, 2007, The peptide binding activity of GRP94 is regulated by calcium, Biochem J, 405, 233, 10.1042/BJ20061867 · DOI
  29. Bruneau, 1998, Participation of GRP94-related protein in secretion of pancreatic bile salt-dependent lipase and in its internalization by the intestinal epithelium, J Cell Sci, 111, 2665, 10.1242/jcs.111.17.2665 · DOI
  30. Altmeyer, 1996, Tumor-specific cell surface expression of the KDEL containing, endoplasmic reticular heat shock protein gp96, Int J Cancer, 69, 340, 10.1002/(SICI)1097-0215(19960822)69:4<340::AID-IJC18>3.0.CO;2-9 · DOI
  31. Koo, 2010, Cell-surface processing of the metalloprotease pro-ADAMTS9 is influenced by the chaperone GRP94/gp96, J Biol Chem, 285, 197, 10.1074/jbc.M109.039677 · DOI
  32. Lev, 2009, Efficient cross-priming of antiviral CD8+ T cells by antigen donor cells is GRP94 independent, J Immunol, 183, 4205, 10.4049/jimmunol.0901828 · DOI
  33. Dollins, 2005, Structure of unliganded GRP94, the endoplasmic reticulum Hsp90. Basis for nucleotide-induced conformational change, J Biol Chem, 280, 30438, 10.1074/jbc.M503761200 · DOI
  34. Ge, 2006, Design, synthesis, and biological evaluation of hydroquinone derivatives of 17-amino-17-demethoxygeldanamycin as potent, water-soluble inhibitors of Hsp90, J Med Chem, 49, 4606, 10.1021/jm0603116 · DOI
  35. Prodromou, 1997, Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone, Cell, 90, 65, 10.1016/S0092-8674(00)80314-1 · DOI
  36. McLaughlin, 2004, Independent ATPase activity of Hsp90 subunits creates a flexible assembly platform, J Mol Biol, 344, 813, 10.1016/j.jmb.2004.09.055 · DOI
  37. Pearl, 2006, Structure and mechanism of the Hsp90 molecular chaperone machinery, Annu Rev Biochem, 75, 271, 10.1146/annurev.biochem.75.103004.142738 · DOI · Paper page
  38. Chu, 2006, Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94, Protein Sci, 15, 1260, 10.1110/ps.052065106 · DOI
  39. Hessling, 2009, Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90, Nat Struct Mol Biol, 16, 287, 10.1038/nsmb.1565 · DOI
  40. Ishiguro, 2002, SHEPHERD is the Arabidopsis GRP94 responsible for the formation of functional CLAVATA proteins, EMBO J, 21, 898, 10.1093/emboj/21.5.898 · DOI
  41. Maynard, 2010, Gp93, the Drosophila GRP94 ortholog, is required for gut epithelial homeostasis and nutrient assimilation-coupled growth control, Dev Biol, 10.1016/j.ydbio.2009.12.023 · DOI
  42. Wanderling, 2007, GRP94 is essential for mesoderm induction and muscle development because it regulates IGF secretion, Mol Biol Cell, 18, 3764, 10.1091/mbc.E07-03-0275 · DOI
  43. Randow, 2001, Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability, Nat Cell Biol, 3, 891, 10.1038/ncb1001-891 · DOI · Paper page
  44. Yang, 2005, Roles of heat shock protein gp96 in the ER quality control: redundant or unique function?, Mol Cells, 20, 173, 10.1016/S1016-8478(23)13214-6 · DOI
  45. Morales, 2009, 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 integrins, J Immunol, 183, 5121, 10.4049/jimmunol.0900811 · DOI · Paper page
  46. Melnick, 1994, Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum, Nature, 370, 373, 10.1038/370373a0 · DOI
  47. Liu, 2008, Endoplasmic reticulum HSP90b1 (gp96, grp94) optimizes B-cell function via chaperoning integrin and TLR but not immunoglobulin, Blood, 112, 1223, 10.1182/blood-2008-03-143107 · DOI · Paper page
  48. Ostrovsky, 2010, Glucose regulated protein 94 is required for muscle differentiation through its control of the autocrine production of insulin-like growth factors, BBA-Mol Cell, 1803, 333
  49. Muresan, 1997, Thyroglobulin transport along the secretory pathway. Investigation of the role of molecular chaperone, GRP94, in protein export from the endoplasmic reticulum [published erratum appears in J Biol Chem 1997 Nov 28;272(48):30590], J Biol Chem, 272, 26095, 10.1074/jbc.272.42.26095 · DOI
  50. Meldolesi, 1998, The endoplasmic reticulum Ca2+ store: a view from the lumen, Trends Biochem Sci, 23, 10, 10.1016/S0968-0004(97)01143-2 · DOI
  51. Macer, 1988, Identification of a set of calcium-binding protein in reticuloplasm, the luminal content of the endoplasmic reticulum, J Cell Sci, 91, 61, 10.1242/jcs.91.1.61 · DOI
  52. Van, 1989, 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, J Biol Chem, 264, 17494, 10.1016/S0021-9258(18)71521-4 · DOI
  53. Cala, 1994, GRP94 resides within cardiac sarcoplasmic reticulum vesicles and is phosphorylated by casein kinase II, J Biol Chem, 269, 5926, 10.1016/S0021-9258(17)37550-6 · DOI
  54. Baksh, 1991, Expression of calreticulin in Escherichia coli and identification of its Ca2+ binding domains, J Biol Chem, 266, 21458, 10.1016/S0021-9258(18)54661-5 · DOI
  55. Obermoeller, 1998, Ca2+ and receptor-associated protein are independently required for proper folding and disulfide bond formation of the low density lipoprotein receptor-related protein, J Biol Chem, 273, 22374, 10.1074/jbc.273.35.22374 · DOI
  56. Di Jeso, 2003, Folding of thyroglobulin in the calnexin/calreticulin pathway and its alteration by loss of Ca2+ from the endoplasmic reticulum, Biochem J, 370, 449, 10.1042/bj20021257 · DOI
  57. Vitadello, 2003, Overexpression of the stress protein Grp94 reduces cardiomyocyte necrosis due to calcium overload and simulated ischemia, FASEB J, 17, 923, 10.1096/fj.02-0644fje · DOI
  58. Gorza, 2000, Reduced amount of the glucose-regulated protein GRP94 in skeletal myoblasts results in loss of fusion competence, FASEB J, 14, 461, 10.1096/fasebj.14.3.461 · DOI
  59. Christianson, 2008, OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD, Nat Cell Biol, 10, 272, 10.1038/ncb1689 · DOI · Paper page
  60. Szathmary, 2005, Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD, Mol Cell, 19, 765, 10.1016/j.molcel.2005.08.015 · DOI
  61. Kim, 2005, Yos9p detects and targets misfolded glycoproteins for ER-associated degradation, Mol Cell, 19, 753, 10.1016/j.molcel.2005.08.010 · DOI
  62. Alcock, 2009, Mammalian OS-9 is upregulated in response to endoplasmic reticulum stress and facilitates ubiquitination of misfolded glycoproteins, J Mol Biol, 385, 1032, 10.1016/j.jmb.2008.11.045 · DOI
  63. Bhamidipati, 2005, Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen, Mol Cell, 19, 741, 10.1016/j.molcel.2005.07.027 · DOI
  64. Bernasconi, 2008, A dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposal, J Biol Chem, 283, 16446, 10.1074/jbc.M802272200 · DOI
  65. Hu, 2007, XBP-1, a key regulator of unfolded protein response, activates transcription of IGF1 and Akt phosphorylation in zebrafish embryonic cell line, Biochem Biophys Res Commun, 359, 778, 10.1016/j.bbrc.2007.05.183 · DOI
  66. Marchand, 2006, Endoplasmic reticulum stress induction of insulin-like growth factor-binding protein-1 involves ATF4, J Biol Chem, 281, 19124, 10.1074/jbc.M602157200 · DOI
  67. Wilson, 2006, Control of MyoD function during initiation of muscle differentiation by an autocrine signaling pathway activated by insulin-like growth factor-II, J Biol Chem, 281, 29962, 10.1074/jbc.M605445200 · DOI
  68. Nakanishi, 2005, Endoplasmic reticulum stress signaling transmitted by ATF6 mediates apoptosis during muscle development, J Cell Biol, 169, 555, 10.1083/jcb.200412024 · DOI
  69. Novosyadlyy, 2008, Insulin-like growth factor-I protects cells from ER stress-induced apoptosis via enhancement of the adaptive capacity of endoplasmic reticulum, Cell Death Differ, 15, 1304, 10.1038/cdd.2008.52 · DOI
  70. Ozcan, 2008, Loss of the tuberous sclerosis complex tumor suppressors triggers the unfolded protein response to regulate insulin signaling and apoptosis, Mol Cell, 29, 541, 10.1016/j.molcel.2007.12.023 · DOI
  71. Calfon, 2002, IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA, Nature, 415, 92, 10.1038/415092a · DOI
  72. van Anken, 2003, Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion, Immunity, 18, 243, 10.1016/S1074-7613(03)00024-4 · DOI
  73. Chang, 1989, Glucose-regulated protein (GRP94 and GRP78) genes share common regulatory domains and are coordinately regulated by common trans-acting factors, Mol Cell Biol, 9, 2153, 10.1128/MCB.9.5.2153 · DOI
  74. Drummond, 1987, Depletion of intracellular calcium stores by calcium ionophore A23187 induces the genes for glucose-regulated proteins in hamster fibroblasts, J Biol Chem, 262, 12801, 10.1016/S0021-9258(18)45277-5 · DOI
  75. Lee, 1987, Coordinated regulation of a set of genes by glucose and calcium ionophores in mammalian cells, Trends Biochem Sci, 12, 20, 10.1016/0968-0004(87)90011-9 · DOI
  76. Wiest, 1990, Membrane biogenesis during B cell differentiation: most endoplasmic reticulum proteins are expressed coordinately, J Cell Biol, 110, 1501, 10.1083/jcb.110.5.1501 · DOI
  77. Iwakoshi, 2003, Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP-1, Nat Immunol, 4, 321, 10.1038/ni907 · DOI · Paper page
  78. Lee, 2003, XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response, Mol Cell Biol, 23, 7448, 10.1128/MCB.23.21.7448-7459.2003 · DOI
  79. Meunier, 2002, A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins, Mol Biol Cell, 13, 4456, 10.1091/mbc.E02-05-0311 · DOI
  80. Snapp, 2006, Monitoring chaperone engagement of substrates in the endoplasmic reticulum of live cells, Proc Natl Acad Sci USA, 103, 6536, 10.1073/pnas.0510657103 · DOI
  81. Xu, 1998, BiP (GRP78) and endoplasmin (GRP94) are induced following rotavirus infection and bind transiently to an endoplasmic reticulum-localized virion component, J Virol, 72, 9865, 10.1128/JVI.72.12.9865-9872.1998 · DOI
  82. Linnik, 1998, Multiple molecular chaperones interact with apolipoprotein B during its maturation. The network of endoplasmic reticulum-resident chaperones (ERp72, GRP94, calreticulin, and BiP) interacts with apolipoprotein b regardless of its lipidation state, J Biol Chem, 273, 21368, 10.1074/jbc.273.33.21368 · DOI
  83. Molinari, 2000, Chaperone selection during glycoprotein translocation into the endoplasmic reticulum, Science, 288, 331, 10.1126/science.288.5464.331 · DOI
  84. Kapulkin, 2005, Compensatory regulation among ER chaperones in C. elegans, FEBS Lett, 579, 3063, 10.1016/j.febslet.2005.04.062 · DOI
  85. Sasagawa, 2007, ER E3 ubiquitin ligase HRD-1 and its specific partner chaperone BiP play important roles in ERAD and developmental growth in Caenorhabditis elegans, Genes Cells, 12, 1063, 10.1111/j.1365-2443.2007.01108.x · DOI
  86. Bernasconi, 2010, Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates, J Cell Biol, 188, 223, 10.1083/jcb.200910042 · DOI
  87. Maruri-Avidal, 2008, Endoplasmic reticulum chaperones are involved in the morphogenesis of rotavirus infectious particles, J Virol, 82, 5368, 10.1128/JVI.02751-07 · DOI
  88. Wolfson, 2008, Subtilase cytotoxin activates PERK, IRE1 and ATF6 endoplasmic reticulum stress-signalling pathways, Cell Microbiol, 10, 1775, 10.1111/j.1462-5822.2008.01164.x · DOI
  89. Mimura, 2008, Altered quality control in the endoplasmic reticulum causes cortical dysplasia in knock-in mice expressing a mutant BiP, Mol Cell Biol, 28, 293, 10.1128/MCB.00473-07 · DOI
  90. Mimura, 2007, Aberrant quality control in the endoplasmic reticulum impairs the biosynthesis of pulmonary surfactant in mice expressing mutant BiP, Cell Death Differ, 14, 1475, 10.1038/sj.cdd.4402151 · DOI
  91. Mesaeli, 1999, Calreticulin is essential for cardiac development, J Cell Biol, 144, 857, 10.1083/jcb.144.5.857 · DOI
  92. Ye, 2010, Grp78 heterozygosity promotes adaptive unfolded protein response and attenuates diet-induced obesity and insulin resistance, Diabetes, 59, 6, 10.2337/db09-0755 · DOI

Cited by

Sorted by citations

Metadata

Authors
Eletto, D., Dersh, D., & Argon, Y.
Venue
Seminars in Cell & Developmental Biology
Publisher
Elsevier BV
Published
2010-07
Volume
21
Issue
5
Pages
479-485
ISSN
1084-9521
Cited by
209
References
0
Language
en

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review