title: GRP94, an ER chaperone with protein and peptide binding properties.
abstract: GRP94 is the ER representative of the HSP90 family of stress-induced proteins. It binds to a limited number of proteins in the secretory pathway, apparently by recognizing advanced folding intermediates or incompletely assembled proteins, GRP94 also binds peptides and can act as a tumor vaccine, delivering the peptides for presentation to T lymphocytes. Here, we review the current data about GRP94 and propose a structural model that integrates the biochemical data and known functions of the protein.
authors.affiliation: Department of Pathology, University of Chicago, IL 60637, USA.
authors.forename: Y
authors.initials: Y
authors.lastname: Argon
authors.forename: B B
authors.initials: BB
authors.lastname: Simen
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D017951:Antigen Presentation; D002118:Calcium / Q000378:metabolism; D019496:Cancer Vaccines / Q000737:chemistry / Q000627:therapeutic use; D004721:Endoplasmic Reticulum / Q000378:metabolism; D005786:Gene Expression Regulation; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry / Q000502:physiology* / Q000627:therapeutic use; D018841:HSP90 Heat-Shock Proteins / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry / Q000502:physiology* / Q000627:therapeutic use; D051379:Mice; D018832:Molecular Chaperones / Q000737:chemistry / Q000502:physiology*; D008969:Molecular Sequence Data; D010455:Peptides / Q000378:metabolism; D011485:Protein Binding; D017510:Protein Folding; D011499:Protein Processing, Post-Translational; D017386:Sequence Homology, Amino Acid
chemical_list: D019496:Cancer Vaccines; D018840:HSP70 Heat-Shock Proteins; D018841:HSP90 Heat-Shock Proteins; D008565:Membrane Proteins; D018832:Molecular Chaperones; D010455:Peptides; C018551:glucose-regulated proteins; D000255:Adenosine Triphosphate; D002118:Calcium