Biochemical, cell biological and immunological issues surrounding the endoplasmic reticulum chaperone GRP94/gp96.
The past year has born witness to compelling demonstrations of the utility of peptide complexes with glucose regulated protein 94 (GRP94, also known as gp96) in cancer immunotherapy. Insights into the structural basis of peptide binding to GRP94 have been obtained and the role of the transporter for antigen presentation in defining the GRP94-bound peptide composition has been determined.
Nicchitta
C V
CV
Department of Cell Biology, Duke University Medical Center, Durham, NC 27710, USA. C.Nicchitta@cellbio.duke.edu
D000818:Animals; D000951:Antigens, Neoplasm / Q000737:chemistry / Q000276:immunology; D004721:Endoplasmic Reticulum / Q000378:metabolism; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D018832:Molecular Chaperones / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D010455:Peptides / Q000378:metabolism; D010802:Phylogeny; D013347:Subcellular Fractions
D000951:Antigens, Neoplasm; D018840:HSP70 Heat-Shock Proteins; D008565:Membrane Proteins; D018832:Molecular Chaperones; D010455:Peptides; C018551:glucose-regulated proteins