The immunological properties of endoplasmic reticulum chaperones: A conflict of interest?

Christopher V. Nicchitta, Robyn C Reed

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

• ER chaperones are abundant and highly conserved proteins that display both peptide binding and chaperone activity. • Of the family of chaperones present in the mammalian ER, GRP94 and calreticulin are apparently unique in their ability to elicit CD8+ T-cell responses against components of their bound-peptide pools. • The ability of GRP94 and calreticulin to elicit CD8+ T-cell responses indicates that both proteins bind peptides suitable for assembly on to MHC class-I molecules. • The capacity to function as molecular chaperones and as peptide-bind-ing proteins capable of transferring, directly or indirectly, peptides on to class-I molecules, indicates that GRP94 and calreticulin participate in the regulation of both peptide and polypeptide traffic in the ER. • Perspectives on the regulation of and interplay between the peptide binding and chaperone activity of GRP94 and calreticulin are discussed.

Original languageEnglish (US)
Pages (from-to)15-25
Number of pages11
JournalEssays in Biochemistry
Volume36
DOIs
StatePublished - Jan 1 2000

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