2002
DOI: 10.1016/s1074-7613(02)00263-7
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Disulfide Bond Isomerization and the Assembly of MHC Class I-Peptide Complexes

Abstract: The presence of a disulfide bond inside the peptide binding groove of MHC class I molecules and of the thiol oxidoreductase ERp57 in the class I loading complex suggests that disulfide bond isomerization may play a role in peptide loading. Here we show that ERp57 and tapasin are disulfide linked inside the loading complex. Mutagenesis of cysteine 95 in tapasin not only abolishes formation of the ERp57-tapasin bond but also prevents complete oxidation of the class I heavy chain in the loading complex. The resul… Show more

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Cited by 207 publications
(333 citation statements)
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“…65) and/or isomerization of the ␣2 domain disulfide bonds (as monitored by ERp57; Ref. 29). Regardless of the role served by the loading complex during MR1 biogenesis, MR1 represents the most divergent member of the class I family known to interact with this complex.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…65) and/or isomerization of the ␣2 domain disulfide bonds (as monitored by ERp57; Ref. 29). Regardless of the role served by the loading complex during MR1 biogenesis, MR1 represents the most divergent member of the class I family known to interact with this complex.…”
Section: Discussionmentioning
confidence: 99%
“…This complex of calreticulin, TAP, tapasin, and ERp57 has been referred to as the peptide-loading complex. In this complex, TAP provides the peptides that bind H chain/␤ 2 m heterodimers, tapasin facilitates the binding of high affinity peptides (28), and ERp57 facilitates disulfide bond formation in tapasin or the H chain (29). Association of MR1 with any of the ER proteins implicated in the full assembly of classical class I molecules has not been defined, but would help determine the molecular mechanism of MR1 assembly.…”
mentioning
confidence: 99%
“…Emerging evidence suggests that the various transient intra-and intermolecular disulfides are formed among components of the peptide-loading complex (Chambers et al, 2008) and that thiol-dependent redox regulation is vital for the assembly of MHC class I-peptide complexes (Dick, 2004). ERp57 exists in the PLC as a disulfide-linked heterodimer with tapasin (Dick et al, 2002;Peaper et al, 2005). ERp57 forms this disulfide interaction through its N-terminal thioredoxin-like domain with the Cys95 residue of tapasin (Dick et al, 2002).…”
Section: Introductionmentioning
confidence: 99%
“…ERp57 exists in the PLC as a disulfide-linked heterodimer with tapasin (Dick et al, 2002;Peaper et al, 2005). ERp57 forms this disulfide interaction through its N-terminal thioredoxin-like domain with the Cys95 residue of tapasin (Dick et al, 2002). The escape pathway (Walker and Gilbert, 1997) that is activated to release ERp57 from its substrates is inhibited by association with tapasin (Peaper et al, 2005), resulting in a stable tapasin-ERp57 disulfide conjugate.…”
Section: Introductionmentioning
confidence: 99%
“…[4][5][6][7][8][9][10] The first five of these associate to form the peptide-loading complex (PLC), which is believed to promote the assembly of peptide-receptive complexes with peptide within the ER. Unlike calreticulin, calnexin and ERp57, which have general chaperone functions, tapasin has a specialised role in MHC class I assembly.…”
Section: Introductionmentioning
confidence: 99%