Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing (Q24307979)

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Sungwook Lee

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Eunkyung Kim

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Kwangmin Cho

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Stanley R Riddell

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Sunglim Cho

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Kwangseog Ahn

Protein disulfide isomerase is the dominant acceptor for peptides translocated into the endoplasmic reticulum

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language of work or name

English

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publication date

20 October 2006

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published in

Cell

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volume

127

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issue

2

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page(s)

369-82

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cites work

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TAP-translocated peptides specifically bind proteins in the endoplasmic reticulum, including gp96, protein disulfide isomerase and calreticulin

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Protein disulfide isomerase: the multifunctional redox chaperone of the endoplasmic reticulum

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Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules

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Beta 2-microglobulin and calnexin can independently promote folding and disulfide bond formation in class I histocompatibility proteins

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Evidence for successive peptide binding and quality control stages during MHC class I assembly.

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The ER-luminal domain of the HCMV glycoprotein US6 inhibits peptide translocation by TAP

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Disulfide bond isomerization and the assembly of MHC class I-peptide complexes

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Optimization of the MHC class I peptide cargo is dependent on tapasin

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Peptide diffusion, protection, and degradation in nuclear and cytoplasmic compartments before antigen presentation by MHC class I.

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