Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP.

@article{Sadasivan1996RolesFC,
  title={Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP.},
  author={B. Sadasivan and P. Lehner and B. Ortmann and T. Spies and P. Cresswell},
  journal={Immunity},
  year={1996},
  volume={5 2},
  pages={
          103-14
        }
}
Assembly of MHC class I-beta 2 microglobulin (beta 2m) dimers in the endoplasmic reticulum involves two chaperones. Calnexin has previously been shown to interact with free class I heavy chains. Here, we show that the related chaperone, calreticulin, binds human class I-beta 2m dimers prior to peptide loading. Calreticulin remains associated with at least a subset of class I molecules when they, in turn, bind to TAP. Further evidence suggests that the interaction of class I-beta 2m dimers with… Expand
Calreticulin binds to the α1 domain of MHC class I independently of tapasin
Prior to binding to antigenic peptide, the major histoconipatibility complex (MHC) heavy chain associates with an assembly complex of proteins that includes calreticulin, tapasin, and the transporterExpand
A Role for Calnexin in the Assembly of the MHC Class I Loading Complex in the Endoplasmic Reticulum1
TLDR
This work has investigated the assembly of the loading complex and provided evidence that after TAP and tapasin associate with each other, the transmembrane chaperone calnexin and ERp57 bind to the TAP-tapasin complex to generate an intermediate. Expand
A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes.
TLDR
The molecular cloning of tapasin revealed it to be a transmembrane glycoprotein encoded by an MHC-linked gene, a member of the immunoglobulin superfamily with a probable cytoplasmic endoplasmic reticulum retention signal. Expand
Association of ERp57 with Mouse MHC Class I Molecules Is Tapasin Dependent and Mimics That of Calreticulin and not Calnexin1
  • Michael R. Harris, L. Lybarger, Yik Y. L. Yu, N. Myers, Ted H. Hansen
  • Biology, Medicine
  • The Journal of Immunology
  • 2001
TLDR
Combined data demonstrate that, during the assembly of the peptide-loading complex, the association of ERp57 with mouse class I is TPN dependent and parallels that of CRT and not calnexin. Expand
Calreticulin and calnexin interact with different protein and glycan determinants during the assembly of MHC class I.
TLDR
Evidence is presented that calreticulin clearly differs from calnexin in how it associates with class I and the structural basis of the association, the oligosaccharide moiety in the alpha1 domain and the amino acid residue at position 227 in thealpha3 domain were both found to be critical for the interaction of class I with cal reticulin. Expand
Mutant MHC class I molecules define interactions between components of the peptide-loading complex.
TLDR
A surprising observation was that all mutants lacking tapasin interaction retained normal association with CRT, which suggests that the organization of the ER peptide-loading complex can vary depending on the specific class I molecule examined. Expand
Calreticulin Promotes Folding of Functional Human Leukocyte Antigen Class I Molecules in Vitro*
TLDR
Calreticulin promotes the folding of HLA class I molecules to a state in which, at low temperature, they spontaneously acquire peptide binding capacity, but does not induce or maintain a peptide-receptive state of the class I-binding site, which is likely to be promoted by one or several other components of theclass I loading complexes. Expand
The Role of Calnexin and Calreticulin in MHC Class I Assembly
Assembly of Major Histocompatibility Complex (MHC) class I heavy chain (HC) with β2-microglobulin (β2m) and subsequent acquisition of optimal peptides is necessary for class 1 antigen presentation toExpand
The role of calnexin, calreticulin and heavy chain glycosylation in MHC class I assembly
 Class I heavy chain (HC) must assemble with β-microglobulin (β2m) and acquire optimal peptide in order to be presented to cytotoxic T cells (CTLs). Calnexin is involved in the initial folding ofExpand
Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin.
TLDR
MHC class I molecules expressed in a calreticulin-deficient cell line (K42) assembled with beta 2-microglobulin (beta2-m) normally, but their subsequent loading with optimal peptides was defective, resulting in impaired T cell recognition and reduced efficiency of peptide loading. Expand
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References

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TLDR
The results suggest that calnexin mediates class I/β2m dimerization, and subsequent binding of the dimers to TAP molecules facilitates their association with TAP-transported peptides. Expand
TAP associates with a unique class I conformation, whereas calnexin associates with multiple class I forms in mouse and man.
TLDR
Open forms of Ld are uniquely and specifically associated with TAP and that the conformational change in the class I H chain coincident with peptide binding induces TAP release, and a model for the sequential assembly of class I heterotrimers and their respective interactions with T AP and calnexin is proposed. Expand
Efficient dissociation of the p88 chaperone from major histocompatibility complex class I molecules requires both beta 2- microglobulin and peptide
TLDR
It is proposed that conformational changes in class I heavy chains induced by the binding of both beta 2m and peptide are required for efficient p88 dissociation and subsequent class I transport. Expand
Species-specific differences in chaperone interaction of human and mouse major histocompatibility complex class I molecules
Previous studies have shown that immature mouse class I molecules transiently associate with a resident endoplasmic reticulum protein of 88 kD that has been proposed to act as a chaperone for class IExpand
Calnexin Influences Folding of Human Class I Histocompatibility Proteins but Not Their Assembly with β2-Microglobulin (*)
TLDR
The data suggest that calnexin can promote disulfide bond formation in class I heavy chains but does not directly facilitate subsequent binding to β2m. Expand
An unstable beta 2-microglobulin: major histocompatibility complex class I heavy chain intermediate dissociates from calnexin and then is stabilized by binding peptide
TLDR
It is speculated that in the stepwise assembly of class I molecules, calnexin may mediate dimerization ofclass I HC with beta 2m, and that the unstablebeta 2m+:HC:pep- complexes, after dissociation from calnexIn, subsequently bind peptide to complete the assembly. Expand
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TLDR
The transporter associated with antigen processing (TAP) delivers cytosolic peptides into the endoplasmic reticulum (ER) where they bind to nascent class 1 histocompatibility molecules, and an association between the transporter and diverse class 1 products is revealed. Expand
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TLDR
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Characteristics of peptide and major histocompatibility complex class I/beta 2-microglobulin binding to the transporters associated with antigen processing (TAP1 and TAP2).
TLDR
TAP photolabeling analysis and photoaffinity labeling experiments suggest that efficient formation of the peptide-binding site occurs only when TAP1 and TAP2 are coexpressed, which correlates with the finding that peptide translocation via TAP occurs only in the presence of both TAP 1 and T AP2. Expand
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TLDR
Binding of peptides to two different pools of class I heterodimers may ensure efficient peptide association in an environment where peptides have a short life span. Expand
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