Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP (Q28287589)

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P J Lehner

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B Ortmann

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T Spies

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P Cresswell

Evidence that transporters associated with antigen processing translocate a major histocompatibility complex class I-binding peptide into the endoplasmic reticulum in an ATP-dependent manner

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language of work or name

English

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publication date

August 1996

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published in

Immunity

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volume

5

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issue

2

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page(s)

103-14

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cites work

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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)

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Immunodominant T cell epitope from signal sequence

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Transport and expression of class I MHC glycoproteins in an antigen-processing mutant cell line

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Efficient dissociation of the p88 chaperone from major histocompatibility complex class I molecules requires both beta 2-microglobulin and peptide

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Homozygous deletions that simultaneously eliminate expressions of class I and class II antigens of EBV-transformed B-lymphoblastoid cells. I. Reduced proliferative responses of autologous and allogeneic T cells to mutant cells that have decreased ex

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Glycosidase inhibitors: inhibitors of N‐linked oligosaccharide processing

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Proteolysis, proteasomes and antigen presentation

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Dependence of peptide binding by MHC class I molecules on their interaction with TAP.

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Quality control in the secretory pathway

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Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control

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An epitope common to HLA class I and class II antigens, Ig light chains, and beta 2-microglobulin

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Functional expression and purification of the ABC transporter complex associated with antigen processing (TAP) in insect cells

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Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase

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MHC class I/beta 2-microglobulin complexes associate with TAP transporters before peptide binding

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A point mutation in HLA-A*0201 results in failure to bind the TAP complex and to present virus-derived peptides to CTL.

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Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins

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An unstable beta 2-microglobulin: major histocompatibility complex class I heavy chain intermediate dissociates from calnexin and then is stabilized by binding peptide

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Interaction of MHC class I molecules with the transporter associated with antigen processing

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Calnexin Influences Folding of Human Class I Histocompatibility Proteins but Not Their Assembly with β2-Microglobulin

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Assembly of MHC class I molecules analyzed in vitro

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The transporters associated with antigen presentation

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Chaperone function of calreticulin when expressed in the endoplasmic reticulum as the membrane-anchored and soluble forms.

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The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins

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Molecular chaperones in antigen presentation

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Calnexin recognizes carbohydrate and protein determinants of class I major histocompatibility complex molecules

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