2000
DOI: 10.4049/jimmunol.164.1.292
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Distinct Functions of Tapasin Revealed by Polymorphism in MHC Class I Peptide Loading

Abstract: Peptide assembly with class I molecules is orchestrated by multiple chaperones including tapasin, which bridges class I molecules with the TAP and is critical for efficient Ag presentation. In this paper, we show that, although constitutive levels of endogenous murine tapasin apparently are sufficient to form stable and long-lived complexes between the human HLA-B*4402 (B*4402) and mouse TAP proteins, this does not result in normal peptide loading and surface expression of B*4402 molecules on mouse APC. Howeve… Show more

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Cited by 51 publications
(60 citation statements)
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“…TAP interaction is mediated through the C terminus of tapasin (9) and has recently been shown to enhance peptide binding to the cytosolic aspect of TAP molecules (8). This implies that tapasin may enhance TAPmediated translocation of antigenic oligopeptides; however, bridging of class I molecules to the TAP does not necessarily lead to enhanced peptide loading (42,53). Therefore, it has been postulated that the class I-tapasin interaction is more critical for class I assembly than is the tapasin-mediated bridging to the TAP (9).…”
Section: Discussionmentioning
confidence: 99%
“…TAP interaction is mediated through the C terminus of tapasin (9) and has recently been shown to enhance peptide binding to the cytosolic aspect of TAP molecules (8). This implies that tapasin may enhance TAPmediated translocation of antigenic oligopeptides; however, bridging of class I molecules to the TAP does not necessarily lead to enhanced peptide loading (42,53). Therefore, it has been postulated that the class I-tapasin interaction is more critical for class I assembly than is the tapasin-mediated bridging to the TAP (9).…”
Section: Discussionmentioning
confidence: 99%
“…Much of the work examining tapasin function has understandably been performed using either tapasin-deficient cells (6,8,(40)(41)(42)(43)(44)(45) or mutant MHC class I molecules that no longer associate with tapasin (13,14,16,23,25). However, in tapasin-deficient cells, it is now apparent that TAPBPR is present and still capable of binding to MHC class I.…”
Section: Discussionmentioning
confidence: 99%
“…HLA class I alleles differ in their requirements for antigen processing components; for example, tumors frequently exhibit alterations in the levels of TAP1-2, LMP2, LMP7, or tapasin expression [22][23][24]. Some alleles, such as HLA-A2, maintain their expression despite low levels of TAP1-2 or tapasin [25,26], whereas others, such as HLA-B44, have strict requirements for certain antigen processing components [27][28][29]. These variations may explain the marked differences between HLA-A2 and HLA-B44 in the frequency of selective loss of expression in human tumors.…”
Section: Discussionmentioning
confidence: 99%