Lehner P J, Surman M J, Cresswell P
Section of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06510, USA.
Immunity. 1998 Feb;8(2):221-31. doi: 10.1016/s1074-7613(00)80474-4.
Tapasin forms a bridge between TAP (transporters associated with antigen processing) and MHC class I molecules and plays a critical role in class I assembly. In its absence, TAP and class I do not associate, and class I cell surface expression is reduced. We now identify two independent functions for tapasin. Tapasin increases TAP levels and allows more peptide to be translocated to the endoplasmic reticulum. Furthermore, when expressed in the tapasin-negative .220 cell line, recombinant soluble tapasin retains its association with class I and restores class I cell surface expression and function, even though it no longer binds TAP or increases TAP levels. This finding suggests that the association of tapasin with class I is sufficient to facilitate loading and assembly of class I molecules.
塔帕辛(Tapasin)在抗原加工相关转运体(TAP)和MHC I类分子之间形成桥梁,在I类分子组装中起关键作用。缺乏塔帕辛时,TAP和I类分子不结合,I类分子在细胞表面的表达减少。我们现在确定了塔帕辛的两种独立功能。塔帕辛可提高TAP水平,并使更多肽转运至内质网。此外,当在缺乏塔帕辛的.220细胞系中表达时,重组可溶性塔帕辛仍与I类分子结合,并恢复I类分子在细胞表面的表达和功能,即便它不再结合TAP或提高TAP水平。这一发现表明,塔帕辛与I类分子的结合足以促进I类分子的装载和组装。