Disruption of the association of 73 kDa heat shock cognate protein with transporters associated with antigen processing (TAP) decreases TAP-dependent translocation of antigenic peptides into the endoplasmic reticulum.

@article{Kamiguchi2008DisruptionOT,
  title={Disruption of the association of 73 kDa heat shock cognate protein with transporters associated with antigen processing (TAP) decreases TAP-dependent translocation of antigenic peptides into the endoplasmic reticulum.},
  author={Kenjiro Kamiguchi and Toshihiko Torigoe and Osamutaro Fujiwara and Shin Ohshima and Yoshihiko Hirohashi and Hiroeki Sahara and Itaru Hirai and Yutaka Kohgo and Noriyuki Sato},
  journal={Microbiology and immunology},
  year={2008},
  volume={52 2},
  pages={94-106}
}
Major histocompatibility complex class I-bound antigenic peptides generated in the cytosol are translocated into the ER by TAP. In the present study, the physical association of HSC73 with TAP in human lymphoblastoid T1 cells was demonstrated. The dissociation was induced in the presence of 10 mM ATP, indicating that the ADP-binding form of HSC73 might be associated with TAP. We found that HSC73-binding immunosuppressant, MeDSG disrupted the HSC73-TAP association, whereas it did not affect the… CONTINUE READING