Apoprotein B100, an inefficiently translocated secretory protein, is bound to the cytosolic chaperone, heat shock protein 70.

@article{Zhou1995ApoproteinBA,
  title={Apoprotein B100, an inefficiently translocated secretory protein, is bound to the cytosolic chaperone, heat shock protein 70.},
  author={Ming Zhou and Xiaosu Wu and Li Shin Huang and Henry N. Ginsberg},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 42},
  pages={25220-4}
}
Apoprotein B100 (apoB) is a secretory protein that appears to be constitutively translated but inefficiently translocated into the lumen of the endoplasmic reticulum. Using several experimental approaches, we found that apoB is bound to the cytosolic chaperone protein, heat shock protein 72/73 (commonly referred to as Hsp70). Similar to other chaperone-protein interactions, this binding was transient and ATP-sensitive. The binding of apoB to Hsp70 in HepG2 cells was decreased by treatment with… CONTINUE READING