Mechanisms targeting apolipoprotein B100 to proteasomal degradation: evidence that degradation is initiated by BiP binding at the N terminus and the formation of a p97 complex at the C terminus.

@article{Rutledge2009MechanismsTA,
  title={Mechanisms targeting apolipoprotein B100 to proteasomal degradation: evidence that degradation is initiated by BiP binding at the N terminus and the formation of a p97 complex at the C terminus.},
  author={Angela C Rutledge and Wei Qiu and Rianna Zhang and Rita Kohen-Avramoglu and Nina Nemat-Gorgani and Khosrow Adeli},
  journal={Arteriosclerosis, thrombosis, and vascular biology},
  year={2009},
  volume={29 4},
  pages={579-85}
}
OBJECTIVE In lipid-poor states, the ubiquitin-proteasomal pathway rapidly degrades misfolded apolipoprotein B100 (apoB) cotranslationally, although the mechanism of delivery from the ER to cytosolic proteasomes is poorly understood. Here we demonstrate key roles of BiP, an ER luminal chaperone, and p97, a cytosolic ATPase anchored to the ER membrane, in the targeting of apoB for proteasomal degradation. METHODS AND RESULTS Using coimmunoprecipitations, we observed associations of apoB with… CONTINUE READING

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