TRAP1 and the proteasome regulatory particle TBP7/Rpt3 interact in the endoplasmic reticulum and control cellular ubiquitination of specific mitochondrial proteins

@article{Amoroso2012TRAP1AT,
  title={TRAP1 and the proteasome regulatory particle TBP7/Rpt3 interact in the endoplasmic reticulum and control cellular ubiquitination of specific mitochondrial proteins},
  author={Maria Rosaria Amoroso and Danilo Swann Matassa and Gabriella Laudiero and Angelina V Egorova and Roman S. Polishchuk and Francesca Maddalena and Annamaria Piscazzi and Simona Paladino and Daniela Sarnataro and Corrado Garbi and Matteo Landriscina and Franca Esposito},
  journal={Cell Death and Differentiation},
  year={2012},
  volume={19},
  pages={592-604}
}
Tumor necrosis factor receptor-associated protein-1 (TRAP1) is a mitochondrial (MITO) antiapoptotic heat-shock protein. The information available on the TRAP1 pathway describes just a few well-characterized functions of this protein in mitochondria. However, our group's use of mass-spectrometric analysis identified TBP7, an AAA-ATPase of the 19S proteasomal subunit, as a putative TRAP1-interacting protein. Surprisingly, TRAP1 and TBP7 colocalize in the endoplasmic reticulum (ER), as… CONTINUE READING
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