The co-chaperone DNAJC12 binds to Hsc70 and is upregulated by endoplasmic reticulum stress

@article{Choi2013TheCD,
  title={The co-chaperone DNAJC12 binds to Hsc70 and is upregulated by endoplasmic reticulum stress},
  author={Jin Kyue Choi and Sonia Djebbar and Andr{\'e}a Fournier and Claude Labrie},
  journal={Cell Stress and Chaperones},
  year={2013},
  volume={19},
  pages={439-446}
}
Human DNAJC12 is a J domain-containing protein whose regulation, subcellular localization, and function are currently unknown. We show here that the abundance of DNAJC12 in human LNCaP prostate cancer cells is upregulated by the stress-inducing drug A23187 and by the stress-regulated transcription factor AIbZIP/CREB3L4. The DNAJC12 gene encodes two isoforms, only one of which (isoform a) is expressed in these cells. Immunofluorescence studies showed that a recombinant DNAJC12 protein is… CONTINUE READING

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