Cell Stress and Chaperones

, Volume 19, Issue 3, pp 439–446 | Cite as

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

  • Jin Choi
  • Sonia Djebbar
  • Andréa Fournier
  • Claude Labrie
Short Communication


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 diffusely distributed in the cytoplasm. To identify substrates of DNAJC12, we used an immunoaffinity-mass spectrometry approach in cells that express epitope-tagged DNAJC12. The list of potential DNAJC12-binding proteins that were identified in this screen includes several nucleotide-binding proteins. The most frequently identified partner of DNAJC12 in unstressed cells was Hsc70, a cognate Hsp70 chaperone, whereas in stressed cells, the ER chaperone BiP was frequently associated with DNAJC12. Immunoprecipitation experiments confirmed that the endogenous DNAJC12 and Hsc70 proteins interact in LNCaP cells. These results clarify the role of DNAJC12 in the regulation of Hsp70 function.


DNAJC12 Hsc70 CREB3L4 Endoplasmic reticulum stress LNCaP 



This work was supported by an operating grant to C.L. from the Canadian Institutes of Health Research (MOP-77599). We thank C. Guillemette, N. Vallières, and L. Boudreau for the reagents and advice.


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Copyright information

© Cell Stress Society International 2013

Authors and Affiliations

  • Jin Choi
    • 1
  • Sonia Djebbar
    • 1
  • Andréa Fournier
    • 1
  • Claude Labrie
    • 1
  1. 1.Laval University and Centre Hospitalier Universitaire de Québec Research CenterQuébecCanada

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