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Miyata, Y. and Yahara, I. (2002) The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity. Journal of Biological Chemistry, 267, 7042-7047.

has been cited by the following article:

• TITLE: Protein kinase CK2 in the ER stress response

  AUTHORS: Claudia Götz, Mathias Montenarh

  KEYWORDS: Protein Kinase CK2; ER Stress; Signalling

  JOURNAL NAME: Advances in Biological Chemistry, Vol.3 No.3A, June 21, 2013

  ABSTRACT: The endoplasmic reticulum is the central organelle within a eukaryotic cell where newly synthesized proteins are processed and properly folded. An excess of unfolded or mis-folded proteins induces ER stress signalling pathways. Usually this means a pro-survival strategy for the cell, whereas under extended stress conditions the ER stress signalling pathways have a pro-apoptotic function. CK2 plays a key role in the regulation of the pro-survival as well as the proapoptotic ER stress signalling by directly modulating the activities of members of the ER stress signalling pathways by phosphorylation, regulating the expression of the key factors of the signalling pathways or binding to regulator proteins. The present review will summarize the state of the art in this new emerging field.