Molecules and Cells

Korean Society for Molecular and Cellular Biology (한국분자세포생물학회)
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Over-Expression of Phospholipase D Isozymes Down-Regulates Protein Kinase CKII Activity via Proteasome-Dependent CKIIβ Degradation in NIH3T3 Cells

  • Yoon, Soo-Hyun (Department of Biochemistry, College of Natural Sciences, Kyungpook National University) ;
  • Min, Do Sik (Department of Molecular Biology, College of Natural Sciences, Pusan National University) ;
  • Bae, Young-Seuk (Department of Biochemistry, College of Natural Sciences, Kyungpook National University)
  • Received : 2008.07.28
  • Accepted : 2008.12.22
  • Published : 2009.03.31
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Abstract

Over-expression of phospholipase D (PLD) 1 or PLD2 down-regulated CKII activity in NIH3T3 cells. The same results were found with catalytically inactive mutants of PLD isozymes, indicating that the catalytic activity of PLD is not required for PLD-mediated CKII inhibition. Consistent with this, 1-butanol did not alter CKII activity. The reduction in CKII activity in PLD-over-expressing NIH3T3 cells was due to reduced protein level, but not mRNA level, of the $CKII{\beta}$ subunit. This PLD-induced $CKII{\beta}$ degradation was mediated by ubiquitin-proteasome machinery, but MAP kinase and mTOR were not involved in $CKII{\beta}$ degradation. PLD isozymes interacted with the $CKII{\beta}$ subunit. Immunocytochemical staining revealed that PLD and $CKII{\beta}$ colocalize in the cytoplasm of NIH3T3 cells, especially in the perinuclear region. PLD binding to $CKII{\beta}$ inhibited $CKII{\beta}$ autophosphorylation, which is known to be important for $CKII{\beta}$ stability. In summary, the current data indicate that PLD isozymes can down-regulate CKII activity through the acceleration of $CKII{\beta}$ degradation by ubiquitin-proteasome machinery.

Keywords

Acknowledgement

Supported by : Korea Research Foundation, Korea Science and Engineering Foundation

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