Multiple biological responses activated by nuclear protein kinase C

J Cell Biochem. 1999 Sep 15;74(4):499-521.


Protein kinase C is a family of serine-threonine kinases that are physiologically activated by a number of lipid cofactors and are important transducers in many agonist-induced signaling cascades. To date, 12 different isozymes of this kinase have been identified and are believed to play distinct regulatory roles. Protein kinase C was thought to reside in the cytosol in an inactive conformation and translocate to the plasma membrane upon cell activation by different stimuli. Nevertheless, a growing body of evidence has illustrated that this family of isozymes is capable of translocating to other cellular sites, including the nucleus. Moreover, it seems that some protein kinase C isoforms are resident within the nucleus. A wealth of data is being accumulated, demonstrating that nuclear protein kinase C isoforms are involved in the regulation of several critical biological functions such as cell proliferation and differentiation, neoplastic transformation, and apoptosis. In this review, we will discuss the most significant findings concerning nuclear protein kinase C which have been published during the past 5 years.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Apoptosis
  • Biological Transport, Active
  • Cell Differentiation
  • Cell Division
  • Cell Nucleus / enzymology*
  • Cell Transformation, Neoplastic
  • Humans
  • Isoenzymes / metabolism
  • Lipid Metabolism
  • Nuclear Proteins / metabolism
  • Protein Binding
  • Protein Kinase C / metabolism*
  • Second Messenger Systems
  • Signal Transduction
  • Subcellular Fractions / enzymology


  • Isoenzymes
  • Nuclear Proteins
  • Protein Kinase C