The many hats of protein kinase Cδ: one enzyme with many functions. (17th November 2014)

• Record Type: Journal Article
• Authors: Qvit, Nir; Mochly-Rosen, Daria
• Is Part Of: Biochemical Society transactions. Volume 42:Number 6(2014)
• Page Start: 1529
• Page End: 1533
• Publication Date: 2014-11-17
• Subjects: cardiac ischaemia -- drug development -- peptide regulators -- substrate specificity; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST20140189
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : A large number of protein substrates are phosphorylated by each protein kinase under physiological and pathological conditions. However, it remains a challenge to determine which of these phosphorylated substrates of a given kinase is critical for each cellular response. Genetics enabled the generation of separation-of-function mutations that selectively cause a loss of one molecular event without affecting others, thus providing some tools to assess the importance of that one event for the measured physiological response. However, the genetic approach is laborious and not adaptable to all systems. Furthermore, pharmacological tools of the catalytic site are not optimal due to their non-selective nature. In the present brief review, we discuss some of the challenges in drug development that will regulate the multifunctional protein kinase Cδ (PKCδ).