The many hats of protein kinase Cδ: One enzyme with many functions

Nir Qvit, Daria Mochly-Rosen

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

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).

Original languageEnglish
Pages (from-to)1529-1533
Number of pages5
JournalBiochemical Society Transactions
Volume42
Issue number6
DOIs
StatePublished - 1 Dec 2014
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 2014 Biochemical Society.

Keywords

  • Cardiac ischaemia
  • Drug development
  • Peptide regulators
  • Substrate specificity

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