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).
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December 2014
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Conference Article|
November 17 2014
The many hats of protein kinase Cδ: one enzyme with many functions
Nir Qvit;
Nir Qvit
*Department of Chemical and Systems Biology, Stanford University, School of Medicine, Stanford, CA 94305-5174, U.S.A.
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Daria Mochly-Rosen
Daria Mochly-Rosen
1
*Department of Chemical and Systems Biology, Stanford University, School of Medicine, Stanford, CA 94305-5174, U.S.A.
1To whom correspondence should be addressed (emailMochly@stanford.edu).
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Publisher: Portland Press Ltd
Received:
July 08 2014
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2014 Biochemical Society
2014
Biochem Soc Trans (2014) 42 (6): 1529–1533.
Article history
Received:
July 08 2014
Citation
Nir Qvit, Daria Mochly-Rosen; The many hats of protein kinase Cδ: one enzyme with many functions. Biochem Soc Trans 1 December 2014; 42 (6): 1529–1533. doi: https://doi.org/10.1042/BST20140189
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