PKCϵ (protein kinase Cϵ) is a serine/threonine kinase, and a member of the PKC family of isoforms. The different PKC isoforms regulate many cellular processes of importance for disease. It is therefore desirable to obtain tools to specifically modulate the activity of the individual isoforms and to develop markers of PKC activity. The paper by Durgan et al. in this issue of the Biochemical Journal has taken us some steps further towards these goals. In the paper they identify three previously unknown phosphorylation sites in PKCϵ. All of them are specific for the ϵ isoform, evolutionarily conserved and tightly regulated. The phosphorylation of one site is critical for the binding of PKCϵ to 14-3-3β, suggesting it is of functional importance. The results provide important novel findings that uncover new aspects of PKCϵ regulation and reveal new possibilities for detecting PKCϵ activity in situ.
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April 2008
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March 27 2008
New insights into PKC family affairs: three novel phosphorylation sites in PKCϵ and at least one is regulated by PKCα
Christer Larsson
Christer Larsson
1
1Lund University, Center for Molecular Pathology, Entrance 78, 3rd floor, Malmö University Hospital, 205 02 Malmö, Sweden
1email Christer.Larsson@med.lu.se
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Publisher: Portland Press Ltd
Received:
February 15 2008
Accepted:
February 18 2008
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2008 Biochemical Society
2008
Biochem J (2008) 411 (2): e15–e16.
Article history
Received:
February 15 2008
Accepted:
February 18 2008
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Christer Larsson; New insights into PKC family affairs: three novel phosphorylation sites in PKCϵ and at least one is regulated by PKCα. Biochem J 15 April 2008; 411 (2): e15–e16. doi: https://doi.org/10.1042/BJ20080373
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