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New insights into PKC family affairs: three novel phosphorylation sites in PKCepsilon and at least one is regulated by PKCalpha.

Larsson, Christer LU (2008) In The Biochemical journal 411(2). p.15-16
Abstract
PKCepsilon (protein kinase Cepsilon) 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 PKCepsilon. All of them are specific for the epsilon isoform, evolutionarily conserved and tightly regulated. The phosphorylation of one site is critical for the binding of PKCepsilon to 14-3-3beta,... (More)
PKCepsilon (protein kinase Cepsilon) 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 PKCepsilon. All of them are specific for the epsilon isoform, evolutionarily conserved and tightly regulated. The phosphorylation of one site is critical for the binding of PKCepsilon to 14-3-3beta, suggesting it is of functional importance. The results provide important novel findings that uncover new aspects of PKCepsilon regulation and reveal new possibilities for detecting PKCepsilon activity in situ. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
The Biochemical journal
volume
411
issue
2
pages
15 - 16
publisher
Portland Press
external identifiers
  • pmid:18363550
  • scopus:42449156010
ISSN
1470-8728
DOI
10.1042/BJ20080373
language
English
LU publication?
yes
id
ce116bbe-1d0c-4b22-8f3a-5028f475aad8 (old id 1052185)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/18363550?dopt=Abstract
date added to LUP
2008-04-02 11:36:36
date last changed
2017-01-01 07:50:51
@article{ce116bbe-1d0c-4b22-8f3a-5028f475aad8,
  abstract     = {PKCepsilon (protein kinase Cepsilon) 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 PKCepsilon. All of them are specific for the epsilon isoform, evolutionarily conserved and tightly regulated. The phosphorylation of one site is critical for the binding of PKCepsilon to 14-3-3beta, suggesting it is of functional importance. The results provide important novel findings that uncover new aspects of PKCepsilon regulation and reveal new possibilities for detecting PKCepsilon activity in situ.},
  author       = {Larsson, Christer},
  issn         = {1470-8728},
  language     = {eng},
  number       = {2},
  pages        = {15--16},
  publisher    = {Portland Press},
  series       = {The Biochemical journal},
  title        = {New insights into PKC family affairs: three novel phosphorylation sites in PKCepsilon and at least one is regulated by PKCalpha.},
  url          = {http://dx.doi.org/10.1042/BJ20080373},
  volume       = {411},
  year         = {2008},
}