New insights into PKC family affairs: three novel phosphorylation sites in PKCepsilon and at least one is regulated by PKCalpha.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1052185
- author
- Larsson, Christer LU
- organization
- publishing date
- 2008
- 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
- pmid:18363550
- ISSN
- 1470-8728
- DOI
- 10.1042/BJ20080373
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Tumour Cell Biology (013017530)
- 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
- 2016-04-04 09:32:46
- date last changed
- 2022-01-29 18:21:47
@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}}, doi = {{10.1042/BJ20080373}}, volume = {{411}}, year = {{2008}}, }