Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.cellsig.2004.12.004
Title: Identification of an integral plasma membrane pool of protein kinase C in mammalian tissues and cells
Authors: Zhu, Y. 
Wee, G.L.
Bee, J.T.
Tian, S.T.
Duan, W. 
Keywords: Diacylglycerol
Integral membrane protein
Phorbol ester
PKC
Plasma membrane
Issue Date: 2005
Source: Zhu, Y., Wee, G.L., Bee, J.T., Tian, S.T., Duan, W. (2005). Identification of an integral plasma membrane pool of protein kinase C in mammalian tissues and cells. Cellular Signalling 17 (9) : 1125-1136. ScholarBank@NUS Repository. https://doi.org/10.1016/j.cellsig.2004.12.004
Abstract: Protein kinase C (PKC) is a family of serine/threonine protein kinases that are pivotal in cellular regulation. Since its discovery in 1977, PKCs have been known as cytosolic and peripheral membrane proteins. However, there are reports that PKC can insert into phospholipids vesicles in vitro. Given the intimate relationship between the plasma membrane and the activation of PKC, it is important to determine whether such "membrane-inserted" form of PKC exists in mammalian cells or tissues. Here, we report the identification of an integral plasma membrane pool for all the 10 PKC isozymes in vivo by their ability to partition into the detergent-rich phase in Triton X-114 phase partitioning, and by their resistance to extractions with 0.2 M sodium carbonate (pH 11.5), 2 M urea and 2 M sodium chloride. The endogenous integral membrane pool of PKC in mouse fibroblasts is found to be acutely regulated by phorbol ester or diacylglycerol, suggesting that this pool of PKC may participate in cellular processes known to be regulated by PKC. At least for PKCα, the C2-V3 region at the regulatory domain of the kinase is responsible for membrane integration. Further exploration of the function of this novel integral plasma membrane pool of PKC will not only shed new light on molecular mechanisms underlying its cellular functions but also provide new strategies for pharmaceutical modulation of this important group of kinases. © 2004 Elsevier Inc. All rights reserved.
Source Title: Cellular Signalling
URI: http://scholarbank.nus.edu.sg/handle/10635/28596
ISSN: 08986568
DOI: 10.1016/j.cellsig.2004.12.004
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

4
checked on Dec 6, 2017

WEB OF SCIENCETM
Citations

4
checked on Nov 17, 2017

Page view(s)

174
checked on Dec 10, 2017

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.