Protein kinase C delta specifically associates with phosphatidylinositol 3-kinase following cytokine stimulation

被引:82
作者
Ettinger, SL [1 ]
Lauener, RW [1 ]
Duronio, V [1 ]
机构
[1] UNIV BRITISH COLUMBIA,JACK BELL RES CTR,DEPT MED,VANCOUVER,BC V6H 3Z6,CANADA
关键词
D O I
10.1074/jbc.271.24.14514
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Phosphatidylinositol (PI) 3-kinase is activated as a result of cytokine-induced association of the enzyme with specific tyrosine phosphorylated proteins. PI 3-kinase lipid products, PI 3,4-P-2 and PI 3,4,5-P-3, have been shown, in vitro, to directly activate novel and atypical protein kinase C (PKC) isozymes. However, the mechanism by which PI 3-kinase may be involved in regulation of PKC isoforms in vivo is presently unknown. We investigated a possible relationship by looking for associations between these enzymes. We found that in a human erythroleukemia cell line, as well as in rabbit platelets, PI 3-kinase and PKC delta associate in a specific manner that is modulated by cell activation. Granulocyte-macrophage colony-stimulating factor treatment of cells caused increased association of PKC delta and PI S-kinase as did treatment of platelets with platelet-activating factor. Results using two PIS-kinase inhibitors, wortmannin and LY-294002, showed that the former inhibited this association, while the latter did not, suggesting that PI 3-kinase lipid products may not be a prerequisite for the PI 3-kinase/PKC delta association. Our results also suggest that tyrosine phosphorylation of PKC delta is not involved in its association with PI 3-kinase.
引用
收藏
页码:14514 / 14518
页数:5
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