Activation of PRK1 by Phosphatidylinositol 4,5-Bisphosphate and Phosphatidylinositol 3,4,5-Trisphosphate
Activation of PRK1 by Phosphatidylinositol 4,5-Bisphosphate and Phosphatidylinositol 3,4,5-Trisphosphate
复制标题
磷脂酰肌醇 4,5-二磷酸和磷脂酰肌醇 3,4,5-三磷酸激活 PRK1
DOI:
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复制
发表时间:
1995
影响因子:
4.8
通讯作者:
P. Parker
中科院分区:
文献类型:
--
作者:
R. Palmer;L. Dekker;R. Woscholski;J. Good;R. Gigg;P. Parker
As potential targets for polyphosphoinositides, activation of protein kinase C (PKC) isotypes (β1, ε, ζ, η) and a member of the PKC-related kinase (PRK) family, PRK1, has been compared in vitro. PRK1 is shown to be activated by both phosphatidylinositol 4,5-bisphosphate (PtdIns 4,5-P2) as well as phosphatidylinositol 3,4,5-trisphosphate (PtdIns-3,4,5-P3) either as pure sonicated lipids or in detergent mixed micelles. When presented as sonicated lipids, PtdIns-4,5-P2 and PtdIns-3,4,5-P3 were equipotent in activating PRK1, and, furthermore, sonicated phosphatidylinositol (PtdIns) and phosphatidylserine (PtdSer) were equally effective. In detergent mixed micelles, PtdIns-4,5-P2 and PtdIns-3,4,5-P3 also showed a similar potency, but PtdIns and PtdSer were 10-fold less effective in this assay. Similarly, PKC-β1, -ε, and -η were all activated by PtdIns-4,5-P2 and PtdIns-3,4,5-P3 in detergent mixed micelles. The activation constants for PtdIns-4,5-P2 and PtdIns-3,4,5-P3 were essentially the same for all the kinases tested, implying no specificity in this in vitro analysis. Consistent with this conclusion, the effects of PtdIns-4,5-P2 and PtdIns-3,4,5-P3 were found to be inhibited at 10 mM Mg2+ and mimicked by high concentrations of inositol hexaphosphate and inositol hexasulfate. The similar responses of these two classes of lipid-activated protein kinase to these phosphoinositides are discussed in light of their potential roles as second messengers.
DOI:
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发表时间:
1985
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Hannun,YA;Loomis,CR;Bell,RM
通讯作者:
Bell,RM
影响因子:
3.1
作者:
Singh,SS;Chauhan,A;Brockerhoff,H;Chauhan,VP
通讯作者:
Chauhan,VP