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Phosphatidylinositol-4-Phosphate 5-Kinase Isoforms Exhibit Acyl Chain Selectivity For Both Substrate And Lipid Activator.

J Biol Chem.. 2012-10;  287(43):35953 - 35963
Yulia V. Shulga, Richard A. Anderson, Matthew K. Topham, and Richard M. Epand. Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario L8S 4K1, Canada.
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摘要

Phosphatidylinositol 4,5-bisphosphate is mostly produced in the cell by phosphatidylinositol-4-phosphate 5-kinases (PIP5K) and has a crucial role in numerous signaling events. Here we demonstrate that in vitro all three isoforms of PIP5K, α, β, and γ, discriminate among substrates with different acyl chains for both the substrates phosphatidylinositol 4-phosphate (PtdIns4P) and phosphatidylinositol (PtdIns) although to different extents, with isoform γ being the most selective. Fully saturated dipalmitoyl-PtdIns4P was a poor substrate for all three isoforms, but both the 1-stearoyl-2-arachidonoyl and the 1-stearoyl-2-oleoyl forms of PtdIns4P were good substrates. V(max) was greater for th... More

关键词

Lipids; Phosphatidic Acid; Phosphatidylinositol; Phosphatidylinositol Kinase; Phosphatidylinositol Signaling; Signal Transduction; Acyl Chain Specificity; Phosphatidic Acid