✦ LIBER ✦

Association of phosphatidylinositol 3 kinase to protein kinase C ζ during interleukin-2 stimulation

✍ Scribed by Javier Gómez; Carlos Martínez-A; Alphonse García; Angelita Rebollo

Book ID: 102825304
Publisher: John Wiley and Sons
Year: 1996
Tongue: English
Weight: 757 KB
Volume: 26
Category: Article
ISSN: 0014-2980
DOI: 10.1002/eji.1830260818

No coin nor oath required. For personal study only.

✦ Synopsis

Interleukin-2 induces a serine-phosphorylated phosphatidylinositol 3 kinase activity in the mouse T cell line TSlaP. Moreover, protein kinase C (PKC) directly or indirectly associates with the phosphatidylinositol 3 kinase and the association appears to be necessary for the serine-phosphorylated phosphatidylinositol 3 kinase activity, since release of SPKC by competition of binding with peptides spanning the pllO sequence from amino acids 907 to 925 abolishes the serine-phosphorylated phosphatidylinositol3 kinase activity. This kinase activity is also blocked when CPKC expression is inhibited by antisense oligonucleotide. Inhibition of phosphatidylinositol 3 kinase activity by wortmannin does not abolish SPKC association.

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