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Papers In Press, published online ahead of print March 17, 2004
Dept. Physiology - 7756, Univ. Texas HSC San Antonio, UTHSCSA, San Antonio, TX 78229-3900
Corresponding Author: stockand{at}uthscsa.edu
The phospholipid PtdIns(4,5)P2 is accepted to be a direct modulator of ion channel activity. The products of PI3-K, PtdIns(3,4)P2 and PtdIns(3,4,5)P3, in contrast, are not. We report here activation of ENaC reconstituted in Chinese hamster ovary cells by PI3-K. Insulin like growth factor-I also activated reconstituted ENaC and increased Na+ reabsorption across renal A6 epithelial cell monolayers via PI3-K. Neither IGF-I nor PI3-K affected the levels of ENaC in the plasma membrane. The effects of PI3-K and IGF-I on ENaC activity paralleled changes in the plasma membrane levels of the PI3-K product phospholipids, PtdIns(3,4)P2/PtdIns(3,4,5)P3, as measured by evanescent field fluorescence microscopy. Both PtdIns(3,4)P2 and PtdIns(3,4,5)P
J. Biol. Chem, 10.1074/jbc.M401004200
Submitted on January 29, 2004
Revised on March 16, 2004
Accepted on March 16, 2004
Direct activation of the epithelial Na+ channel by phosphatidylinositol 3,4,5-trisphosphate and phosphatidylinositol 3,4-bisphosphate produced by phosphoinositide 3-OH kinase
3 activated ENaC in excised patches. Activation of ENaC by PI3-K and its phospholipid products corresponded to changes in channel open probability. We conclude that PI3-K directly modulates ENaC activity via PtdIns(3,4)P2 and PtdIns(3,4,5)P3. This represents a novel transduction pathway whereby growth factors, such as IGF-I, rapidly modulate target proteins independent of signaling elicited by kinases downstream of PI3-K.
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