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1 Department of Biology, Indiana University-Purdue University at Indianapolis, Indianapolis 46202; and 2 Therapeutic Area Discovery Research and Chemistry Information Technology and 3 Cardiovascular Research, Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, Indiana 46285
ENaC-EGFP (enhanced green fluorescent
protein-tagged -subunit of the epithelial Na+ channel)
stably transfected clonal lines derived from the A6 parental cell line
were used to study the physical mechanisms of insulin-stimulated
Na+ transport. Within 1 min of insulin stimulation, ENaC
migrates from a diffuse cytoplasmic localization to the apical and
lateral membranes. Concurrently, after insulin stimulation,
phosphatidylinositol 3-kinase (PI 3-kinase) is colocalized with ENaC on
the lateral but not apical membrane. An inhibitor of PI 3-kinase,
LY-294002, does not inhibit ENaC/PI 3-kinase colocalization but does
alter the intracellular site of the colocalization, preventing the
translocation of ENaC to the lateral and apical membranes. These data
show that insulin stimulation causes the migration of ENaC to the
lateral and apical cell membranes and that this trafficking is
dependent on PI 3-kinase activity.
epithelial sodium channels; phosphatidylinositol 3,4,5-bisphosphate; phosphatidylinositol 3-kinase; phosphoinositide pathway; transepithelial signal transduction; sodium transport
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