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Pkd1 Inhibits Ampk2 Through Phosphorylation Of Serine 491 And Impairs Insulin Signaling In Skeletal Muscle Cells, Kimberly A. Coughlan, Rudy J. Valentine, Bella S. Sudit, Katherine Allen, Yossi Dagon, Barbara B. Kahn, Neil B. Ruderman, Asish K. Saha
Pkd1 Inhibits Ampk2 Through Phosphorylation Of Serine 491 And Impairs Insulin Signaling In Skeletal Muscle Cells, Kimberly A. Coughlan, Rudy J. Valentine, Bella S. Sudit, Katherine Allen, Yossi Dagon, Barbara B. Kahn, Neil B. Ruderman, Asish K. Saha
Rudy Valentine
Background: Diminished activity of the enzyme AMP-activated protein kinase (AMPK) is associated with impaired insulin signaling.
Results: Protein Kinase (PK)C/D1 activation inhibits AMPK2 via Ser491 phosphorylation; PKD1 inhibition prevents this in skeletal muscle cells.
Conclusion: PKD1 is a novel upstream AMPK-kinase that phosphorylates AMPK on Ser491 and regulates insulin signaling.
Significance: PKD1 inhibition may be a novel strategy for improving insulin sensitivity.