Article
PKD1 Inhibits AMPK2 through Phosphorylation of Serine 491 and Impairs Insulin Signaling in Skeletal Muscle Cells
Journal of Biological Chemistry
Document Type
Article
Disciplines
Publication Version
Published Version
Publication Date
3-11-2016
DOI
10.1074/jbc.M115.696849
Abstract
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.
Copyright Owner
The American Society for Biochemistry and Molecular Biology, Inc.
Copyright Date
2016
Language
en
File Format
application/pdf
Citation Information
Kimberly A. Coughlan, Rudy J. Valentine, Bella S. Sudit, Katherine Allen, et al.. "PKD1 Inhibits AMPK2 through Phosphorylation of Serine 491 and Impairs Insulin Signaling in Skeletal Muscle Cells" Journal of Biological Chemistry Vol. 291 Iss. 11 (2016) p. 5664 - 5675 Available at: http://works.bepress.com/rudy-valentine/6/
This article is published as Coughlan KA, Valentine RJ, Sudit BS, Allen K, Dagon Y, Kahn BB, Ruderman NB, Saha AK. PKD1 inhibits AMPKα2 through phosphorylation of Ser491 and impairs insulin signaling in skeletal muscle cells. Journal Biological Chemistry. 2016; 291(11):5664-75. DOI: 10.1074/jbc.M115.696849. Posted with permission.