AMP-activated Protein Kinase Impairs Endothelial Actin Cytoskeleton Assembly by Phosphorylating Vasodilator-stimulated Phosphoprotein *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 282, Issue: 7, Page: 4601-4612
2007
- 84Citations
- 45Captures
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Metrics Details
- Citations84
- Citation Indexes84
- 84
- CrossRef79
- Captures45
- Readers45
- 45
Article Description
Vasodilator-stimulated phosphoprotein (VASP) is an actin regulatory protein that links signaling pathways to remodeling of the cytoskeleton. VASP functions are modulated by protein kinases, which phosphorylate the sites Ser-157, Ser-239, and Thr-278. The kinase responsible for Thr-278 phosphorylation, biological functions of the phosphorylation, and association with disease states have remained enigmatic. Using VASP phosphorylation status-specific antibodies, we identified AMP-activated protein kinase (AMPK), a serine-threonine kinase and fundamental sensor of energy homeostasis, in a screen for kinases that phosphorylate the Thr-278 site of VASP in endothelial cells. Pharmacological AMPK inhibitors and activators and AMPK mutants revealed that the kinase specifically targets residue Thr-278 but not Ser-157 or Ser-239. Quantitative fluorescence-activated cell sorter analysis and serum response factor transcriptional reporter assays, which quantify the cellular F-/G-actin equilibrium, indicated that AMPK-mediated VASP phosphorylation impaired actin stress fiber formation and altered cell morphology. In the Zucker Diabetic Fatty (ZDF) rat model for type II diabetes, AMPK activity and Thr-278 phosphorylation were substantially reduced in arterial vessel walls. These findings suggest that VASP is a new AMPK substrate, that VASP Thr-278 phosphorylation translates metabolic signals into actin cytoskeleton rearrangements, and that this signaling system becomes down-regulated in diabetic vessels.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925820650323; http://dx.doi.org/10.1074/jbc.m608866200; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=33947515200&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/17082196; https://linkinghub.elsevier.com/retrieve/pii/S0021925820650323; http://www.jbc.org/lookup/doi/10.1074/jbc.M608866200; https://syndication.highwire.org/content/doi/10.1074/jbc.M608866200; https://dx.doi.org/10.1074/jbc.m608866200
Elsevier BV
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