Journal article

Perilipin 5 S155 phosphorylation by PKA is required for the control of hepatic lipid metabolism and glycemic control

Stacey N Keenan, William De Nardo, Jieqiong Lou, Ralf B Schittenhelm, Magdalene K Montgomery, James G Granneman, Elizabeth Hinde, Matthew J Watt



Perilipin 5 (PLIN5) is a lipid-droplet-associated protein that coordinates intracellular lipolysis in highly oxidative tissues and is thought to regulate lipid metabolism in response to phosphorylation by protein kinase A (PKA). We sought to identify PKA phosphorylation sites in PLIN5 and assess their functional relevance in cultured cells and the livers of mice. We detected phosphorylation on S155 and identified S155 as a functionally important site for lipid metabolism. Expression of phosphorylation-defective PLIN5 S155A in Plin5 null cells resulted in decreased rates of lipolysis and triglyceride-derived fatty acid oxidation. FLIM-FRET analysis of protein-protein interactions showed that ..

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Awarded by National Health and Medical Research Council of Australia (NHMRC)

Awarded by NHMRC

Awarded by Australian NHMRC Career Development Fellowship

Funding Acknowledgements

This work was funded by the National Health and Medical Research Council of Australia (NHMRC, ID: 1047138). M. J. W. (APP1077703) and M. K. M. (APP1143224) were supported by a research fellowship from the NHMRC. E. H. was supported by an Australian NHMRC Career Development Fellowship (APP1124762) and the Jacob Haimson Beverly Mecklenburg Lectureship. W. D. is supported by a Melbourne Research Scholarship (University of Melbourne).