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A correction to this article has been published: J. Cell Biol. 162 (2) 353
Published online 16 June 2003. doi:10.1083/jcb.200210169
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© The Rockefeller University Press, 0021-9525/2003/6/1093 $5.00
The Journal of Cell Biology, Volume 161, Number 6, 1093-1103

Article

Perilipin A is essential for the translocation of hormone-sensitive lipase during lipolytic activation



Carole Sztalryd1, Guoheng Xu1, Heidi Dorward1, John T. Tansey1, Juan A. Contreras2, Alan R. Kimmel1 and Constantine Londos1

1 Laboratory of Cellular and Developmental Biology, National Institute of Diabetes, Digestive, and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892
2 Department of Cell and Molecular Biology, Section for Molecular Signaling, Lund University, SE221 84 Lund, Sweden

Address correspondence to Dr. Constantine Londos, Laboratory of Cellular and Developmental Biology, National Institute of Diabetes, Digestive, and Kidney Diseases, National Institutes of Health, Bldg. 6, Rm. B1-32A, 9000 Rockville Pike, Bethesda, MD 20892-2715. Tel.: (301) 496-6991 Fax: (301) 496-5239. E-mail: DeanL{at}intra.niddk.nih.gov

Akey step in lipolytic activation of adipocytes is the translocation of hormone-sensitive lipase (HSL) from the cytosol to the surface of the lipid storage droplet. Adipocytes from perilipin-null animals have an elevated basal rate of lipolysis compared with adipocytes from wild-type mice, but fail to respond maximally to lipolytic stimuli. This defect is downstream of the ß-adrenergic receptor–adenylyl cyclase complex. Now, we show that HSL is basally associated with lipid droplet surfaces at a low level in perilipin nulls, but that stimulated translocation from the cytosol to lipid droplets is absent in adipocytes derived from embryonic fibroblasts of perilipin-null mice. We have also reconstructed the HSL translocation reaction in the nonadipocyte Chinese hamster ovary cell line by introduction of GFP-tagged HSL with and without perilipin A. On activation of protein kinase A, HSL-GFP translocates to lipid droplets only in cells that express fully phosphorylatable perilipin A, confirming that perilipin is required to elicit the HSL translocation reaction. Moreover, in Chinese hamster ovary cells that express both HSL and perilipin A, these two proteins cooperate to produce a more rapidly accelerated lipolysis than do cells that express either of these proteins alone, indicating that lipolysis is a concerted reaction mediated by both protein kinase A–phosphorylated HSL and perilipin A.

Key Words: lipolysis; adipocytes; ADRP/adipophilin; HSL; lipid storage droplets

C. Sztalryd and G. Xu contributed equally to this paper.

The online version of this article includes supplemental material.

* Abbreviations used in this paper: ADRP, adipose differentiation–related protein; HSL, hormone-sensitive lipase; IBMX, isobutylmethylxanthine; PIA, N6-phenylisopropyladenosine; PKA, cAMP-dependent protein kinase; TAG, triacylglycerols; wt, wild type.


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