Chemistry Faculty Scholarship
Document Type
Article
Publication Date
6-1-2003
Publication Title
The Journal of Cell Biology
Keywords
Lipolytic activation, Adipocytes
Abstract
A key 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 -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 A 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.
First Page
1093
Last Page
1103
Volume
161
Repository Citation
Tansey, John, "Perilipin A is essential for the translocation of hormone-sensitive lipase during lipolytic activation. J Cell Biol" (2003). Chemistry Faculty Scholarship. 16.
https://digitalcommons.otterbein.edu/chem_fac/16
DOI
10.1083/jcb.200210169
Version
Publisher's Version
Peer Reviewed
1
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.