HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Hokkaido University Hospital >
Peer-reviewed Journal Articles, etc >

Functional interaction of hormone-sensitive lipase and perilipin in lipolysis

Files in This Item:
JLipidRes-2009-Shen-2306-13.pdf1.1 MBPDFView/Open
Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/67268

Title: Functional interaction of hormone-sensitive lipase and perilipin in lipolysis
Authors: Shen, Wen-Jun Browse this author
Patel, Shailja Browse this author
Miyoshi, Hideaki Browse this author →KAKEN DB
Greenberg, Andrew S. Browse this author
Kraemer, Fredric B. Browse this author
Keywords: translocation
lipid droplet
adipocyte
Issue Date: Nov-2009
Publisher: American Society for Biochemistry and Molecular Biology
Journal Title: Journal of lipid research
Volume: 50
Issue: 11
Start Page: 2306
End Page: 2313
Publisher DOI: 10.1194/jlr.M900176-JLR200
Abstract: Adipocyte lipolysis is controlled by complex interactions of lipases, cofactors, and structural proteins associated with lipid droplets. Perilipin (Plin) A is a major droplet-associated protein that functions as a scaffold, both suppressing basal and facilitating cAMP-dependent protein kinase (PKA)-stimulated lipolysis. Plin is required for the translocation of hormone-sensitive lipase (HSL) from the cytosol to lipid droplets upon stimulation. In these studies, we provide direct evidence for a physical interaction of HSL with Plin. By coexpressing HSL with truncation mutations of Plin, we demonstrate using coimmunoprecipitation that HSL can interact with an N-terminal region located between amino acids 141 and 200 of Plin A as well as with a C-terminal region located between amino acids 406 and 480. The N-terminal construct, Plin 1-200, which does not associate with lipid droplets but interacts with HSL, can function as a dominant negative for PKA-stimulated lipolysis. Using confocal microscopy of Plin truncations, we demonstrate that sequences between amino acids 463 and 517 may be important for or participate in lipid targeting. The results suggest the translocation of HSL to the lipid droplet occurs by virtue of Plin localization to the surface of lipid droplets and a physical interaction of HSL occurring with sequences within the N-terminal region of Plin.
Rights: This research was originally published in Journal of Lipid Research. Wen-Jun Shen, Shailja Patel, Hideaki Miyoshi, Andrew S. Greenberg, and Fredric B. Kraemer. Functional interaction of hormone-sensitive lipase and perilipin in lipolysis. J. Lipid Res. 2009; 50:(11) 2306-2313. © the American Society for Biochemistry and Molecular Biology.
Type: article
URI: http://hdl.handle.net/2115/67268
Appears in Collections:北海道大学病院 (Hokkaido University Hospital) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 三好 秀明

Export metadata:

OAI-PMH ( junii2 , jpcoar_1.0 )

MathJax is now OFF:


 

 - Hokkaido University