The G0/G1 Switch Gene 2 Regulates Adipose Lipolysis through Association with Adipose Triglyceride Lipase

Xingyuan Yang, Xin Lu, Marc Lombès, Geun Bae Rha, Young In Chi, Theresa M. Guerin, Eric J. Smart, Jun D Liu

Research output: Contribution to journalArticle

262 Citations (Scopus)

Abstract

Adipose triglyceride lipase (ATGL) is the rate-limiting enzyme for triacylglycerol (TAG) hydrolysis in adipocytes. The precise mechanisms whereby ATGL is regulated remain uncertain. Here, we demonstrate that a protein encoded by G0/G1 switch gene 2 (G0S2) is a selective regulator of ATGL. G0S2 is highly expressed in adipose tissue and differentiated adipocytes. When overexpressed in HeLa cells, G0S2 localizes to lipid droplets and prevents their degradation mediated by ATGL. Moreover, G0S2 specifically interacts with ATGL through the hydrophobic domain of G0S2 and the patatin-like domain of ATGL. More importantly, interaction with G0S2 inhibits ATGL TAG hydrolase activity. Knockdown of endogenous G0S2 accelerates basal and stimulated lipolysis in adipocytes, whereas overexpression of G0S2 diminishes the rate of lipolysis in both adipocytes and adipose tissue explants. Thus, G0S2 functions to attenuate ATGL action both in vitro and in vivo and by this mechanism regulates TAG hydrolysis.

Original languageEnglish (US)
Pages (from-to)194-205
Number of pages12
JournalCell Metabolism
Volume11
Issue number3
DOIs
StatePublished - Mar 3 2010
Externally publishedYes

Fingerprint

Switch Genes
Lipolysis
Lipase
Adipocytes
Adipose Tissue
Triglycerides
Hydrolysis
HeLa Cells

Keywords

  • HUMDISEASE

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology
  • Physiology

Cite this

The G0/G1 Switch Gene 2 Regulates Adipose Lipolysis through Association with Adipose Triglyceride Lipase. / Yang, Xingyuan; Lu, Xin; Lombès, Marc; Rha, Geun Bae; Chi, Young In; Guerin, Theresa M.; Smart, Eric J.; Liu, Jun D.

In: Cell Metabolism, Vol. 11, No. 3, 03.03.2010, p. 194-205.

Research output: Contribution to journalArticle

Yang, Xingyuan ; Lu, Xin ; Lombès, Marc ; Rha, Geun Bae ; Chi, Young In ; Guerin, Theresa M. ; Smart, Eric J. ; Liu, Jun D. / The G0/G1 Switch Gene 2 Regulates Adipose Lipolysis through Association with Adipose Triglyceride Lipase. In: Cell Metabolism. 2010 ; Vol. 11, No. 3. pp. 194-205.
@article{d222a4453d1a4da28cb99a5d2329a4f5,
title = "The G0/G1 Switch Gene 2 Regulates Adipose Lipolysis through Association with Adipose Triglyceride Lipase",
abstract = "Adipose triglyceride lipase (ATGL) is the rate-limiting enzyme for triacylglycerol (TAG) hydrolysis in adipocytes. The precise mechanisms whereby ATGL is regulated remain uncertain. Here, we demonstrate that a protein encoded by G0/G1 switch gene 2 (G0S2) is a selective regulator of ATGL. G0S2 is highly expressed in adipose tissue and differentiated adipocytes. When overexpressed in HeLa cells, G0S2 localizes to lipid droplets and prevents their degradation mediated by ATGL. Moreover, G0S2 specifically interacts with ATGL through the hydrophobic domain of G0S2 and the patatin-like domain of ATGL. More importantly, interaction with G0S2 inhibits ATGL TAG hydrolase activity. Knockdown of endogenous G0S2 accelerates basal and stimulated lipolysis in adipocytes, whereas overexpression of G0S2 diminishes the rate of lipolysis in both adipocytes and adipose tissue explants. Thus, G0S2 functions to attenuate ATGL action both in vitro and in vivo and by this mechanism regulates TAG hydrolysis.",
keywords = "HUMDISEASE",
author = "Xingyuan Yang and Xin Lu and Marc Lomb{\`e}s and Rha, {Geun Bae} and Chi, {Young In} and Guerin, {Theresa M.} and Smart, {Eric J.} and Liu, {Jun D}",
year = "2010",
month = "3",
day = "3",
doi = "10.1016/j.cmet.2010.02.003",
language = "English (US)",
volume = "11",
pages = "194--205",
journal = "Cell Metabolism",
issn = "1550-4131",
publisher = "Cell Press",
number = "3",

}

TY - JOUR

T1 - The G0/G1 Switch Gene 2 Regulates Adipose Lipolysis through Association with Adipose Triglyceride Lipase

AU - Yang, Xingyuan

AU - Lu, Xin

AU - Lombès, Marc

AU - Rha, Geun Bae

AU - Chi, Young In

AU - Guerin, Theresa M.

AU - Smart, Eric J.

AU - Liu, Jun D

PY - 2010/3/3

Y1 - 2010/3/3

N2 - Adipose triglyceride lipase (ATGL) is the rate-limiting enzyme for triacylglycerol (TAG) hydrolysis in adipocytes. The precise mechanisms whereby ATGL is regulated remain uncertain. Here, we demonstrate that a protein encoded by G0/G1 switch gene 2 (G0S2) is a selective regulator of ATGL. G0S2 is highly expressed in adipose tissue and differentiated adipocytes. When overexpressed in HeLa cells, G0S2 localizes to lipid droplets and prevents their degradation mediated by ATGL. Moreover, G0S2 specifically interacts with ATGL through the hydrophobic domain of G0S2 and the patatin-like domain of ATGL. More importantly, interaction with G0S2 inhibits ATGL TAG hydrolase activity. Knockdown of endogenous G0S2 accelerates basal and stimulated lipolysis in adipocytes, whereas overexpression of G0S2 diminishes the rate of lipolysis in both adipocytes and adipose tissue explants. Thus, G0S2 functions to attenuate ATGL action both in vitro and in vivo and by this mechanism regulates TAG hydrolysis.

AB - Adipose triglyceride lipase (ATGL) is the rate-limiting enzyme for triacylglycerol (TAG) hydrolysis in adipocytes. The precise mechanisms whereby ATGL is regulated remain uncertain. Here, we demonstrate that a protein encoded by G0/G1 switch gene 2 (G0S2) is a selective regulator of ATGL. G0S2 is highly expressed in adipose tissue and differentiated adipocytes. When overexpressed in HeLa cells, G0S2 localizes to lipid droplets and prevents their degradation mediated by ATGL. Moreover, G0S2 specifically interacts with ATGL through the hydrophobic domain of G0S2 and the patatin-like domain of ATGL. More importantly, interaction with G0S2 inhibits ATGL TAG hydrolase activity. Knockdown of endogenous G0S2 accelerates basal and stimulated lipolysis in adipocytes, whereas overexpression of G0S2 diminishes the rate of lipolysis in both adipocytes and adipose tissue explants. Thus, G0S2 functions to attenuate ATGL action both in vitro and in vivo and by this mechanism regulates TAG hydrolysis.

KW - HUMDISEASE

UR - http://www.scopus.com/inward/record.url?scp=77249118270&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77249118270&partnerID=8YFLogxK

U2 - 10.1016/j.cmet.2010.02.003

DO - 10.1016/j.cmet.2010.02.003

M3 - Article

C2 - 20197052

AN - SCOPUS:77249118270

VL - 11

SP - 194

EP - 205

JO - Cell Metabolism

JF - Cell Metabolism

SN - 1550-4131

IS - 3

ER -