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Distinct roles for α-β hydrolase domain 5 (ABHD5/CGI-58) and adipose triglyceride lipase (ATGL/PNPLA2) in lipid metabolism and signaling

Catabolism of stored triacylglycerol (TAG) from cytoplasmic lipid droplets is critical for providing energy substrates, membrane building blocks and signaling lipids in most cells of the body. However, the lipolytic machinery dictating TAG hydrolysis varies greatly among different cell types. Within...

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Detalles Bibliográficos
Autores principales: Lord, Caleb C., Brown, J. Mark
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3492958/
https://www.ncbi.nlm.nih.gov/pubmed/23145367
http://dx.doi.org/10.4161/adip.20035
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author Lord, Caleb C.
Brown, J. Mark
author_facet Lord, Caleb C.
Brown, J. Mark
author_sort Lord, Caleb C.
collection PubMed
description Catabolism of stored triacylglycerol (TAG) from cytoplasmic lipid droplets is critical for providing energy substrates, membrane building blocks and signaling lipids in most cells of the body. However, the lipolytic machinery dictating TAG hydrolysis varies greatly among different cell types. Within the adipocyte, TAG hydrolysis is dynamically regulated by hormones to ensure appropriate metabolic adaptation to nutritional and physiologic cues. In other cell types such as hepatocytes, myocytes and macrophages, mobilization of stored TAG is regulated quite differently. Within the last decade, mutations in two key genes involved in TAG hydrolysis, α-β hydrolase domain 5 (ABHD5/CGI-58) and adipose triglyceride lipase (ATGL/PNPLA2), were found to cause two distinct neutral lipid storage diseases (NLSD) in humans. These genetic links, along with supporting evidence in mouse models, have prompted a number of studies surrounding the biochemical function(s) of these proteins. Although both CGI-58 and ATGL have been clearly implicated in TAG hydrolysis in multiple tissues and have even been shown to physically interact with each other, recent evidence suggests that they may also have distinct roles. The purpose of this review is to summarize the most recent insights into how CGI-58 and ATGL regulate lipid metabolism and signaling.
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spelling pubmed-34929582012-11-08 Distinct roles for α-β hydrolase domain 5 (ABHD5/CGI-58) and adipose triglyceride lipase (ATGL/PNPLA2) in lipid metabolism and signaling Lord, Caleb C. Brown, J. Mark Adipocyte Mini Review Catabolism of stored triacylglycerol (TAG) from cytoplasmic lipid droplets is critical for providing energy substrates, membrane building blocks and signaling lipids in most cells of the body. However, the lipolytic machinery dictating TAG hydrolysis varies greatly among different cell types. Within the adipocyte, TAG hydrolysis is dynamically regulated by hormones to ensure appropriate metabolic adaptation to nutritional and physiologic cues. In other cell types such as hepatocytes, myocytes and macrophages, mobilization of stored TAG is regulated quite differently. Within the last decade, mutations in two key genes involved in TAG hydrolysis, α-β hydrolase domain 5 (ABHD5/CGI-58) and adipose triglyceride lipase (ATGL/PNPLA2), were found to cause two distinct neutral lipid storage diseases (NLSD) in humans. These genetic links, along with supporting evidence in mouse models, have prompted a number of studies surrounding the biochemical function(s) of these proteins. Although both CGI-58 and ATGL have been clearly implicated in TAG hydrolysis in multiple tissues and have even been shown to physically interact with each other, recent evidence suggests that they may also have distinct roles. The purpose of this review is to summarize the most recent insights into how CGI-58 and ATGL regulate lipid metabolism and signaling. Landes Bioscience 2012-07-01 /pmc/articles/PMC3492958/ /pubmed/23145367 http://dx.doi.org/10.4161/adip.20035 Text en Copyright © 2012 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Mini Review
Lord, Caleb C.
Brown, J. Mark
Distinct roles for α-β hydrolase domain 5 (ABHD5/CGI-58) and adipose triglyceride lipase (ATGL/PNPLA2) in lipid metabolism and signaling
title Distinct roles for α-β hydrolase domain 5 (ABHD5/CGI-58) and adipose triglyceride lipase (ATGL/PNPLA2) in lipid metabolism and signaling
title_full Distinct roles for α-β hydrolase domain 5 (ABHD5/CGI-58) and adipose triglyceride lipase (ATGL/PNPLA2) in lipid metabolism and signaling
title_fullStr Distinct roles for α-β hydrolase domain 5 (ABHD5/CGI-58) and adipose triglyceride lipase (ATGL/PNPLA2) in lipid metabolism and signaling
title_full_unstemmed Distinct roles for α-β hydrolase domain 5 (ABHD5/CGI-58) and adipose triglyceride lipase (ATGL/PNPLA2) in lipid metabolism and signaling
title_short Distinct roles for α-β hydrolase domain 5 (ABHD5/CGI-58) and adipose triglyceride lipase (ATGL/PNPLA2) in lipid metabolism and signaling
title_sort distinct roles for α-β hydrolase domain 5 (abhd5/cgi-58) and adipose triglyceride lipase (atgl/pnpla2) in lipid metabolism and signaling
topic Mini Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3492958/
https://www.ncbi.nlm.nih.gov/pubmed/23145367
http://dx.doi.org/10.4161/adip.20035
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