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The Lipolysome—A Highly Complex and Dynamic Protein Network Orchestrating Cytoplasmic Triacylglycerol Degradation

The catabolism of intracellular triacylglycerols (TAGs) involves the activity of cytoplasmic and lysosomal enzymes. Cytoplasmic TAG hydrolysis, commonly termed lipolysis, is catalyzed by the sequential action of three major hydrolases, namely adipose triglyceride lipase, hormone-sensitive lipase, an...

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Autores principales: Hofer, Peter, Taschler, Ulrike, Schreiber, Renate, Kotzbeck, Petra, Schoiswohl, Gabriele
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7240967/
https://www.ncbi.nlm.nih.gov/pubmed/32290093
http://dx.doi.org/10.3390/metabo10040147
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author Hofer, Peter
Taschler, Ulrike
Schreiber, Renate
Kotzbeck, Petra
Schoiswohl, Gabriele
author_facet Hofer, Peter
Taschler, Ulrike
Schreiber, Renate
Kotzbeck, Petra
Schoiswohl, Gabriele
author_sort Hofer, Peter
collection PubMed
description The catabolism of intracellular triacylglycerols (TAGs) involves the activity of cytoplasmic and lysosomal enzymes. Cytoplasmic TAG hydrolysis, commonly termed lipolysis, is catalyzed by the sequential action of three major hydrolases, namely adipose triglyceride lipase, hormone-sensitive lipase, and monoacylglycerol lipase. All three enzymes interact with numerous protein binding partners that modulate their activity, cellular localization, or stability. Deficiencies of these auxiliary proteins can lead to derangements in neutral lipid metabolism and energy homeostasis. In this review, we summarize the composition and the dynamics of the complex lipolytic machinery we like to call “lipolysome”.
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spelling pubmed-72409672020-06-11 The Lipolysome—A Highly Complex and Dynamic Protein Network Orchestrating Cytoplasmic Triacylglycerol Degradation Hofer, Peter Taschler, Ulrike Schreiber, Renate Kotzbeck, Petra Schoiswohl, Gabriele Metabolites Review The catabolism of intracellular triacylglycerols (TAGs) involves the activity of cytoplasmic and lysosomal enzymes. Cytoplasmic TAG hydrolysis, commonly termed lipolysis, is catalyzed by the sequential action of three major hydrolases, namely adipose triglyceride lipase, hormone-sensitive lipase, and monoacylglycerol lipase. All three enzymes interact with numerous protein binding partners that modulate their activity, cellular localization, or stability. Deficiencies of these auxiliary proteins can lead to derangements in neutral lipid metabolism and energy homeostasis. In this review, we summarize the composition and the dynamics of the complex lipolytic machinery we like to call “lipolysome”. MDPI 2020-04-10 /pmc/articles/PMC7240967/ /pubmed/32290093 http://dx.doi.org/10.3390/metabo10040147 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Hofer, Peter
Taschler, Ulrike
Schreiber, Renate
Kotzbeck, Petra
Schoiswohl, Gabriele
The Lipolysome—A Highly Complex and Dynamic Protein Network Orchestrating Cytoplasmic Triacylglycerol Degradation
title The Lipolysome—A Highly Complex and Dynamic Protein Network Orchestrating Cytoplasmic Triacylglycerol Degradation
title_full The Lipolysome—A Highly Complex and Dynamic Protein Network Orchestrating Cytoplasmic Triacylglycerol Degradation
title_fullStr The Lipolysome—A Highly Complex and Dynamic Protein Network Orchestrating Cytoplasmic Triacylglycerol Degradation
title_full_unstemmed The Lipolysome—A Highly Complex and Dynamic Protein Network Orchestrating Cytoplasmic Triacylglycerol Degradation
title_short The Lipolysome—A Highly Complex and Dynamic Protein Network Orchestrating Cytoplasmic Triacylglycerol Degradation
title_sort lipolysome—a highly complex and dynamic protein network orchestrating cytoplasmic triacylglycerol degradation
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7240967/
https://www.ncbi.nlm.nih.gov/pubmed/32290093
http://dx.doi.org/10.3390/metabo10040147
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