AustralieFrV1, PubMed, Curation, bibRecord, 002691

A MARCH6 and IDOL E3 Ubiquitin Ligase Circuit Uncouples Cholesterol Synthesis from Lipoprotein Uptake in Hepatocytes.

Identifieur interne : 002691 ( PubMed/Curation ); précédent : 002690; suivant : 002692

A MARCH6 and IDOL E3 Ubiquitin Ligase Circuit Uncouples Cholesterol Synthesis from Lipoprotein Uptake in Hepatocytes.

Auteurs : Anke Loregger [Pays-Bas] ; Emma Claire Laura Cook [Pays-Bas] ; Jessica Kristin Nelson [Pays-Bas] ; Martina Moeton [Pays-Bas] ; Laura Jane Sharpe [Australie] ; Susanna Engberg [Suède] ; Madina Karimova [Suède] ; Gilles Lambert [France] ; Andrew John Brown [Australie] ; Noam Zelcer [Pays-Bas]

Source :

Molecular and cellular biology [ 1098-5549 ] ; 2015.

RBID : pubmed:26527619

Descripteurs français

English descriptors

KwdEn :
- Biosynthetic Pathways, Cell Line, Cholesterol (metabolism), Gene Silencing, Hep G2 Cells, Hepatocytes (metabolism), Humans, Lipoproteins (metabolism), Membrane Proteins (genetics), Membrane Proteins (metabolism), Receptors, LDL (metabolism), Ubiquitin-Protein Ligases (genetics), Ubiquitin-Protein Ligases (metabolism).
MESH :
- chemical , genetics : Membrane Proteins, Ubiquitin-Protein Ligases.
- chemical , metabolism : Cholesterol, Lipoproteins, Membrane Proteins, Receptors, LDL, Ubiquitin-Protein Ligases.
- metabolism : Hepatocytes.
- Biosynthetic Pathways, Cell Line, Gene Silencing, Hep G2 Cells, Humans.

Abstract

Cholesterol synthesis and lipoprotein uptake are tightly coordinated to ensure that the cellular level of cholesterol is adequately maintained. Hepatic dysregulation of these processes is associated with pathological conditions, most notably cardiovascular disease. Using a genetic approach, we have recently identified the E3 ubiquitin ligase MARCH6 as a regulator of cholesterol biosynthesis, owing to its ability to promote degradation of the rate-limiting enzymes 3-hydroxy-3-methyl-glutaryl coenzyme A reductase (HMGCR) and squalene epoxidase (SQLE). Here, we present evidence for MARCH6 playing a multifaceted role in the control of cholesterol homeostasis in hepatocytes. We identify MARCH6 as an endogenous inhibitor of the sterol regulatory element binding protein (SREBP) transcriptional program. Accordingly, loss of MARCH6 increases expression of SREBP-regulated genes involved in cholesterol biosynthesis and lipoprotein uptake. Unexpectedly, this is associated with a decrease in cellular lipoprotein uptake, induced by enhanced lysosomal degradation of the low-density lipoprotein receptor (LDLR). Finally, we provide evidence that induction of the E3 ubiquitin ligase IDOL represents the molecular mechanism underlying this MARCH6-induced phenotype. Our study thus highlights a MARCH6-dependent mechanism to direct cellular cholesterol accretion that relies on uncoupling of cholesterol synthesis from lipoprotein uptake.

DOI: 10.1128/MCB.00890-15
PubMed: 26527619

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<term>Hepatocytes (metabolism)</term>
<term>Humans</term>
<term>Lipoproteins (metabolism)</term>
<term>Membrane Proteins (genetics)</term>
<term>Membrane Proteins (metabolism)</term>
<term>Receptors, LDL (metabolism)</term>
<term>Ubiquitin-Protein Ligases (genetics)</term>
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<term>Protéines membranaires (métabolisme)</term>
<term>Récepteurs aux lipoprotéines LDL (métabolisme)</term>
<term>Ubiquitin-protein ligases (génétique)</term>
<term>Ubiquitin-protein ligases (métabolisme)</term>
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<term>Protéines membranaires</term>
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<term>Hep G2 Cells</term>
<term>Humans</term>
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<term>Extinction de l'expression des gènes</term>
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<front><div type="abstract" xml:lang="en">Cholesterol synthesis and lipoprotein uptake are tightly coordinated to ensure that the cellular level of cholesterol is adequately maintained. Hepatic dysregulation of these processes is associated with pathological conditions, most notably cardiovascular disease. Using a genetic approach, we have recently identified the E3 ubiquitin ligase MARCH6 as a regulator of cholesterol biosynthesis, owing to its ability to promote degradation of the rate-limiting enzymes 3-hydroxy-3-methyl-glutaryl coenzyme A reductase (HMGCR) and squalene epoxidase (SQLE). Here, we present evidence for MARCH6 playing a multifaceted role in the control of cholesterol homeostasis in hepatocytes. We identify MARCH6 as an endogenous inhibitor of the sterol regulatory element binding protein (SREBP) transcriptional program. Accordingly, loss of MARCH6 increases expression of SREBP-regulated genes involved in cholesterol biosynthesis and lipoprotein uptake. Unexpectedly, this is associated with a decrease in cellular lipoprotein uptake, induced by enhanced lysosomal degradation of the low-density lipoprotein receptor (LDLR). Finally, we provide evidence that induction of the E3 ubiquitin ligase IDOL represents the molecular mechanism underlying this MARCH6-induced phenotype. Our study thus highlights a MARCH6-dependent mechanism to direct cellular cholesterol accretion that relies on uncoupling of cholesterol synthesis from lipoprotein uptake.</div>
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<Abstract><AbstractText>Cholesterol synthesis and lipoprotein uptake are tightly coordinated to ensure that the cellular level of cholesterol is adequately maintained. Hepatic dysregulation of these processes is associated with pathological conditions, most notably cardiovascular disease. Using a genetic approach, we have recently identified the E3 ubiquitin ligase MARCH6 as a regulator of cholesterol biosynthesis, owing to its ability to promote degradation of the rate-limiting enzymes 3-hydroxy-3-methyl-glutaryl coenzyme A reductase (HMGCR) and squalene epoxidase (SQLE). Here, we present evidence for MARCH6 playing a multifaceted role in the control of cholesterol homeostasis in hepatocytes. We identify MARCH6 as an endogenous inhibitor of the sterol regulatory element binding protein (SREBP) transcriptional program. Accordingly, loss of MARCH6 increases expression of SREBP-regulated genes involved in cholesterol biosynthesis and lipoprotein uptake. Unexpectedly, this is associated with a decrease in cellular lipoprotein uptake, induced by enhanced lysosomal degradation of the low-density lipoprotein receptor (LDLR). Finally, we provide evidence that induction of the E3 ubiquitin ligase IDOL represents the molecular mechanism underlying this MARCH6-induced phenotype. Our study thus highlights a MARCH6-dependent mechanism to direct cellular cholesterol accretion that relies on uncoupling of cholesterol synthesis from lipoprotein uptake.</AbstractText>
<CopyrightInformation>Copyright © 2016, American Society for Microbiology. All Rights Reserved.</CopyrightInformation>
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<ForeName>Anke</ForeName>
<Initials>A</Initials>
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	Serveur d'exploration sur les relations entre la France et l'Australie
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A MARCH6 and IDOL E3 Ubiquitin Ligase Circuit Uncouples Cholesterol Synthesis from Lipoprotein Uptake in Hepatocytes.

A MARCH6 and IDOL E3 Ubiquitin Ligase Circuit Uncouples Cholesterol Synthesis from Lipoprotein Uptake in Hepatocytes.

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