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Article ; Online: The Role of Cullin-RING Ligases in Striated Muscle Development, Function, and Disease.

Blondelle, Jordan / Biju, Andrea / Lange, Stephan

International journal of molecular sciences

2020 Volume 21, Issue 21

Abstract: The well-orchestrated turnover of proteins in cross-striated muscles is one of the fundamental processes required for muscle cell function and survival. Dysfunction of the intricate protein degradation machinery is often associated with development of ... ...

Abstract	The well-orchestrated turnover of proteins in cross-striated muscles is one of the fundamental processes required for muscle cell function and survival. Dysfunction of the intricate protein degradation machinery is often associated with development of cardiac and skeletal muscle myopathies. Most muscle proteins are degraded by the ubiquitin-proteasome system (UPS). The UPS involves a number of enzymes, including E3-ligases, which tightly control which protein substrates are marked for degradation by the proteasome. Recent data reveal that E3-ligases of the cullin family play more diverse and crucial roles in cross striated muscles than previously anticipated. This review highlights some of the findings on the multifaceted functions of cullin-RING E3-ligases, their substrate adapters, muscle protein substrates, and regulatory proteins, such as the Cop9 signalosome, for the development of cross striated muscles, and their roles in the etiology of myopathies.
MeSH term(s)	COP9 Signalosome Complex/metabolism ; Cullin Proteins/metabolism ; Gene Expression Regulation, Developmental ; Humans ; Muscle Proteins/metabolism ; Muscle, Striated/growth & development ; Muscle, Striated/physiology ; Muscular Diseases/metabolism ; Proteolysis
Chemical Substances	Cullin Proteins ; Muscle Proteins ; COP9 Signalosome Complex (EC 3.4.19.12)
Language	English
Publishing date	2020-10-26
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms21217936
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Article ; Online: The Role of Cullin-RING Ligases in Striated Muscle Development, Function, and Disease

Jordan Blondelle / Andrea Biju / Stephan Lange

International Journal of Molecular Sciences, Vol 21, Iss 7936, p

2020 Volume 7936

Abstract	The well-orchestrated turnover of proteins in cross-striated muscles is one of the fundamental processes required for muscle cell function and survival. Dysfunction of the intricate protein degradation machinery is often associated with development of cardiac and skeletal muscle myopathies. Most muscle proteins are degraded by the ubiquitin–proteasome system (UPS). The UPS involves a number of enzymes, including E3-ligases, which tightly control which protein substrates are marked for degradation by the proteasome. Recent data reveal that E3-ligases of the cullin family play more diverse and crucial roles in cross striated muscles than previously anticipated. This review highlights some of the findings on the multifaceted functions of cullin-RING E3-ligases, their substrate adapters, muscle protein substrates, and regulatory proteins, such as the Cop9 signalosome, for the development of cross striated muscles, and their roles in the etiology of myopathies.
Keywords	cullin-RING ligase (CRL) ; Nedd8 ; protein degradation ; ubiquitin-proteasome system (UPS) ; autophagy-lysosome system ; striated muscle development ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
Subject code	570
Language	English
Publishing date	2020-10-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
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Article ; Online: Hacd2 deficiency in mice leads to an early and lethal mitochondrial disease.

Khadhraoui, Nahed / Prola, Alexandre / Vandestienne, Aymeline / Blondelle, Jordan / Guillaud, Laurent / Courtin, Guillaume / Bodak, Maxime / Prost, Bastien / Huet, Hélène / Wintrebert, Mélody / Péchoux, Christine / Solgadi, Audrey / Relaix, Frédéric / Tiret, Laurent / Pilot-Storck, Fanny

Molecular metabolism

2023 Volume 69, Page(s) 101677

Abstract: Objective: Mitochondria fuel most animal cells with ATP, ensuring proper energetic metabolism of organs. Early and extensive mitochondrial dysfunction often leads to severe disorders through multiorgan failure. Hacd2 gene encodes an enzyme involved in ... ...

Abstract	Objective: Mitochondria fuel most animal cells with ATP, ensuring proper energetic metabolism of organs. Early and extensive mitochondrial dysfunction often leads to severe disorders through multiorgan failure. Hacd2 gene encodes an enzyme involved in very long chain fatty acid (C ≥ 18) synthesis, yet its roles in vivo remain poorly understood. Since mitochondria function relies on specific properties of their membranes conferred by a particular phospholipid composition, we investigated if Hacd2 gene participates to mitochondrial integrity. Methods: We generated two mouse models, the first one leading to a partial knockdown of Hacd2 expression and the second one, to a complete knockout of Hacd2 expression. We performed an in-depth analysis of the associated phenotypes, from whole organism to molecular scale. Results: Thanks to these models, we show that Hacd2 displays an early and broad expression, and that its deficiency in mice is lethal. Specifically, partial knockdown of Hacd2 expression leads to death within one to four weeks after birth, from a sudden growth arrest followed by cachexia and lethargy. The total knockout of Hacd2 is even more severe, characterized by embryonic lethality around E9.5 following developmental arrest and pronounced cardiovascular malformations. In-depth mechanistic analysis revealed that Hacd2 deficiency causes altered mitochondrial efficiency and ultrastructure, as well as accumulation of oxidized cardiolipin. Conclusions: Altogether, these data indicate that the Hacd2 gene is essential for energetic metabolism during embryonic and postnatal development, acting through the control of proper mitochondrial organization and function.
MeSH term(s)	Animals ; Mice ; Cardiolipins ; Fatty Acids, Nonesterified/metabolism ; Hydro-Lyases/metabolism ; Membrane Proteins/metabolism ; Mitochondria/metabolism ; Mitochondrial Diseases/metabolism ; Phospholipids/metabolism
Chemical Substances	Cardiolipins ; Fatty Acids, Nonesterified ; Hydro-Lyases (EC 4.2.1.-) ; Membrane Proteins ; Phospholipids ; Hacd2 protein, mouse (EC 4.2.1.134)
Language	English
Publishing date	2023-01-21
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2708735-9
ISSN	2212-8778 ; 2212-8778
ISSN (online)	2212-8778
ISSN	2212-8778
DOI	10.1016/j.molmet.2023.101677
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Article ; Online: Hacd2 deficiency in mice leads to an early and lethal mitochondrial disease

Nahed Khadhraoui / Alexandre Prola / Aymeline Vandestienne / Jordan Blondelle / Laurent Guillaud / Guillaume Courtin / Maxime Bodak / Bastien Prost / Hélène Huet / Mélody Wintrebert / Christine Péchoux / Audrey Solgadi / Frédéric Relaix / Laurent Tiret / Fanny Pilot-Storck

Molecular Metabolism, Vol 69, Iss , Pp 101677- (2023)

2023

Abstract	Objective: Mitochondria fuel most animal cells with ATP, ensuring proper energetic metabolism of organs. Early and extensive mitochondrial dysfunction often leads to severe disorders through multiorgan failure. Hacd2 gene encodes an enzyme involved in very long chain fatty acid (C ≥ 18) synthesis, yet its roles in vivo remain poorly understood. Since mitochondria function relies on specific properties of their membranes conferred by a particular phospholipid composition, we investigated if Hacd2 gene participates to mitochondrial integrity. Methods: We generated two mouse models, the first one leading to a partial knockdown of Hacd2 expression and the second one, to a complete knockout of Hacd2 expression. We performed an in-depth analysis of the associated phenotypes, from whole organism to molecular scale. Results: Thanks to these models, we show that Hacd2 displays an early and broad expression, and that its deficiency in mice is lethal. Specifically, partial knockdown of Hacd2 expression leads to death within one to four weeks after birth, from a sudden growth arrest followed by cachexia and lethargy. The total knockout of Hacd2 is even more severe, characterized by embryonic lethality around E9.5 following developmental arrest and pronounced cardiovascular malformations. In-depth mechanistic analysis revealed that Hacd2 deficiency causes altered mitochondrial efficiency and ultrastructure, as well as accumulation of oxidized cardiolipin. Conclusions: Altogether, these data indicate that the Hacd2 gene is essential for energetic metabolism during embryonic and postnatal development, acting through the control of proper mitochondrial organization and function.
Keywords	Phospholipid ; Fatty acid ; VLCFA ; ELOVL ; OXPHOS coupling ; Heart development ; Internal medicine ; RC31-1245
Subject code	570 ; 572
Language	English
Publishing date	2023-03-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
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Article ; Online: Cullin E3 Ligase Activity Is Required for Myoblast Differentiation.

Blondelle, Jordan / Shapiro, Paige / Domenighetti, Andrea A / Lange, Stephan

Journal of molecular biology

2017 Volume 429, Issue 7, Page(s) 1045–1066

Abstract: The role of cullin E3-ubiquitin ligases for muscle homeostasis is best known during muscle atrophy, as the cullin-1 substrate adaptor atrogin-1 is among the most well-characterized muscle atrogins. We investigated whether cullin activity was also crucial ...

Abstract	The role of cullin E3-ubiquitin ligases for muscle homeostasis is best known during muscle atrophy, as the cullin-1 substrate adaptor atrogin-1 is among the most well-characterized muscle atrogins. We investigated whether cullin activity was also crucial during terminal myoblast differentiation and aggregation of acetylcholine receptors for the establishment of neuromuscular junctions in vitro. The activity of cullin E3-ligases is modulated through post-translational modification with the small ubiquitin-like modifier nedd8. Using either the Nae1 inhibitor MLN4924 (Pevonedistat) or siRNA against nedd8 in early or late stages of differentiation on C2C12 myoblasts, and primary satellite cells from mouse and human, we show that cullin E3-ligase activity is necessary for each step of the muscle cell differentiation program in vitro. We further investigate known transcriptional repressors for terminal muscle differentiation, namely ZBTB38, Bhlhe41, and Id1. Due to their identified roles for terminal muscle differentiation, we hypothesize that the accumulation of these potential cullin E3-ligase substrates may be partially responsible for the observed phenotype. MLN4924 is currently undergoing clinical trials in cancer patients, and our experiments highlight concerns on the homeostasis and regenerative capacity of muscles in these patients who often experience cachexia.
MeSH term(s)	Animals ; Cell Differentiation ; Cells, Cultured ; Humans ; Mice ; Myoblasts/enzymology ; Myoblasts/physiology ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2017-02-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2017.02.012
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Article: Cullin E3 Ligase Activity Is Required for Myoblast Differentiation

Blondelle, Jordan / Andrea A. Domenighetti / Paige Shapiro / Stephan Lange

Journal of Molecular Biology. 2017 Apr. 07, v. 429

2017

Abstract	The role of cullin E3-ubiquitin ligases for muscle homeostasis is best known during muscle atrophy, as the cullin-1 substrate adaptor atrogin-1 is among the most well-characterized muscle atrogins. We investigated whether cullin activity was also crucial during terminal myoblast differentiation and aggregation of acetylcholine receptors for the establishment of neuromuscular junctions in vitro.The activity of cullin E3-ligases is modulated through post-translational modification with the small ubiquitin-like modifier nedd8. Using either the Nae1 inhibitor MLN4924 (Pevonedistat) or siRNA against nedd8 in early or late stages of differentiation on C2C12 myoblasts, and primary satellite cells from mouse and human, we show that cullin E3-ligase activity is necessary for each step of the muscle cell differentiation program in vitro. We further investigate known transcriptional repressors for terminal muscle differentiation, namely ZBTB38, Bhlhe41, and Id1. Due to their identified roles for terminal muscle differentiation, we hypothesize that the accumulation of these potential cullin E3-ligase substrates may be partially responsible for the observed phenotype.MLN4924 is currently undergoing clinical trials in cancer patients, and our experiments highlight concerns on the homeostasis and regenerative capacity of muscles in these patients who often experience cachexia.
Keywords	cachexia ; cell differentiation ; cholinergic receptors ; clinical trials ; enzyme activity ; homeostasis ; humans ; in vitro studies ; mice ; muscles ; muscular atrophy ; myoblasts ; neoplasms ; patients ; post-translational modification ; repressor proteins ; small interfering RNA ; synapse ; ubiquitin-protein ligase
Language	English
Dates of publication	2017-0407
Size	p. 1045-1066.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2017.02.012
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Article ; Online: Cathepsins in heart disease-chewing on the heartache?

Blondelle, Jordan / Lange, Stephan / Greenberg, Barry H / Cowling, Randy T

American journal of physiology. Heart and circulatory physiology

2015 Volume 308, Issue 9, Page(s) H974–6

MeSH term(s)	Animals ; Cathepsin B/deficiency ; Female ; Humans ; Hypertrophy, Left Ventricular/prevention & control ; JNK Mitogen-Activated Protein Kinases/metabolism ; MAP Kinase Kinase Kinase 5/metabolism ; Male ; Myocytes, Cardiac/enzymology ; Tumor Necrosis Factor-alpha/metabolism ; Ventricular Function, Left ; Ventricular Remodeling
Chemical Substances	Tumor Necrosis Factor-alpha ; JNK Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; MAP Kinase Kinase Kinase 5 (EC 2.7.11.25) ; Cathepsin B (EC 3.4.22.1)
Language	English
Publishing date	2015-03-06
Publishing country	United States
Document type	Editorial ; Comment
ZDB-ID	603838-4
ISSN	1522-1539 ; 0363-6135
ISSN (online)	1522-1539
ISSN	0363-6135
DOI	10.1152/ajpheart.00125.2015
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Article ; Online: Cullin-3 dependent deregulation of ACTN1 represents a new pathogenic mechanism in nemaline myopathy.

Blondelle, Jordan / Tallapaka, Kavya / Seto, Jane T / Ghassemian, Majid / Clark, Madison / Laitila, Jenni M / Bournazos, Adam / Singer, Jeffrey D / Lange, Stephan

JCI insight

2019 Volume 5

Abstract: Nemaline myopathy is a congenital neuromuscular disorder characterized by muscle weakness, fiber atrophy and presence of nemaline bodies within myofibers. However, the understanding of underlying pathomechanisms is lacking. Recently, mutations in KBTBD13, ...

Abstract	Nemaline myopathy is a congenital neuromuscular disorder characterized by muscle weakness, fiber atrophy and presence of nemaline bodies within myofibers. However, the understanding of underlying pathomechanisms is lacking. Recently, mutations in KBTBD13, KLHL40 and KLHL41, three substrate adaptors for the E3-ubiquitin ligase Cullin-3, have been associated with early-onset nemaline myopathies. We hypothesized that deregulation of Cullin-3 and its muscle protein substrates may be responsible for the disease development. Using Cullin-3 knockout mice, we identified accumulation of non-muscle alpha-Actinins (ACTN1 and ACTN4) in muscles of these mice, which we also observed in KBTBD13 patients. Our data reveal that proper regulation of Cullin-3 activity and ACTN1 levels is essential for normal muscle and neuromuscular junction development. While ACTN1 is naturally downregulated during myogenesis, its overexpression in C2C12 myoblasts triggered defects in fusion, myogenesis and acetylcholine receptor clustering; features that we characterized in Cullin-3 deficient mice. Taken together, our data highlight the importance for Cullin-3 mediated degradation of ACTN1 for muscle development, and indicate a new pathomechanism for the etiology of myopathies seen in Cullin-3 knockout mice and nemaline myopathy patients.
MeSH term(s)	Actinin/metabolism ; Animals ; Cullin Proteins/genetics ; Cullin Proteins/metabolism ; Disease Models, Animal ; Gene Expression Regulation, Developmental ; Genetic Predisposition to Disease/genetics ; Humans ; Membrane Proteins/metabolism ; Mice ; Mice, Knockout/embryology ; Muscle Proteins/genetics ; Muscle Proteins/metabolism ; Muscle Weakness/embryology ; Muscle Weakness/genetics ; Muscle Weakness/metabolism ; Muscle, Skeletal/embryology ; Muscle, Skeletal/metabolism ; Muscular Diseases/metabolism ; Muscular Diseases/pathology ; Mutation ; Myopathies, Nemaline/embryology ; Myopathies, Nemaline/genetics ; Myopathies, Nemaline/metabolism ; Myopathies, Nemaline/pathology ; Neuromuscular Junction/growth & development ; Neuromuscular Junction/metabolism ; Neuromuscular Junction/pathology ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	ACTN1 protein, human ; ACTN4 protein, human ; C2CD2L protein, human ; Cullin Proteins ; KBTBD13 protein, human ; Membrane Proteins ; Muscle Proteins ; Actinin (11003-00-2) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2019-04-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2379-3708
ISSN (online)	2379-3708
DOI	10.1172/jci.insight.125665
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Article ; Online: Targeted Lipidomic Analysis of Myoblasts by GC-MS and LC-MS/MS.

Blondelle, Jordan / Pais de Barros, Jean-Paul / Pilot-Storck, Fanny / Tiret, Laurent

Methods in molecular biology (Clifton, N.J.)

2017 Volume 1668, Page(s) 39–60

Abstract: Lipids represent ∼10% of the cell dry mass and play essential roles in membrane composition and physical properties, energy storage, and signaling pathways. In the developing or the regenerating skeletal muscle, modifications in the content or the ... ...

Abstract	Lipids represent ∼10% of the cell dry mass and play essential roles in membrane composition and physical properties, energy storage, and signaling pathways. In the developing or the regenerating skeletal muscle, modifications in the content or the flipping between leaflets of membrane lipid components can modulate the fusion capacity of myoblasts, thus constituting one of the regulatory mechanisms underlying myofiber growth. Recently, few genes controlling these qualitative and quantitative modifications have started to be unraveled. The precise functional characterization of these genes requires both qualitative and quantitative evaluations of a global lipid profile. Here, we describe a lipidomic protocol using mass spectrometry, allowing assessing the content of fatty acids, glycerophospholipids, and cholesterol in the routinely used C2C12 mouse myoblast cell line, or in primary cultures of mouse myoblasts.
MeSH term(s)	Animals ; Cell Fusion ; Cell Line ; Cholesterol/analysis ; Cholesterol/metabolism ; Chromatography, Liquid ; Fatty Acids/analysis ; Fatty Acids/metabolism ; Gas Chromatography-Mass Spectrometry ; Glycerophospholipids/analysis ; Glycerophospholipids/metabolism ; Membrane Lipids/analysis ; Membrane Lipids/metabolism ; Mice ; Myoblasts/cytology ; Primary Cell Culture ; Tandem Mass Spectrometry
Chemical Substances	Fatty Acids ; Glycerophospholipids ; Membrane Lipids ; Cholesterol (97C5T2UQ7J)
Language	English
Publishing date	2017
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-7283-8_4
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Article ; Online: Murine obscurin and Obsl1 have functionally redundant roles in sarcolemmal integrity, sarcoplasmic reticulum organization, and muscle metabolism.

Blondelle, Jordan / Marrocco, Valeria / Clark, Madison / Desmond, Patrick / Myers, Stephanie / Nguyen, Jim / Wright, Matthew / Bremner, Shannon / Pierantozzi, Enrico / Ward, Samuel / Estève, Eric / Sorrentino, Vincenzo / Ghassemian, Majid / Lange, Stephan

Communications biology

2019 Volume 2, Page(s) 178

Abstract: Biological roles of obscurin and its close homolog Obsl1 (obscurin-like 1) have been enigmatic. While obscurin is highly expressed in striated muscles, Obsl1 is found ubiquitously. Accordingly, obscurin mutations have been linked to myopathies, whereas ... ...

Abstract	Biological roles of obscurin and its close homolog Obsl1 (obscurin-like 1) have been enigmatic. While obscurin is highly expressed in striated muscles, Obsl1 is found ubiquitously. Accordingly, obscurin mutations have been linked to myopathies, whereas mutations in Obsl1 result in 3M-growth syndrome. To further study unique and redundant functions of these closely related proteins, we generated and characterized Obsl1 knockouts. Global Obsl1 knockouts are embryonically lethal. In contrast, skeletal muscle-specific Obsl1 knockouts show a benign phenotype similar to obscurin knockouts. Only deletion of both proteins and removal of their functional redundancy revealed their roles for sarcolemmal stability and sarcoplasmic reticulum organization. To gain unbiased insights into changes to the muscle proteome, we analyzed tibialis anterior and soleus muscles by mass spectrometry, uncovering additional changes to the muscle metabolism. Our analyses suggest that all obscurin protein family members play functions for muscle membrane systems.
MeSH term(s)	Animals ; Cytoskeletal Proteins/deficiency ; Cytoskeletal Proteins/genetics ; Cytoskeletal Proteins/metabolism ; Female ; Humans ; Male ; Mice ; Mice, 129 Strain ; Mice, Knockout ; Muscle Development/genetics ; Muscle Development/physiology ; Muscle, Skeletal/growth & development ; Muscle, Skeletal/metabolism ; Protein Serine-Threonine Kinases/genetics ; Protein Serine-Threonine Kinases/metabolism ; Proteome/metabolism ; Rho Guanine Nucleotide Exchange Factors/genetics ; Rho Guanine Nucleotide Exchange Factors/metabolism ; Sarcoglycans/metabolism ; Sarcolemma/metabolism ; Sarcoplasmic Reticulum/metabolism
Chemical Substances	Cytoskeletal Proteins ; OBSL1 protein, human ; Proteome ; Rho Guanine Nucleotide Exchange Factors ; Sarcoglycans ; OBSCN protein, human (EC 2.7.11.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; obscn protein, mouse (EC 2.7.11.1)
Language	English
Publishing date	2019-05-09
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2399-3642
ISSN (online)	2399-3642
DOI	10.1038/s42003-019-0405-7
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