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Article: Editorial: Post-translational Modifications and Compartmentalized Protein Quality Control in Cardiac Muscle and Disease.

Ranek, Mark J / Gomes, Aldrin V / Su, Huabo

2021 Volume 12, Page(s) 745887

Language	English
Publishing date	2021-08-30
Publishing country	Switzerland
Document type	Editorial
ZDB-ID	2564217-0
ISSN	1664-042X
ISSN	1664-042X
DOI	10.3389/fphys.2021.745887
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Article ; Online: Emerging Roles of Cullin-RING Ubiquitin Ligases in Cardiac Development.

Zambrano-Carrasco, Josue / Zou, Jianqiu / Wang, Wenjuan / Sun, Xinghui / Li, Jie / Su, Huabo

Cells

2024 Volume 13, Issue 3

Abstract: Heart development is a spatiotemporally regulated process that extends from the embryonic phase to postnatal stages. Disruption of this highly orchestrated process can lead to congenital heart disease or predispose the heart to cardiomyopathy or heart ... ...

Abstract	Heart development is a spatiotemporally regulated process that extends from the embryonic phase to postnatal stages. Disruption of this highly orchestrated process can lead to congenital heart disease or predispose the heart to cardiomyopathy or heart failure. Consequently, gaining an in-depth understanding of the molecular mechanisms governing cardiac development holds considerable promise for the development of innovative therapies for various cardiac ailments. While significant progress in uncovering novel transcriptional and epigenetic regulators of heart development has been made, the exploration of post-translational mechanisms that influence this process has lagged. Culling-RING E3 ubiquitin ligases (CRLs), the largest family of ubiquitin ligases, control the ubiquitination and degradation of ~20% of intracellular proteins. Emerging evidence has uncovered the critical roles of CRLs in the regulation of a wide range of cellular, physiological, and pathological processes. In this review, we summarize current findings on the versatile regulation of cardiac morphogenesis and maturation by CRLs and present future perspectives to advance our comprehensive understanding of how CRLs govern cardiac developmental processes.
MeSH term(s)	Ubiquitin/metabolism ; Cullin Proteins/metabolism ; Ubiquitination ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	Ubiquitin ; Cullin Proteins ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2024-01-26
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells13030235
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Article ; Online: Targeting neddylation E2 for anticancer therapy, putting new wine into new bottles?

Zou, Jianqiu / Su, Huabo

EBioMedicine

2019 Volume 45, Page(s) 3–4

MeSH term(s)	Humans ; Lung Neoplasms ; NEDD8 Protein ; Ubiquitins ; Wine
Chemical Substances	NEDD8 Protein ; NEDD8 protein, human ; Ubiquitins
Language	English
Publishing date	2019-07-09
Publishing country	Netherlands
Document type	Journal Article ; Comment
ZDB-ID	2851331-9
ISSN	2352-3964
ISSN (online)	2352-3964
DOI	10.1016/j.ebiom.2019.07.012
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Article ; Online: Multifaceted roles of Meg3 in cellular senescence and atherosclerosis.

Cheng, Xiao / Shihabudeen Haider Ali, Mohamed Sham / Baki, Vijaya Bhaskar / Moran, Matthew / Su, Huabo / Sun, Xinghui

Atherosclerosis

2024 Volume 392, Page(s) 117506

Abstract: Background and aims: Long noncoding RNAs are involved in the pathogenesis of atherosclerosis. As long noncoding RNAs maternally expressed gene 3 (Meg3) prevents cellular senescence of hepatic vascular endothelium and obesity-induced insulin resistance, ... ...

Abstract	Background and aims: Long noncoding RNAs are involved in the pathogenesis of atherosclerosis. As long noncoding RNAs maternally expressed gene 3 (Meg3) prevents cellular senescence of hepatic vascular endothelium and obesity-induced insulin resistance, we decided to examine its role in cellular senescence and atherosclerosis. Methods and results: By analyzing our data and human and mouse data from the Gene Expression Omnibus database, we found that Meg3 expression was reduced in humans and mice with cardiovascular disease, indicating its potential role in atherosclerosis. In Ldlr Conclusions: Our data demonstrate that Meg3 promotes the formation of atherosclerotic lesions independent of its effects on plasma lipid profiles. In addition, Meg3 regulates cellular senescence in a tissue-specific manner during atherosclerosis. Thus, we demonstrated that Meg3 has multifaceted roles in cellular senescence and atherosclerosis.
Language	English
Publishing date	2024-03-08
Publishing country	Ireland
Document type	Journal Article
ZDB-ID	80061-2
ISSN	1879-1484 ; 0021-9150
ISSN (online)	1879-1484
ISSN	0021-9150
DOI	10.1016/j.atherosclerosis.2024.117506
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Article ; Online: Proteasome malfunction activates the PPP3/calcineurin-TFEB-SQSTM1/p62 pathway to induce macroautophagy in the heart.

Su, Huabo / Wang, Xuejun

Autophagy

2020 Volume 16, Issue 11, Page(s) 2114–2116

Abstract: Proteasome inhibition (PSMI) is known to activate macroautophagy (autophagy hereafter), but the underlying mechanisms remain to be fully delineated. Here we discuss our recent work identifying an important PPP3/calcineurin-TFEB-SQSTM1/p62 pathway in ... ...

Abstract	Proteasome inhibition (PSMI) is known to activate macroautophagy (autophagy hereafter), but the underlying mechanisms remain to be fully delineated. Here we discuss our recent work identifying an important PPP3/calcineurin-TFEB-SQSTM1/p62 pathway in mediating activation of autophagy by PSMI, a compensatory process for the heart with proteasome malfunction. Through increasing PPP3/calcineurin activity and inhibiting MTOR signaling, PSMI promotes the dephosphorylation and thereby nuclear translocation of TFEB, resulting in transactivation of genes in the autophagic-lysosomal pathway (ALP) such as
MeSH term(s)	Autophagy ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors/metabolism ; Calcineurin/metabolism ; Macroautophagy ; Proteasome Endopeptidase Complex ; Sequestosome-1 Protein/metabolism
Chemical Substances	Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; Sequestosome-1 Protein ; Calcineurin (EC 3.1.3.16) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2020-09-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Comment
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2020.1816666
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Article ; Online: Neddylation Regulates Class IIa and III Histone Deacetylases to Mediate Myoblast Differentiation

Hongyi Zhou / Huabo Su / Weiqin Chen

International Journal of Molecular Sciences, Vol 22, Iss 9509, p

2021 Volume 9509

Abstract: As the largest tissue in the body, skeletal muscle has multiple functions in movement and energy metabolism. Skeletal myogenesis is controlled by a transcriptional cascade including a set of muscle regulatory factors (MRFs) that includes Myogenic ... ...

Abstract	As the largest tissue in the body, skeletal muscle has multiple functions in movement and energy metabolism. Skeletal myogenesis is controlled by a transcriptional cascade including a set of muscle regulatory factors (MRFs) that includes Myogenic Differentiation 1 (MYOD1), Myocyte Enhancer Factor 2 (MEF2), and Myogenin (MYOG), which direct the fusion of myogenic myoblasts into multinucleated myotubes. Neddylation is a posttranslational modification that covalently conjugates ubiquitin-like NEDD8 (neural precursor cell expressed, developmentally downregulated 8) to protein targets. Inhibition of neddylation impairs muscle differentiation; however, the underlying molecular mechanisms remain less explored. Here, we report that neddylation is temporally regulated during myoblast differentiation. Inhibition of neddylation through pharmacological blockade using MLN4924 (Pevonedistat) or genetic deletion of NEDD8 Activating Enzyme E1 Subunit 1 (NAE1), a subunit of the E1 neddylation-activating enzyme, blocks terminal myoblast differentiation partially through repressing MYOG expression. Mechanistically, we found that neddylation deficiency enhances the mRNA and protein expressions of class IIa histone deacetylases 4 and 5 (HDAC4 and 5) and prevents the downregulation and nuclear export of class III HDAC (NAD-Dependent Protein Deacetylase Sirtuin-1, SIRT1), all of which have been shown to repress MYOD1-mediated MYOG transcriptional activation. Together, our findings for the first time identify the crucial role of neddylation in mediating class IIa and III HDAC co-repressors to control myogenic program and provide new insights into the mechanisms of muscle disease and regeneration.
Keywords	neddylation ; histone deacetylases ; myoblast differentiation ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
Subject code	571
Language	English
Publishing date	2021-09-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
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Article ; Online: Neddylation Regulates Class IIa and III Histone Deacetylases to Mediate Myoblast Differentiation.

Zhou, Hongyi / Su, Huabo / Chen, Weiqin

International journal of molecular sciences

2021 Volume 22, Issue 17

Abstract	As the largest tissue in the body, skeletal muscle has multiple functions in movement and energy metabolism. Skeletal myogenesis is controlled by a transcriptional cascade including a set of muscle regulatory factors (MRFs) that includes Myogenic Differentiation 1 (MYOD1), Myocyte Enhancer Factor 2 (MEF2), and Myogenin (MYOG), which direct the fusion of myogenic myoblasts into multinucleated myotubes. Neddylation is a posttranslational modification that covalently conjugates ubiquitin-like NEDD8 (neural precursor cell expressed, developmentally downregulated 8) to protein targets. Inhibition of neddylation impairs muscle differentiation; however, the underlying molecular mechanisms remain less explored. Here, we report that neddylation is temporally regulated during myoblast differentiation. Inhibition of neddylation through pharmacological blockade using MLN4924 (Pevonedistat) or genetic deletion of NEDD8 Activating Enzyme E1 Subunit 1 (NAE1), a subunit of the E1 neddylation-activating enzyme, blocks terminal myoblast differentiation partially through repressing MYOG expression. Mechanistically, we found that neddylation deficiency enhances the mRNA and protein expressions of class IIa histone deacetylases 4 and 5 (HDAC4 and 5) and prevents the downregulation and nuclear export of class III HDAC (NAD-Dependent Protein Deacetylase Sirtuin-1, SIRT1), all of which have been shown to repress MYOD1-mediated MYOG transcriptional activation. Together, our findings for the first time identify the crucial role of neddylation in mediating class IIa and III HDAC co-repressors to control myogenic program and provide new insights into the mechanisms of muscle disease and regeneration.
MeSH term(s)	Cell Differentiation ; Cell Line ; Histone Deacetylases/genetics ; Histone Deacetylases/metabolism ; Humans ; MyoD Protein/genetics ; MyoD Protein/metabolism ; Myoblasts, Skeletal/metabolism ; Myogenin/genetics ; Myogenin/metabolism ; NEDD8 Protein/genetics ; NEDD8 Protein/metabolism ; Protein Processing, Post-Translational ; Repressor Proteins/genetics ; Repressor Proteins/metabolism ; Sirtuin 1/genetics ; Sirtuin 1/metabolism ; Ubiquitin-Activating Enzymes/genetics ; Ubiquitin-Activating Enzymes/metabolism
Chemical Substances	MYOG protein, human ; MyoD Protein ; MyoD1 myogenic differentiation protein ; Myogenin ; NEDD8 Protein ; NEDD8 protein, human ; Repressor Proteins ; SIRT1 protein, human (EC 3.5.1.-) ; Sirtuin 1 (EC 3.5.1.-) ; HDAC4 protein, human (EC 3.5.1.98) ; HDAC5 protein, human (EC 3.5.1.98) ; Histone Deacetylases (EC 3.5.1.98) ; Ubiquitin-Activating Enzymes (EC 6.2.1.45) ; NAE protein, human (EC 6.3.2.-)
Language	English
Publishing date	2021-09-01
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms22179509
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Article: The Ubiquitin Ligase RBX2/SAG Regulates Mitochondrial Ubiquitination and Mitophagy.

Wang, Wenjuan / Li, Ermin / Zou, Jianqiu / Qu, Chen / Ayala, Juan / Wen, Yuan / Islam, Md Sadikul / Weintraub, Neal L / Fulton, David J / Liang, Qiangrong / Zhou, Jiliang / Liu, Jinbao / Li, Jie / Sun, Yi / Su, Huabo

bioRxiv : the preprint server for biology

2024

Abstract: Clearance of damaged mitochondria via mitophagy is crucial for cellular homeostasis. While the role of ubiquitin (Ub) ligase PARKIN in mitophagy has been extensively studied, increasing evidence suggests the existence of PARKIN-independent mitophagy in ... ...

Abstract	Clearance of damaged mitochondria via mitophagy is crucial for cellular homeostasis. While the role of ubiquitin (Ub) ligase PARKIN in mitophagy has been extensively studied, increasing evidence suggests the existence of PARKIN-independent mitophagy in highly metabolically active organs such as the heart. Here, we identify a crucial role for Cullin-RING Ub ligase 5 (CRL5) in basal mitochondrial turnover in cardiomyocytes. CRL5 is a multi-subunit Ub ligase comprised by the catalytic RING box protein RBX2 (also known as SAG), scaffold protein Cullin 5 (CUL5), and a substrate-recognizing receptor. Analysis of the mitochondrial outer membrane-interacting proteome uncovered a robust association of CRLs with mitochondria. Subcellular fractionation, immunostaining, and immunogold electron microscopy established that RBX2 and Cul5, two core components of CRL5, localizes to mitochondria. Depletion of RBX2 inhibited mitochondrial ubiquitination and turnover, impaired mitochondrial membrane potential and respiration, and increased cell death in cardiomyocytes.
Language	English
Publishing date	2024-04-25
Publishing country	United States
Document type	Preprint
DOI	10.1101/2024.02.24.581168
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Article ; Online: A novel mouse model carrying a gene trap insertion into the Hmgxb4 gene locus to examine Hmgxb4 expression in vivo.

Wang, Liang / He, Xiangqin / Hu, Guoqing / Liu, Jinhua / Kang, Xiuhua / Yu, Luyi / Dong, Kunzhe / Zhao, Juanjuan / Zhang, Aizhen / Zhang, Wei / Brands, Michael W / Su, Huabo / Zheng, Zeqi / Zhou, Jiliang

Physiological reports

2024 Volume 12, Issue 8, Page(s) e16014

Abstract: HMG (high mobility group) proteins are a diverse family of nonhistone chromosomal proteins that interact with DNA and a wide range of transcriptional regulators to regulate the structural architecture of DNA. HMGXB4 (also known as HMG2L1) is an HMG ... ...

Abstract	HMG (high mobility group) proteins are a diverse family of nonhistone chromosomal proteins that interact with DNA and a wide range of transcriptional regulators to regulate the structural architecture of DNA. HMGXB4 (also known as HMG2L1) is an HMG protein family member that contains a single HMG box domain. Our previous studies have demonstrated that HMGXB4 suppresses smooth muscle differentiation and exacerbates endotoxemia by promoting a systemic inflammatory response in mice. However, the expression of Hmgxb4 in vivo has not fully examined. Herein, we generated a mouse model that harbors a gene trap in the form of a lacZ gene insertion into the Hmgxb4 gene. This mouse enables the visualization of endogenous HMGXB4 expression in different tissues via staining for the β-galactosidase activity of LacZ which is under the control of the endogenous Hmgxb4 gene promoter. We found that HMGXB4 is widely expressed in mouse tissues and is a nuclear protein. Furthermore, the Hmgxb4 gene trap mice exhibit normal cardiac function and blood pressure. Measurement of β-galactosidase activity in the Hmgxb4 gene trap mice demonstrated that the arterial injury significantly induces Hmgxb4 expression. In summary, the Hmgxb4 gene trap reporter mouse described here provides a valuable tool to examine the expression level of endogenous Hmgxb4 in both physiological and pathological settings in vivo.
MeSH term(s)	Animals ; Mice ; Mice, Inbred C57BL ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Male ; High Mobility Group Proteins/genetics ; High Mobility Group Proteins/metabolism ; Lac Operon/genetics ; Mice, Transgenic ; beta-Galactosidase/metabolism ; beta-Galactosidase/genetics
Chemical Substances	Transcription Factors ; High Mobility Group Proteins ; beta-Galactosidase (EC 3.2.1.23)
Language	English
Publishing date	2024-04-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2724325-4
ISSN	2051-817X ; 2051-817X
ISSN (online)	2051-817X
ISSN	2051-817X
DOI	10.14814/phy2.16014
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Article: Neddylation, an Emerging Mechanism Regulating Cardiac Development and Function.

Li, Jie / Zou, Jianqiu / Littlejohn, Rodney / Liu, Jinbao / Su, Huabo

Frontiers in physiology

2020 Volume 11, Page(s) 612927

Abstract: Defects in protein quality control have been increasingly recognized as pathogenic factors in the development of heart failure, a persistent devastating disease lacking efficacious therapies. Ubiquitin and ubiquitin-like proteins, a family of post- ... ...

Abstract	Defects in protein quality control have been increasingly recognized as pathogenic factors in the development of heart failure, a persistent devastating disease lacking efficacious therapies. Ubiquitin and ubiquitin-like proteins, a family of post-translational modifying polypeptides, play important roles in controlling protein quality by maintaining the stability and functional diversity of the proteome. NEDD8 (neural precursor cell expressed, developmentally downregulated 8), a small ubiquitin-like protein, was discovered two decades ago but until recently the biological significance of NEDD8 modifications (neddylation) in the heart has not been appreciated. In this review, we summarize the current knowledge of the biology of neddylation, highlighting several mechanisms by which neddylation regulates the function of its downstream targets, and discuss the expanding roles for neddylation in cardiac physiology and disease, with an emphasis on cardiac protein quality control. Finally, we outline challenges linked to the study of neddylation in health and disease.
Language	English
Publishing date	2020-12-17
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2564217-0
ISSN	1664-042X
ISSN	1664-042X
DOI	10.3389/fphys.2020.612927
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