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Article ; Online: Ruptured primary omental ectopic pregnancy during the first trimester.

Zhuang, Haixia / Zang, Jing / Luo, Hong

2023 Volume 25, Issue 4, Page(s) 481–482

Abstract: ...

Abstract	.
MeSH term(s)	Pregnancy ; Female ; Humans ; Pregnancy Trimester, First ; Pregnancy, Ectopic/diagnostic imaging ; Pregnancy, Ectopic/surgery ; Omentum/diagnostic imaging
Language	English
Publishing date	2023-12-27
Publishing country	Romania
Document type	Letter
ZDB-ID	2529606-1
ISSN	2066-8643 ; 1844-4172
ISSN (online)	2066-8643
ISSN	1844-4172
DOI	10.11152/mu-4313
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Article ; Online: Molecular Regulations of FUNDC1 at ER-Mitochondria Contacts Under Hypoxic Stress.

Zhang, Yi / Zhuang, Haixia / Liu, Hao / Feng, Du

Contact (Thousand Oaks (Ventura County, Calif.))

2022 Volume 5, Page(s) 25152564221092487

Abstract: A recent research paper published in Journal of Cell Biology by Chen and colleagues describes a novel mechanism by which the MAM (Mitochondrial-associated endoplasmic reticulum membrane) protein FUNDC1 (FUN14 domain-containing protein 1) regulates ... ...

Abstract	A recent research paper published in Journal of Cell Biology by Chen and colleagues describes a novel mechanism by which the MAM (Mitochondrial-associated endoplasmic reticulum membrane) protein FUNDC1 (FUN14 domain-containing protein 1) regulates mitochondrial division through altered protein post-translational modifications under hypoxic stress. The authors found that in a hypoxic environment, the endoplasmic reticulum-localized deubiquitinating enzyme USP19 accumulates at the MAM and interacts with the enriched mitochondrial outer membrane protein FUNDC1, which subsequently induces its deubiquitination and promotes the oligomerization and activity of DRP1, and mitochondria eventually divide in the presence of DRP1. This article provides new insights into the regulation of mitochondrial dynamics by FUNDC1 under hypoxic condition.
Language	English
Publishing date	2022-04-05
Publishing country	United States
Document type	Journal Article
ZDB-ID	2964312-0
ISSN	2515-2564 ; 2515-2564
ISSN (online)	2515-2564
ISSN	2515-2564
DOI	10.1177/25152564221092487
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Article ; Online: RNF6 promotes chronic myelogenous leukemia cell proliferation and migration by stabilizing vimentin via multiple atypical ubiquitinations.

Zhang, Hongxia / Zhong, Yueya / He, Yuanming / Xu, Yujia / Ren, Ying / Zhuang, Haixia / Sun, Tong / Zhu, Zhigang / Mao, Xinliang

Genes & diseases

2023 Volume 11, Issue 1, Page(s) 87–90

Language	English
Publishing date	2023-05-10
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2821806-1
ISSN	2352-3042 ; 2352-3042
ISSN (online)	2352-3042
ISSN	2352-3042
DOI	10.1016/j.gendis.2023.04.004
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Article ; Online: Molecular machineries and physiological relevance of ER-mediated membrane contacts.

Lin, Shiyin / Meng, Tian / Huang, Haofeng / Zhuang, Haixia / He, Zhengjie / Yang, Huan / Feng, Du

Theranostics

2021 Volume 11, Issue 2, Page(s) 974–995

Abstract: Membrane contact sites (MCSs) are defined as regions where two organelles are closely apposed, and most MCSs associated with each other via protein-protein or protein-lipid interactions. A number of key molecular machinery systems participate in ... ...

Abstract	Membrane contact sites (MCSs) are defined as regions where two organelles are closely apposed, and most MCSs associated with each other via protein-protein or protein-lipid interactions. A number of key molecular machinery systems participate in mediating substance exchange and signal transduction, both of which are essential processes in terms of cellular physiology and pathophysiology. The endoplasmic reticulum (ER) is the largest reticulum network within the cell and has extensive communication with other cellular organelles, including the plasma membrane (PM), mitochondria, Golgi, endosomes and lipid droplets (LDs). The contacts and reactions between them are largely mediated by various protein tethers and lipids. Ions, lipids and even proteins can be transported between the ER and neighboring organelles or recruited to the contact site to exert their functions. This review focuses on the key molecules involved in the formation of different contact sites as well as their biological functions.
MeSH term(s)	Animals ; Biological Transport ; Cell Membrane/metabolism ; Cell Physiological Phenomena ; Endoplasmic Reticulum/metabolism ; Endosomes/metabolism ; Humans ; Intracellular Membranes/metabolism ; Lipid Metabolism ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism
Language	English
Publishing date	2021-01-01
Publishing country	Australia
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2592097-2
ISSN	1838-7640 ; 1838-7640
ISSN (online)	1838-7640
ISSN	1838-7640
DOI	10.7150/thno.51871
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Article ; Online: ATP9A deficiency causes ADHD and aberrant endosomal recycling via modulating RAB5 and RAB11 activity.

Meng, Tian / Chen, Xiaoting / He, Zhengjie / Huang, Haofeng / Lin, Shiyin / Liu, Kunru / Bai, Guo / Liu, Hao / Xu, Mindong / Zhuang, Haixia / Zhang, Yunlong / Waqas, Ahmed / Liu, Qian / Zhang, Chuan / Sun, Xiang-Dong / Huang, Huansen / Umair, Muhammad / Yan, Yousheng / Feng, Du

Molecular psychiatry

2023 Volume 28, Issue 3, Page(s) 1219–1231

Abstract: ATP9A, a lipid flippase of the class II P4-ATPases, is involved in cellular vesicle trafficking. Its homozygous variants are linked to neurodevelopmental disorders in humans. However, its physiological function, the underlying mechanism as well as its ... ...

Abstract	ATP9A, a lipid flippase of the class II P4-ATPases, is involved in cellular vesicle trafficking. Its homozygous variants are linked to neurodevelopmental disorders in humans. However, its physiological function, the underlying mechanism as well as its pathophysiological relevance in humans and animals are still largely unknown. Here, we report two independent families in which the nonsense mutations c.433C>T/c.658C>T/c.983G>A (p. Arg145/p. Arg220/p. Trp328*) in ATP9A (NM_006045.3) cause autosomal recessive hypotonia, intellectual disability (ID) and attention deficit hyperactivity disorder (ADHD). Atp9a null mice show decreased muscle strength, memory deficits and hyperkinetic movement disorder, recapitulating the symptoms observed in patients. Abnormal neurite morphology and impaired synaptic transmission are found in the primary motor cortex and hippocampus of the Atp9a null mice. ATP9A is also required for maintaining neuronal neurite morphology and the viability of neural cells in vitro. It mainly localizes to endosomes and plays a pivotal role in endosomal recycling pathway by modulating small GTPase RAB5 and RAB11 activation. However, ATP9A pathogenic mutants have aberrant subcellular localization and cause abnormal endosomal recycling. These findings provide strong evidence that ATP9A deficiency leads to neurodevelopmental disorders and synaptic dysfunctions in both humans and mice, and establishes novel regulatory roles for ATP9A in RAB5 and RAB11 activity-dependent endosomal recycling pathway and neurological diseases.
MeSH term(s)	Animals ; Humans ; Mice ; Attention Deficit Disorder with Hyperactivity/metabolism ; Endosomes/metabolism ; Protein Transport ; rab5 GTP-Binding Proteins/genetics ; rab5 GTP-Binding Proteins/metabolism
Chemical Substances	rab5 GTP-Binding Proteins (EC 3.6.5.2) ; ATP9A protein, human (EC 7.6.2.1)
Language	English
Publishing date	2023-01-06
Publishing country	England
Document type	Case Reports ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1330655-8
ISSN	1476-5578 ; 1359-4184
ISSN (online)	1476-5578
ISSN	1359-4184
DOI	10.1038/s41380-022-01940-w
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Article ; Online: ATP9A knockdown leads to neurite fracture and retraction.

Molecular psychiatry

2023 Volume 28, Issue 3, Page(s) 967

MeSH term(s)	Neurites
Language	English
Publishing date	2023-03-10
Publishing country	England
Document type	Journal Article
ZDB-ID	1330655-8
ISSN	1476-5578 ; 1359-4184
ISSN (online)	1476-5578
ISSN	1359-4184
DOI	10.1038/s41380-023-01961-z
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Article ; Online: Prohibitin 1 regulates mtDNA release and downstream inflammatory responses.

Liu, Hao / Fan, Hualin / He, Pengcheng / Zhuang, Haixia / Liu, Xiao / Chen, Meiting / Zhong, Wenwei / Zhang, Yi / Zhen, Cien / Li, Yanling / Jiang, Huilin / Meng, Tian / Xu, Yiming / Zhao, Guojun / Feng, Du

The EMBO journal

2022 Volume 41, Issue 24, Page(s) e111173

Abstract: Exposure of mitochondrial DNA (mtDNA) to the cytosol activates innate immune responses. But the mechanisms by which mtDNA crosses the inner mitochondrial membrane are unknown. Here, we found that the inner mitochondrial membrane protein prohibitin 1 ( ... ...

Abstract	Exposure of mitochondrial DNA (mtDNA) to the cytosol activates innate immune responses. But the mechanisms by which mtDNA crosses the inner mitochondrial membrane are unknown. Here, we found that the inner mitochondrial membrane protein prohibitin 1 (PHB1) plays a critical role in mtDNA release by regulating permeability across the mitochondrial inner membrane. Loss of PHB1 results in alterations in mitochondrial integrity and function. PHB1-deficient macrophages, serum from myeloid-specific PHB1 KO (Phb1MyeKO) mice, and peripheral blood mononuclear cells from neonatal sepsis patients show increased interleukin-1β (IL-1β) levels. PHB1 KO mice are also intolerant of lipopolysaccharide shock. Phb1-depleted macrophages show increased cytoplasmic release of mtDNA and inflammatory responses. This process is suppressed by cyclosporine A and VBIT-4, which inhibit the mitochondrial permeability transition pore (mPTP) and VDAC oligomerization. Inflammatory stresses downregulate PHB1 expression levels in macrophages. Under normal physiological conditions, the inner mitochondrial membrane proteins, AFG3L2 and SPG7, are tethered to PHB1 to inhibit mPTP opening. Downregulation of PHB1 results in enhanced interaction between AFG3L2 and SPG7, mPTP opening, mtDNA release, and downstream inflammatory responses.
MeSH term(s)	Animals ; Humans ; Mice ; ATPases Associated with Diverse Cellular Activities/metabolism ; DNA, Mitochondrial/genetics ; Leukocytes, Mononuclear/metabolism ; Metalloendopeptidases/metabolism ; Prohibitins/metabolism ; Repressor Proteins/metabolism ; Mitochondrial Permeability Transition Pore
Chemical Substances	ATPases Associated with Diverse Cellular Activities (EC 3.6.4.-) ; DNA, Mitochondrial ; Metalloendopeptidases (EC 3.4.24.-) ; Prohibitins ; Repressor Proteins ; Spg7 protein, mouse (EC 3.4.24.-) ; Mitochondrial Permeability Transition Pore
Language	English
Publishing date	2022-10-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.15252/embj.2022111173
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Zs.A 1808: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Induction of zinc finger protein RNF6 auto-ubiquitination for the treatment of myeloma and chronic myeloid leukemia.

Zhuang, Haixia / Ren, Ying / Mao, Chenyu / Zhong, Yueya / Zhang, Zubin / Cao, Biyin / Zhang, Yuming / Huang, Jinqi / Xu, Guoqiang / Huang, Zhenqian / Xu, Yujia / Mao, Xinliang

The Journal of biological chemistry

2022 Volume 298, Issue 9, Page(s) 102314

Abstract: The zinc finger ubiquitin ligase RNF6 has been proposed as a potential therapeutic target in several cancers, but understanding its molecular mechanism of degradation has been elusive. In the present study, we find that RNF6 is degraded via auto- ... ...

Abstract	The zinc finger ubiquitin ligase RNF6 has been proposed as a potential therapeutic target in several cancers, but understanding its molecular mechanism of degradation has been elusive. In the present study, we find that RNF6 is degraded via auto-ubiquitination in a manner dependent on its Really Interesting New Gene (RING) domain. We determine that when the RING domain is deleted (ΔRING) or the core cysteine residues in the zinc finger are mutated (C632S/C635S), the WT protein, but not the ΔRING or mutant RNF6 protein, undergoes polyubiquitination. We also identify USP7 as a deubiquitinase of RNF6 by tandem mass spectrometry. We show that USP7 interacts with RNF6 and abolishes its K48-linked polyubiquitination, thereby preventing its degradation. In contrast, we found a USP7-specific inhibitor promotes RNF6 polyubiquitination, degradation, and cell death. Furthermore, we demonstrate the anti-leukemic drug Nilotinib and anti-myeloma drug Panobinostat (LBH589) induce RNF6 K48-linked polyubiquitination and degradation in both multiple myeloma (MM) and leukemia cells. In agreement with our hypothesis on the mode of RNF6 degradation, we show these drugs promote RNF6 auto-ubiquitination in an in vitro ubiquitination system without other E3 ligases. Consistently, reexpression of RNF6 ablates drug-induced MM and leukemia cell apoptosis. Therefore, our results reveal that RNF6 is a RING E3 ligase that undergoes auto-ubiquitination, which could be abolished by USP7 and induced by anti-cancer drugs. We propose that chemical induction of RNF6 auto-ubiquitination and degradation could be a novel strategy for the treatment of hematological malignancies including MM and leukemia.
MeSH term(s)	Antineoplastic Agents/pharmacology ; Antineoplastic Agents/therapeutic use ; Cysteine/metabolism ; DNA-Binding Proteins/metabolism ; Humans ; Leukemia, Myelogenous, Chronic, BCR-ABL Positive/drug therapy ; Leukemia, Myelogenous, Chronic, BCR-ABL Positive/genetics ; Multiple Myeloma/drug therapy ; Panobinostat/pharmacology ; Panobinostat/therapeutic use ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitin-Specific Peptidase 7/metabolism ; Ubiquitination ; Zinc Fingers
Chemical Substances	Antineoplastic Agents ; DNA-Binding Proteins ; RNF6 protein, human ; Ubiquitin ; Panobinostat (9647FM7Y3Z) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; USP7 protein, human (EC 3.4.19.12) ; Ubiquitin-Specific Peptidase 7 (EC 3.4.19.12) ; Cysteine (K848JZ4886)
Language	English
Publishing date	2022-08-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2022.102314
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Article: Mitochondrial Quality Control in Cardiomyocytes: A Critical Role in the Progression of Cardiovascular Diseases.

Fan, Hualin / He, Zhengjie / Huang, Haofeng / Zhuang, Haixia / Liu, Hao / Liu, Xiao / Yang, Sijun / He, Pengcheng / Yang, Huan / Feng, Du

Frontiers in physiology

2020 Volume 11, Page(s) 252

Abstract: Mitochondria serve as an energy plant and participate in a variety of signaling pathways to regulate cellular metabolism, survival and immunity. Mitochondrial dysfunction, in particular in cardiomyocytes, is associated with the development and ... ...

Abstract	Mitochondria serve as an energy plant and participate in a variety of signaling pathways to regulate cellular metabolism, survival and immunity. Mitochondrial dysfunction, in particular in cardiomyocytes, is associated with the development and progression of cardiovascular disease, resulting in heart failure, cardiomyopathy, and cardiac ischemia/reperfusion injury. Therefore, mitochondrial quality control processes, including post-translational modifications of mitochondrial proteins, mitochondrial dynamics, mitophagy, and formation of mitochondrial-driven vesicles, play a critical role in maintenance of mitochondrial and even cellular homeostasis in physiological or pathological conditions. Accumulating evidence suggests that mitochondrial quality control in cardiomyocytes is able to improve cardiac function, rescue dying cardiomyocytes, and prevent the deterioration of cardiovascular disease upon external environmental stress. In this review, we discuss recent progress in understanding mitochondrial quality control in cardiomyocytes. We also evaluate potential targets to prevent or treat cardiovascular diseases, and highlight future research directions which will help uncover additional mechanisms underlying mitochondrial homeostasis in cardiomyocytes.
Language	English
Publishing date	2020-03-27
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2564217-0
ISSN	1664-042X
ISSN	1664-042X
DOI	10.3389/fphys.2020.00252
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Article: Mitochondrial Contact Sites in Inflammation-Induced Cardiovascular Disease.

Liu, Hao / Liu, Xiao / Zhuang, Haixia / Fan, Hualin / Zhu, Dongxing / Xu, Yiming / He, Pengcheng / Liu, Jinbao / Feng, Du

Frontiers in cell and developmental biology

2020 Volume 8, Page(s) 692

Abstract: The mitochondrion, the ATP-producing center, is both physically and functionally associated with almost all other organelles in the cell. Mitochondrial-associated membranes (MAMs) are involved in a variety of biological processes, such as lipid exchange, ...

Abstract	The mitochondrion, the ATP-producing center, is both physically and functionally associated with almost all other organelles in the cell. Mitochondrial-associated membranes (MAMs) are involved in a variety of biological processes, such as lipid exchange, protein transport, mitochondrial fission, mitophagy, and inflammation. Several inflammation-related diseases in the cardiovascular system involve several intracellular events including mitochondrial dysfunction as well as disruption of MAMs. Therefore, an in-depth exploration of the function of MAMs will be of great significance for us to understand the initiation, progression, and clinical complications of cardiovascular disease (CVD). In this review, we summarize the recent advances in our knowledge of MAM regulation and function in CVD-related cells. We discuss the potential roles of MAMs in activating inflammation to influence the development of CVD.
Language	English
Publishing date	2020-07-30
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2737824-X
ISSN	2296-634X
ISSN	2296-634X
DOI	10.3389/fcell.2020.00692
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