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Article ; Online: Varicella zoster virus glycoprotein E facilitates PINK1/Parkin-mediated mitophagy to evade STING and MAVS-mediated antiviral innate immunity.

Oh, Soo-Jin / Yu, Je-Wook / Ahn, Jin-Hyun / Choi, Seok Tae / Park, Hosun / Yun, Jeanho / Shin, Ok Sarah

2024 Volume 15, Issue 1, Page(s) 16

Abstract: Viruses have evolved to control mitochondrial quality and content to facilitate viral replication. Mitophagy is a selective autophagy, in which the damaged or unnecessary mitochondria are removed, and thus considered an essential mechanism for ... ...

Abstract	Viruses have evolved to control mitochondrial quality and content to facilitate viral replication. Mitophagy is a selective autophagy, in which the damaged or unnecessary mitochondria are removed, and thus considered an essential mechanism for mitochondrial quality control. Although mitophagy manipulation by several RNA viruses has recently been reported, the effect of mitophagy regulation by varicella zoster virus (VZV) remains to be fully determined. In this study, we showed that dynamin-related protein-1 (DRP1)-mediated mitochondrial fission and subsequent PINK1/Parkin-dependent mitophagy were triggered during VZV infection, facilitating VZV replication. In addition, VZV glycoprotein E (gE) promoted PINK1/Parkin-mediated mitophagy by interacting with LC3 and upregulating mitochondrial reactive oxygen species. Importantly, VZV gE inhibited MAVS oligomerization and STING translocation to disrupt MAVS- and STING-mediated interferon (IFN) responses, and PINK1/Parkin-mediated mitophagy was required for VZV gE-mediated inhibition of IFN production. Similarly, carbonyl cyanide m-chlorophenyl hydrazone (CCCP)-mediated mitophagy induction led to increased VZV replication but attenuated IFN production in a three-dimensional human skin organ culture model. Our results provide new insights into the immune evasion mechanism of VZV gE via PINK1/Parkin-dependent mitophagy.
MeSH term(s)	Humans ; Mitophagy ; Immunity, Innate ; Carbonyl Cyanide m-Chlorophenyl Hydrazone ; Ubiquitin-Protein Ligases ; Antiviral Agents ; Protein Kinases
Chemical Substances	glycoprotein E, varicella-zoster virus ; Carbonyl Cyanide m-Chlorophenyl Hydrazone (555-60-2) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Antiviral Agents ; Protein Kinases (EC 2.7.-)
Language	English
Publishing date	2024-01-06
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2541626-1
ISSN	2041-4889 ; 2041-4889
ISSN (online)	2041-4889
ISSN	2041-4889
DOI	10.1038/s41419-023-06400-z
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Corrigendum: CVB3-Mediated Mitophagy Plays an Important Role in Viral Replication

Oh, Soo-Jin / Lim, Byung-Kwan / Yun, Jeanho / Shin, Ok Sarah

Frontiers in cellular and infection microbiology

2021 Volume 11, Page(s) 757341

Abstract: This corrects the article DOI: 10.3389/fcimb.2021.704494.]. ...

Abstract	[This corrects the article DOI: 10.3389/fcimb.2021.704494.].
Language	English
Publishing date	2021-09-10
Publishing country	Switzerland
Document type	Published Erratum
ZDB-ID	2619676-1
ISSN	2235-2988 ; 2235-2988
ISSN (online)	2235-2988
ISSN	2235-2988
DOI	10.3389/fcimb.2021.757341
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Article ; Online: CVB3-Mediated Mitophagy Plays an Important Role in Viral Replication

Oh, Soo-Jin / Lim, Byung-Kwan / Yun, Jeanho / Shin, Ok Sarah

Frontiers in cellular and infection microbiology

2021 Volume 11, Page(s) 704494

Abstract: Coxsackievirus B3 (CVB3) is a common enterovirus that causes systemic inflammatory diseases, such as myocarditis, meningitis, and encephalitis. CVB3 has been demonstrated to subvert host cellular ... ...

Abstract	Coxsackievirus B3 (CVB3) is a common enterovirus that causes systemic inflammatory diseases, such as myocarditis, meningitis, and encephalitis. CVB3 has been demonstrated to subvert host cellular responses
MeSH term(s)	Antiviral Agents/pharmacology ; Carbonyl Cyanide m-Chlorophenyl Hydrazone/pharmacology ; Enterovirus B, Human/pathogenicity ; Enterovirus B, Human/physiology ; HeLa Cells ; Humans ; Interferons/pharmacology ; Mitophagy ; Virus Replication
Chemical Substances	Antiviral Agents ; Carbonyl Cyanide m-Chlorophenyl Hydrazone (555-60-2) ; Interferons (9008-11-1)
Language	English
Publishing date	2021-07-06
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2619676-1
ISSN	2235-2988 ; 2235-2988
ISSN (online)	2235-2988
ISSN	2235-2988
DOI	10.3389/fcimb.2021.704494
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Nonstructural Protein NS1 of Influenza Virus Disrupts Mitochondrial Dynamics and Enhances Mitophagy via ULK1 and BNIP3.

Lee, Jae-Hwan / Oh, Soo-Jin / Yun, Jeanho / Shin, Ok Sarah

Viruses

2021 Volume 13, Issue 9

Abstract: Nonstructural protein 1 (NS1) of influenza virus (IFV) is essential for evading interferon (IFN)-mediated antiviral responses, thereby contributing to the pathogenesis of influenza. Mitophagy is a type of autophagy that selectively removes damaged ... ...

Abstract	Nonstructural protein 1 (NS1) of influenza virus (IFV) is essential for evading interferon (IFN)-mediated antiviral responses, thereby contributing to the pathogenesis of influenza. Mitophagy is a type of autophagy that selectively removes damaged mitochondria. The role of NS1 in IFV-mediated mitophagy is currently unknown. Herein, we showed that overexpression of NS1 protein led to enhancement of mitophagy. Mitophagy induction via carbonyl cyanide 3-chlorophenylhydrazone treatment in IFV-infected A549 cells led to increased viral replication efficiency, whereas the knockdown of PTEN-induced kinase 1 (PINK1) led to the opposite effect on viral replication. Overexpression of NS1 protein led to changes in mitochondrial dynamics, including depolarization of mitochondrial membrane potential. In contrast, infection with NS1-deficient virus resulted in impaired mitochondrial fragmentation, subsequent mitolysosomal formation, and mitophagy induction, suggesting an important role of NS1 in mitophagy. Meanwhile, NS1 protein increased the phosphorylation of Unc-51-like autophagy activating kinase 1 (ULK1) and the mitochondrial expression of BCL2- interacting protein 3 (BNIP3), both of which were found to be important for IFV-mediated mitophagy. Overall, these data highlight the importance of IFV NS1, ULK1, and BNIP3 during mitophagy activation.
MeSH term(s)	A549 Cells ; Animals ; Autophagy-Related Protein-1 Homolog/metabolism ; Carbonyl Cyanide m-Chlorophenyl Hydrazone/pharmacology ; Humans ; Influenza A Virus, H1N1 Subtype/metabolism ; Influenza A Virus, H1N1 Subtype/physiology ; Intracellular Signaling Peptides and Proteins/metabolism ; Membrane Potential, Mitochondrial ; Membrane Proteins/metabolism ; Mitochondria/physiology ; Mitochondrial Dynamics ; Mitophagy ; Proto-Oncogene Proteins/metabolism ; Viral Nonstructural Proteins/drug effects ; Viral Nonstructural Proteins/metabolism ; Virus Replication
Chemical Substances	BNIP3 protein, human ; INS1 protein, influenza virus ; Intracellular Signaling Peptides and Proteins ; Membrane Proteins ; Proto-Oncogene Proteins ; Viral Nonstructural Proteins ; Carbonyl Cyanide m-Chlorophenyl Hydrazone (555-60-2) ; Autophagy-Related Protein-1 Homolog (EC 2.7.11.1) ; ULK1 protein, human (EC 2.7.11.1)
Language	English
Publishing date	2021-09-15
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v13091845
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Article: The PINK1 Activator Niclosamide Mitigates Mitochondrial Dysfunction and Thermal Hypersensitivity in a Paclitaxel-Induced

Jang, Hye-Ji / Kim, Young-Yeon / Lee, Kang-Min / Shin, Jung-Eun / Yun, Jeanho

Biomedicines

2022 Volume 10, Issue 4

Abstract: Paclitaxel is a widely used anticancer drug that induces dose-limiting peripheral neuropathy. Mitochondrial dysfunction has been implicated in paclitaxel-induced neuronal damage and in the onset of peripheral neuropathy. We have previously shown that the ...

Abstract	Paclitaxel is a widely used anticancer drug that induces dose-limiting peripheral neuropathy. Mitochondrial dysfunction has been implicated in paclitaxel-induced neuronal damage and in the onset of peripheral neuropathy. We have previously shown that the expression of PINK1, a key mediator of mitochondrial quality control, ameliorated the paclitaxel-induced thermal hyperalgesia phenotype and restored mitochondrial homeostasis in
Language	English
Publishing date	2022-04-07
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2720867-9
ISSN	2227-9059
ISSN	2227-9059
DOI	10.3390/biomedicines10040863
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Article ; Online: Berberine Induces Mitophagy through Adenosine Monophosphate-Activated Protein Kinase and Ameliorates Mitochondrial Dysfunction in PINK1 Knockout Mouse Embryonic Fibroblasts.

Um, Jee-Hyun / Lee, Kang-Min / Kim, Young-Yeon / Lee, Da-Ye / Kim, Eunmi / Kim, Dong-Hyun / Yun, Jeanho

International journal of molecular sciences

2023 Volume 25, Issue 1

Abstract: Mitophagy stimulation has been shown to have a therapeutic effect on various neurodegenerative diseases. However, nontoxic mitophagy inducers are still very limited. In this study, we found that the natural alkaloid berberine exhibited mitophagy ... ...

Abstract	Mitophagy stimulation has been shown to have a therapeutic effect on various neurodegenerative diseases. However, nontoxic mitophagy inducers are still very limited. In this study, we found that the natural alkaloid berberine exhibited mitophagy stimulation activity in various human cells. Berberine did not interfere with mitochondrial function, unlike the well-known mitophagy inducer carbonyl cyanide m-chlorophenyl hydrazone (CCCP), and subsequently induced mitochondrial biogenesis. Berberine treatment induced the activation of adenosine monophosphate-activated protein kinase (AMPK), and the AMPK inhibitor compound C abolished berberine-induced mitophagy, suggesting that AMPK activation is essential for berberine-induced mitophagy. Notably, berberine treatment reversed mitochondrial dysfunction in PINK1 knockout mouse embryonic fibroblasts. Our results suggest that berberine is a mitophagy-specific inducer and can be used as a therapeutic treatment for neurodegenerative diseases, including Parkinson's disease, and that natural alkaloids are potential sources of mitophagy inducers.
MeSH term(s)	Animals ; Humans ; Mice ; Mice, Knockout ; Berberine/pharmacology ; AMP-Activated Protein Kinases ; Mitophagy ; Fibroblasts ; Carbonyl Cyanide m-Chlorophenyl Hydrazone/pharmacology ; Parkinson Disease ; Mitochondrial Diseases
Chemical Substances	Berberine (0I8Y3P32UF) ; AMP-Activated Protein Kinases (EC 2.7.11.31) ; Carbonyl Cyanide m-Chlorophenyl Hydrazone (555-60-2)
Language	English
Publishing date	2023-12-22
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/ijms25010219
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Article ; Online: Checkpoint-dependent phosphorylation of Med1/TRAP220 in response to DNA damage.

Kim, Hyun-Ju / Yun, Jeanho

Acta biochimica et biophysica Sinica

2017 Volume 49, Issue 6, Page(s) 496–502

Abstract: Mediator complex subunit 1 (Med1)/Thyroid hormone receptor-associated protein 220 (TRAP220), an essential component of thyroid hormone receptor-associated proteins (TRAP)/mediator, plays important roles in hormone responses and tumorigenesis. However, ... ...

Abstract	Mediator complex subunit 1 (Med1)/Thyroid hormone receptor-associated protein 220 (TRAP220), an essential component of thyroid hormone receptor-associated proteins (TRAP)/mediator, plays important roles in hormone responses and tumorigenesis. However, the role of Med1 in the DNA damage response has not been studied. In this study, we found that DNA damage, resulted from γ-irradiation, ultraviolet (UV)-irradiation, or hydroxyurea, induced phosphorylation of Med1 in vivo. Phosphorylation of Med1 was abrogated by either caffeine or wortmannin treatment, suggesting that Med1 is phosphorylated through the DNA damage checkpoint pathway. A checkpoint kinase 1 (Chk1)/checkpoint kinase 2 (Chk2) consensus phosphorylation motif was identified at Serine 671 of Med1 and Ser671 motif was primarily phosphorylated by Chk2 in vitro. Moreover, the in vivo phosphorylation of Med1 was abrogated by a Chk2 inhibitor, and physical interaction between Chk2 and Med1 was observed, confirming that Chk2 is responsible for Med1 phosphorylation upon DNA damage. These results suggest that Med1 is a novel target for the DNA damage checkpoint pathway and may participate in the DNA damage response. Consistent with this notion, knockdown of Med1 expression caused a significant increase in cellular sensitivity to UV irradiation. Moreover, microarray analysis revealed that the UV-induced activation of the transcription of important regulators of cell cycle control and DNA repair, including p21, Gadd45, Rad50, DnaJ, and RecQL, was impaired upon Med1 knockdown. Taken together, our data suggest that Med1 is a novel target for Chk2-mediated phosphorylation and may play a role in cellular DNA damage responses by mediating proper induction of gene transcription upon DNA damage.
Language	English
Publishing date	2017-06-01
Publishing country	China
Document type	Journal Article
ZDB-ID	2175256-4
ISSN	1745-7270 ; 0582-9879 ; 1672-9145
ISSN (online)	1745-7270
ISSN	0582-9879 ; 1672-9145
DOI	10.1093/abbs/gmx036
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Article ; Online: The Natural Alkaloid Palmatine Selectively Induces Mitophagy and Restores Mitochondrial Function in an Alzheimer's Disease Mouse Model.

Lee, Da-Ye / Lee, Kang-Min / Um, Jee-Hyun / Kim, Young-Yeon / Kim, Dong-Hyun / Yun, Jeanho

International journal of molecular sciences

2023 Volume 24, Issue 22

Abstract: Palmatine, a natural alkaloid found in various plants, has been reported to have diverse pharmacological and biological effects, including anti-inflammatory, antioxidant, and cardiovascular effects. However, the role of palmatine in mitophagy, a ... ...

Abstract	Palmatine, a natural alkaloid found in various plants, has been reported to have diverse pharmacological and biological effects, including anti-inflammatory, antioxidant, and cardiovascular effects. However, the role of palmatine in mitophagy, a fundamental process crucial for maintaining mitochondrial function, remains elusive. In this study, we found that palmatine efficiently induces mitophagy in various human cell lines. Palmatine specifically induces mitophagy and subsequently stimulates mitochondrial biogenesis. Palmatine did not interfere with mitochondrial function, similar to CCCP, suggesting that palmatine is not toxic to mitochondria. Importantly, palmatine treatment alleviated mitochondrial dysfunction in PINK1-knockout MEFs. Moreover, the administration of palmatine resulted in significant improvements in cognitive function and restored mitochondrial function in an Alzheimer's disease mouse model. This study identifies palmatine as a novel inducer of selective mitophagy. Our results suggest that palmatine-mediated mitophagy induction could be a potential strategy for Alzheimer's disease treatment and that natural alkaloids are potential sources of mitophagy inducers.
MeSH term(s)	Mice ; Animals ; Humans ; Mitophagy ; Alzheimer Disease/drug therapy ; Alzheimer Disease/metabolism ; Mitochondria/metabolism ; Alkaloids/pharmacology ; Alkaloids/therapeutic use ; Alkaloids/metabolism ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	palmatine (G50C034217) ; Alkaloids ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2023-11-20
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/ijms242216542
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Article ; Online: Emerging role of mitophagy in human diseases and physiology.

Um, Jee-Hyun / Yun, Jeanho

BMB reports

2017 Volume 50, Issue 6, Page(s) 299–307

Abstract: Mitophagy is a process of selective removal of damaged or unnecessary mitochondria using autophagic machinery. Mitophagy plays an essential role in maintaining mitochondrial quality control and homeostasis. Mitochondrial dysfunctions and defective ... ...

Abstract	Mitophagy is a process of selective removal of damaged or unnecessary mitochondria using autophagic machinery. Mitophagy plays an essential role in maintaining mitochondrial quality control and homeostasis. Mitochondrial dysfunctions and defective mitophagy in neurodegenerative diseases, cancer, and metabolic diseases indicate a close link between human disease and mitophagy. Furthermore, recent studies showing the involvement of mitophagy in differentiation and development, suggest that mitophagy may play a more active role in controlling cellular functions. A better understanding of mitophagy will provide insights about human disease and offer novel chance for treatment. This review mainly focuses on the recent implications for mitophagy in human diseases and normal physiology. [BMB Reports 2017; 50(6): 299-307].
MeSH term(s)	Animals ; Autophagy/genetics ; Autophagy/physiology ; Cell Differentiation/genetics ; Cell Differentiation/physiology ; Humans ; Mitochondria/metabolism ; Mitochondrial Degradation/genetics ; Mitochondrial Degradation/physiology ; Neurodegenerative Diseases/genetics ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/physiopathology
Language	English
Publishing date	2017-04-01
Publishing country	Korea (South)
Document type	Journal Article ; Review
ZDB-ID	2410389-5
ISSN	1976-670X ; 1976-6696
ISSN (online)	1976-670X
ISSN	1976-6696
DOI	10.5483/bmbrep.2017.50.6.056
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: The Mst1/2-BNIP3 axis is required for mitophagy induction and neuronal viability under mitochondrial stress.

Jeong, Dae Jin / Um, Jee-Hyun / Kim, Young Yeon / Shin, Dong Jin / Im, Sangwoo / Lee, Kang-Min / Lee, Yun-Hee / Lim, Dae-Sik / Kim, Donghoon / Yun, Jeanho

Experimental & molecular medicine

2024 Volume 56, Issue 3, Page(s) 674–685

Abstract: Mitophagy induction upon mitochondrial stress is critical for maintaining mitochondrial homeostasis and cellular function. Here, we found that Mst1/2 (Stk3/4), key regulators of the Hippo pathway, are required for the induction of mitophagy under various ...

Abstract	Mitophagy induction upon mitochondrial stress is critical for maintaining mitochondrial homeostasis and cellular function. Here, we found that Mst1/2 (Stk3/4), key regulators of the Hippo pathway, are required for the induction of mitophagy under various mitochondrial stress conditions. Knockdown of Mst1/2 or pharmacological inhibition by XMU-MP-1 treatment led to impaired mitophagy induction upon CCCP and DFP treatment. Mechanistically, Mst1/2 induces mitophagy independently of the PINK1-Parkin pathway and the canonical Hippo pathway. Moreover, our results suggest the essential involvement of BNIP3 in Mst1/2-mediated mitophagy induction upon mitochondrial stress. Notably, Mst1/2 knockdown diminishes mitophagy induction, exacerbates mitochondrial dysfunction, and reduces cellular survival upon neurotoxic stress in both SH-SY5Y cells and Drosophila models. Conversely, Mst1 and Mst2 expression enhances mitophagy induction and cell survival. In addition, AAV-mediated Mst1 expression reduced the loss of TH-positive neurons, ameliorated behavioral deficits, and improved mitochondrial function in an MPTP-induced Parkinson's disease mouse model. Our findings reveal the Mst1/2-BNIP3 regulatory axis as a novel mediator of mitophagy induction under conditions of mitochondrial stress and suggest that Mst1/2 play a pivotal role in maintaining mitochondrial function and neuronal viability in response to neurotoxic treatment.
MeSH term(s)	Animals ; Humans ; Mice ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mitochondria/metabolism ; Mitophagy/genetics ; Mitophagy/physiology ; Neuroblastoma ; Neurons/metabolism ; Protein Serine-Threonine Kinases/genetics ; Protein Serine-Threonine Kinases/metabolism ; Proto-Oncogene Proteins/genetics ; Proto-Oncogene Proteins/metabolism ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; Serine-Threonine Kinase 3/genetics ; Serine-Threonine Kinase 3/metabolism ; Drosophila/genetics
Chemical Substances	BNIP3 protein, human ; Membrane Proteins ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Proto-Oncogene Proteins ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; STK3 protein, human (EC 2.7.11.1) ; Stk3 protein, mouse (EC 2.7.11.1) ; STK4 protein, human (EC 2.7.1.11) ; Stk4 protein, mouse (EC 2.7.1.-) ; Serine-Threonine Kinase 3 (EC 2.7.11.1) ; hpo protein, Drosophila (EC 2.7.11.1) ; BNip3 protein, mouse
Language	English
Publishing date	2024-03-05
Publishing country	United States
Document type	Journal Article
ZDB-ID	1328915-9
ISSN	2092-6413 ; 1226-3613 ; 0378-8512
ISSN (online)	2092-6413
ISSN	1226-3613 ; 0378-8512
DOI	10.1038/s12276-024-01198-y
Database	MEDical Literature Analysis and Retrieval System OnLINE

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