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Article: The emerging roles of vacuolar-type ATPase-dependent Lysosomal acidification in neurodegenerative diseases.

Song, Qiaoyun / Meng, Bo / Xu, Haidong / Mao, Zixu

2020 Volume 9, Issue 1, Page(s) 17

Abstract: Background: Lysosomes digest extracellular material from the endocytic pathway and intracellular material from the autophagic pathway. This process is performed by the resident hydrolytic enzymes activated by the highly acidic pH within the lysosomal ... ...

Abstract	Background: Lysosomes digest extracellular material from the endocytic pathway and intracellular material from the autophagic pathway. This process is performed by the resident hydrolytic enzymes activated by the highly acidic pH within the lysosomal lumen. Lysosome pH gradients are mainly maintained by the vacuolar (H Main body: As a large multi-subunit complex, the V-ATPase is composed of an integral membrane V0 domain involved in proton translocation and a peripheral V1 domain catalyzing ATP hydrolysis. The canonical functions of V-ATPase rely on its H Conclusion: V-ATPase complex is a universal proton pump and plays an important role in lysosome acidification in all types of cells. Since V-ATPase dysfunction contributes to the pathogenesis of multiple neurodegenerative diseases, further understanding the mechanisms that regulate the canonical and non-canonical functions of V-ATPase will reveal molecular details of disease process and help assess V-ATPase or molecules related to its regulation as therapeutic targets.
MeSH term(s)	Humans ; Hydrogen-Ion Concentration ; Lysosomal Storage Diseases/metabolism ; Lysosomal Storage Diseases/therapy ; Lysosomes/metabolism ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/therapy ; Vacuolar Proton-Translocating ATPases/chemistry ; Vacuolar Proton-Translocating ATPases/metabolism ; Vacuoles/chemistry ; Vacuoles/metabolism
Chemical Substances	Vacuolar Proton-Translocating ATPases (EC 3.6.1.-)
Language	English
Publishing date	2020-05-11
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2653701-1
ISSN	2047-9158
ISSN	2047-9158
DOI	10.1186/s40035-020-00196-0
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Study of ATM Phosphorylation by Cdk5 in Neuronal Cells.

She, Hua / Mao, Zixu

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

2017 Volume 1599, Page(s) 363–374

Abstract: The phosphatidylinositol-3-kinase-like kinase ATM (ataxia-telangiectasia mutated) plays a central role in coordinating the DNA damage responses including cell cycle checkpoint control, DNA repair, and apoptosis. Mutations of ATM cause a spectrum of ... ...

Abstract	The phosphatidylinositol-3-kinase-like kinase ATM (ataxia-telangiectasia mutated) plays a central role in coordinating the DNA damage responses including cell cycle checkpoint control, DNA repair, and apoptosis. Mutations of ATM cause a spectrum of defects ranging from neurodegeneration to cancer predisposition. We previously showed that Cdk5 (cyclin-dependent kinase 5) is activated by DNA damage and directly phosphorylates ATM at serine 794 in postmitotic neurons. Phosphorylation at serine 794 precedes and is required for ATM autophosphorylation at serine 1981, and activates ATM kinase activity. Cdk5-ATM pathway plays a crucial role in DNA damage-induced neuronal injury. This chapter describes protocols used in analyzing ATM phosphorylation by Cdk5 in CGNs (cerebellar granule neurons) and its effects on neuronal survival.
Language	English
Publishing date	2017
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-6955-5_26
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Article: The question of cell cycle reentry by mature neurons in response to amyloid-beta and tau pathology.

Mao, Zixu

Journal of Alzheimer's disease : JAD

2009 Volume 17, Issue 1, Page(s) 49–51

MeSH term(s)	Amyloid beta-Peptides/metabolism ; Animals ; Cell Cycle/physiology ; Humans ; Neurons/physiology
Chemical Substances	Amyloid beta-Peptides
Language	English
Publishing date	2009
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	1440127-7
ISSN	1875-8908 ; 1387-2877
ISSN (online)	1875-8908
ISSN	1387-2877
DOI	10.3233/JAD-2009-1025
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Article: Autophagy in inflammation: the p38α MAPK-ULK1 axis.

She, Hua / He, Yingli / Zhao, Yingren / Mao, Zixu

Macrophage

2018 Volume 5

Abstract: Autophagy and inflammation are two processes vital for immune cells to perform their functions. Their proper interplay upon signal is pivotal for proper response to stress. The stress kinase p38α MAPK in microglia senses inflammatory cue LPS, directly ... ...

Abstract	Autophagy and inflammation are two processes vital for immune cells to perform their functions. Their proper interplay upon signal is pivotal for proper response to stress. The stress kinase p38α MAPK in microglia senses inflammatory cue LPS, directly phosphorylates ULK1, relieves the autophagic inhibition on the inflammatory machinery, and thus allows for a full immune response.
Language	English
Publishing date	2018-03-09
Publishing country	United States
Document type	Journal Article
ISSN	2378-136X
ISSN	2378-136X
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Article ; Online: Release the autophage brake on inflammation: The MAPK14/p38α-ULK1 pedal.

She, Hua / He, Yingli / Zhao, Yingren / Mao, Zixu

Autophagy

2018 Volume 14, Issue 6, Page(s) 1097–1098

Abstract: Macroautophagy/autophagy and inflammation are 2 intertwined processes vital for immune cells to perform their functions. Under resting conditions, autophagy acts as a brake to suppress inflammation in microglia. Upon signal stimulation, their fine-tuned ... ...

Abstract	Macroautophagy/autophagy and inflammation are 2 intertwined processes vital for immune cells to perform their functions. Under resting conditions, autophagy acts as a brake to suppress inflammation in microglia. Upon signal stimulation, their fine-tuned interplay is pivotal for proper response to stress. How inflammatory signals remove this autophagy brake on inflammation remains unclear. In a recent study, we showed that the stress kinase MAPK14/p38α in microglia senses the inflammatory cue lipopolysaccharide (LPS), directly phosphorylates and inhibits ULK1, relieves the autophagic inhibition on the inflammatory machinery, and thus allows for a full immune response.
MeSH term(s)	Autophagy ; Autophagy-Related Protein-1 Homolog ; Humans ; Inflammation ; Intracellular Signaling Peptides and Proteins ; Microglia ; Mitogen-Activated Protein Kinase 14 ; p38 Mitogen-Activated Protein Kinases
Chemical Substances	Intracellular Signaling Peptides and Proteins ; Autophagy-Related Protein-1 Homolog (EC 2.7.11.1) ; ULK1 protein, human (EC 2.7.11.1) ; Mitogen-Activated Protein Kinase 14 (EC 2.7.11.24) ; p38 Mitogen-Activated Protein Kinases (EC 2.7.11.24)
Language	English
Publishing date	2018-05-11
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	10.1080/15548627.2018.1446626
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Article ; Online: Signaling and induction of chaperone-mediated autophagy by the endoplasmic reticulum under stress conditions.

Li, Wenming / Yang, Qian / Mao, Zixu

Autophagy

2018 Volume 14, Issue 6, Page(s) 1094–1096

Abstract: Chaperone-mediated autophagy (CMA), a form of selective autophagy, maintains cellular proteostasis in response to diverse stress conditions. Whether and how endoplasmic reticulum (ER) stress triggers CMA remains elusive. In our recent study, we ... ...

Abstract	Chaperone-mediated autophagy (CMA), a form of selective autophagy, maintains cellular proteostasis in response to diverse stress conditions. Whether and how endoplasmic reticulum (ER) stress triggers CMA remains elusive. In our recent study, we demonstrate that various types of ER stress activate the CMA pathway via an EIF2AK3/PERK-MAP2K4/MKK4-MAPK14/p38-dependent manner. We term this process ERICA for ER stress-induced chaperone-mediated autophagy. This pathway is activated in response to stress associated with Parkinson disease and is required for the viability of the SNc dopaminergic neurons in an animal model of Parkinson disease.
MeSH term(s)	Animals ; Autophagy ; Endoplasmic Reticulum ; Endoplasmic Reticulum Stress ; Phosphorylation ; p38 Mitogen-Activated Protein Kinases
Chemical Substances	p38 Mitogen-Activated Protein Kinases (EC 2.7.11.24)
Language	English
Publishing date	2018-05-17
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	10.1080/15548627.2018.1444314
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Article ; Online: Chaperone-mediated autophagy degrades Keap1 and promotes Nrf2-mediated antioxidative response.

Zhu, Lin / He, Shulei / Huang, Lu / Ren, Dongni / Nie, Tiejian / Tao, Kai / Xia, Li / Lu, Fangfang / Mao, Zixu / Yang, Qian

Aging cell

2022 Volume 21, Issue 6, Page(s) e13616

Abstract: Accumulation of oxidative stress is highly intertwined with aging process and contributes to aging-related diseases, such as neurodegenerative diseases. Deciphering the molecular machinery that regulates oxidative stress is fundamental to further ... ...

Abstract	Accumulation of oxidative stress is highly intertwined with aging process and contributes to aging-related diseases, such as neurodegenerative diseases. Deciphering the molecular machinery that regulates oxidative stress is fundamental to further uncovering the pathogenesis of these diseases. Chaperone-mediated autophagy (CMA), a highly selective lysosome-dependent degradation process, has been proven to be an important maintainer of cellular homeostasis through multiple mechanisms, one of which is the attenuation of oxidative stress. However, the specific mechanisms underlying this antioxidative action of CMA are not fully understood. In this study, we found that CMA directly degrades Kelch-like ECH-associated protein 1 (Keap1), an adaptor of E3 ligase complex that promotes the degradation of nuclear factor erythroid 2-related factor 2 (Nrf2), which is a master transcriptional regulator in antioxidative response. Activated CMA induced by prolonged oxidative stress led to an increase in Nrf2 level by effectively degrading Keap1, contributing to Nrf2 nuclear translocation and the expression of multiple downstream antioxidative genes. Meanwhile, together with previous study showing that Nrf2 can also transcriptionally regulate LAMP2A, the rate-limiting factor of CMA process, we reveal a feed-forward loop between CMA and Nrf2. Our study identifies CMA as a previously unrecognized regulator of Keap1-Nrf2 pathway and reinforces the antioxidative role of CMA.
MeSH term(s)	Antioxidants/pharmacology ; Autophagy ; Chaperone-Mediated Autophagy ; GA-Binding Protein Transcription Factor ; Kelch-Like ECH-Associated Protein 1/genetics ; Kelch-Like ECH-Associated Protein 1/metabolism ; NF-E2-Related Factor 2/genetics ; NF-E2-Related Factor 2/metabolism ; Oxidative Stress
Chemical Substances	Antioxidants ; GA-Binding Protein Transcription Factor ; Kelch-Like ECH-Associated Protein 1 ; NF-E2-Related Factor 2
Language	English
Publishing date	2022-05-10
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2113083-8
ISSN	1474-9726 ; 1474-9718
ISSN (online)	1474-9726
ISSN	1474-9718
DOI	10.1111/acel.13616
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Article ; Online: Mechanisms Underlying Dysregulation of miR-132 in Alzheimer's Disease.

Song, Qiaoyun / Dou, Juan / Mao, Zixu / Wen, Zhexing / Li, Wenming

Biomedical journal of scientific & technical research

2019 Volume 22, Issue 5, Page(s) 17018–17020

Language	English
Publishing date	2019-11-15
Publishing country	United States
Document type	Journal Article
ISSN	2574-1241
ISSN (online)	2574-1241
DOI	10.26717/bjstr.2019.22.003824
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Article: Targeting Hsc70-based autophagy to eliminate amyloid β oligomers

Dou, Juan / Su, Peng / Xu, Chongchong / Wen, Zhexing / Mao, Zixu / Li, Wenming

Biochemical and biophysical research communications. 2020 Feb. 04,

2020

Abstract: Amyloid β (Aβ) oligomers may be a real culprit in the pathogenesis of Alzheimer’s disease (AD); therefore, the elimination of these toxic oligomers may be of great significance for AD therapy. Autophagy is the catabolic process by which lysosomes degrade ...

Abstract	Amyloid β (Aβ) oligomers may be a real culprit in the pathogenesis of Alzheimer’s disease (AD); therefore, the elimination of these toxic oligomers may be of great significance for AD therapy. Autophagy is the catabolic process by which lysosomes degrade cytosolic components, and heat shock cognate 70 kDa protein (Hsc70) binds to proteins with their KFERQ-like motifs [also known as chaperone-mediated autophagy (CMA) motifs] and carries them to lysosomes through CMA or late endosomes through endosomal microautophagy (eMI) for degradation. In this study, our strategy is to make the pathological Aβ become one selective and suitable substrate for CMA and eMI (termed as Hsc70-based autophagy) by tagging its oligomers with multiple CMA motifs. First, we design and synthesize Aβ oligomer binding peptides with three CMA motifs. Second, we determine that the peptide can help Aβ oligomers enter endosomes and lysosomes, which can be further enhanced by ketone. More importantly, we find that the peptide can dramatically reduce Aβ oligomers in induced pluripotent stem cell (iPSC) cortical neurons derived from AD patient fibroblasts and protect primary cultured cortical neurons against the Aβ oligomer-induced neurotoxicity. In conclusion, we demonstrate that the peptide targeting Hsc70-based autophagy can effectively eliminate Aβ oligomers and have superior neuroprotective activity.
Keywords	amyloid ; catabolism ; chaperone-mediated autophagy ; endosomes ; fibroblasts ; heat shock proteins ; lysosomes ; neuroprotective effect ; neurotoxicity ; pathogenesis ; patients ; peptides ; research ; stem cells ; therapeutics
Language	English
Dates of publication	2020-0204
Publishing place	Elsevier Inc.
Document type	Article
Note	NAL-AP-2-clean ; Pre-press version
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2020.02.016
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Article ; Online: Targeting Hsc70-based autophagy to eliminate amyloid β oligomers.

Dou, Juan / Su, Peng / Xu, Chongchong / Wen, Zhexing / Mao, Zixu / Li, Wenming

Biochemical and biophysical research communications

2020 Volume 524, Issue 4, Page(s) 923–928

Abstract: Amyloid β (Aβ) oligomers may be a real culprit in the pathogenesis of Alzheimer's disease (AD); therefore, the elimination of these toxic oligomers may be of great significance for AD therapy. Autophagy is the catabolic process by which lysosomes degrade ...

Abstract	Amyloid β (Aβ) oligomers may be a real culprit in the pathogenesis of Alzheimer's disease (AD); therefore, the elimination of these toxic oligomers may be of great significance for AD therapy. Autophagy is the catabolic process by which lysosomes degrade cytosolic components, and heat shock cognate 70 kDa protein (Hsc70) binds to proteins with their KFERQ-like motifs [also known as chaperone-mediated autophagy (CMA) motifs] and carries them to lysosomes through CMA or late endosomes through endosomal microautophagy (eMI) for degradation. In this study, our strategy is to make the pathological Aβ become one selective and suitable substrate for CMA and eMI (termed as Hsc70-based autophagy) by tagging its oligomers with multiple CMA motifs. First, we design and synthesize Aβ oligomer binding peptides with three CMA motifs. Second, we determine that the peptide can help Aβ oligomers enter endosomes and lysosomes, which can be further enhanced by ketone. More importantly, we find that the peptide can dramatically reduce Aβ oligomers in induced pluripotent stem cell (iPSC) cortical neurons derived from AD patient fibroblasts and protect primary cultured cortical neurons against the Aβ oligomer-induced neurotoxicity. In conclusion, we demonstrate that the peptide targeting Hsc70-based autophagy can effectively eliminate Aβ oligomers and have superior neuroprotective activity.
MeSH term(s)	Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Alzheimer Disease/therapy ; Amino Acid Motifs ; Amyloid beta-Peptides/antagonists & inhibitors ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Peptides/pharmacology ; Animals ; Cell Differentiation ; Cerebral Cortex/metabolism ; Cerebral Cortex/pathology ; Chaperone-Mediated Autophagy/drug effects ; Endosomes/drug effects ; Endosomes/metabolism ; Fibroblasts/drug effects ; Fibroblasts/metabolism ; Fibroblasts/pathology ; HSC70 Heat-Shock Proteins/genetics ; HSC70 Heat-Shock Proteins/metabolism ; Humans ; Induced Pluripotent Stem Cells/drug effects ; Induced Pluripotent Stem Cells/metabolism ; Induced Pluripotent Stem Cells/pathology ; Lysosomes/drug effects ; Lysosomes/metabolism ; Molecular Targeted Therapy ; Neurons/drug effects ; Neurons/metabolism ; Neurons/pathology ; Neuroprotective Agents/chemical synthesis ; Neuroprotective Agents/pharmacology ; Peptides/chemical synthesis ; Peptides/pharmacology ; Primary Cell Culture ; Protein Binding ; Proteolysis ; Rats ; Rats, Long-Evans
Chemical Substances	Amyloid beta-Peptides ; HSC70 Heat-Shock Proteins ; Neuroprotective Agents ; Peptides
Language	English
Publishing date	2020-02-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2020.02.016
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