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Article ; Online: The BPAN and intellectual disability disease proteins WDR45 and WDR45B modulate autophagosome-lysosome fusion.

Ji, Cuicui / Zhao, Yan G

2021 Volume 17, Issue 7, Page(s) 1783–1784

Abstract: WDR45 and WDR45B are β-propeller proteins belonging to the WIPI (WD repeat domain, phosphoinositide interacting) family. Mutations ... ...

Abstract	WDR45 and WDR45B are β-propeller proteins belonging to the WIPI (WD repeat domain, phosphoinositide interacting) family. Mutations in
MeSH term(s)	Autophagosomes ; Autophagy ; Carrier Proteins/genetics ; Humans ; Intellectual Disability/genetics ; Lysosomes ; Macroautophagy
Chemical Substances	Carrier Proteins ; WDR45 protein, human
Language	English
Publishing date	2021-06-09
Publishing country	United States
Document type	Journal Article ; 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	10.1080/15548627.2021.1924039
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Article ; Online: Endomembrane remodeling in SARS-CoV-2 infection.

Chen, Di / Zhao, Yan G / Zhang, Hong

Cell insight

2022 Volume 1, Issue 3, Page(s) 100031

Abstract: During severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection, the viral proteins intimately interact with host factors to remodel the endomembrane system at various steps of the viral lifecycle. The entry of SARS-CoV-2 can be mediated by ...

Abstract	During severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection, the viral proteins intimately interact with host factors to remodel the endomembrane system at various steps of the viral lifecycle. The entry of SARS-CoV-2 can be mediated by endocytosis-mediated internalization. Virus-containing endosomes then fuse with lysosomes, in which the viral S protein is cleaved to trigger membrane fusion. Double-membrane vesicles generated from the ER serve as platforms for viral replication and transcription. Virions are assembled at the ER-Golgi intermediate compartment and released through the secretory pathway and/or lysosome-mediated exocytosis. In this review, we will focus on how SARS-CoV-2 viral proteins collaborate with host factors to remodel the endomembrane system for viral entry, replication, assembly and egress. We will also describe how viral proteins hijack the host cell surveillance system-the autophagic degradation pathway-to evade destruction and benefit virus production. Finally, potential antiviral therapies targeting the host cell endomembrane system will be discussed.
Language	English
Publishing date	2022-05-17
Publishing country	Netherlands
Document type	Journal Article ; Review
ISSN	2772-8927
ISSN (online)	2772-8927
DOI	10.1016/j.cellin.2022.100031
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Article ; Online: Phase Separation in Membrane Biology: The Interplay between Membrane-Bound Organelles and Membraneless Condensates.

Zhao, Yan G / Zhang, Hong

Developmental cell

2020 Volume 55, Issue 1, Page(s) 30–44

Abstract: In eukaryotic cells, various membrane-bound organelles compartmentalize diverse cellular activities in a spatially and temporally controlled manner. Numerous membraneless organelles assembled via liquid-liquid phase separation (LLPS), known as ... ...

Abstract	In eukaryotic cells, various membrane-bound organelles compartmentalize diverse cellular activities in a spatially and temporally controlled manner. Numerous membraneless organelles assembled via liquid-liquid phase separation (LLPS), known as condensates, also facilitate compartmentalization of cellular functions. Emerging evidence shows that these two organelle types interact in many biological processes. Membranes modulate the biogenesis and dynamics of phase-separated condensates by serving as assembly platforms or by forming direct contacts. Phase separation of membrane-associated proteins participates in various trafficking events, such as clustering of vesicles for temporally controlled fusion and storage, and transport of membraneless condensates on membrane-bound organelles. Phase separation also acts in cargo trafficking pathways by sorting and docking cargos for translocon-mediated transport across membranes, by shuttling cargos through the nuclear pore complex, and by triggering the formation of surrounding autophagosomes for delivery to lysosomes. The coordinated actions of membrane-bound and membraneless organelles ensure spatiotemporal control of various cellular functions.
MeSH term(s)	Autophagosomes/metabolism ; Biology/methods ; Biophysical Phenomena/physiology ; Cell Physiological Phenomena/physiology ; Humans ; Membranes/metabolism ; Organelles/metabolism
Language	English
Publishing date	2020-07-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2054967-2
ISSN	1878-1551 ; 1534-5807
ISSN (online)	1878-1551
ISSN	1534-5807
DOI	10.1016/j.devcel.2020.06.033
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Zs.A 5742: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 76: Show issues

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Article ; Online: Machinery, regulation and pathophysiological implications of autophagosome maturation.

Zhao, Yan G / Codogno, Patrice / Zhang, Hong

Nature reviews. Molecular cell biology

2021 Volume 22, Issue 11, Page(s) 733–750

Abstract: Autophagy is a versatile degradation system for maintaining cellular homeostasis whereby cytosolic materials are sequestered in a double-membrane autophagosome and subsequently delivered to lysosomes, where they are broken down. In multicellular ... ...

Abstract	Autophagy is a versatile degradation system for maintaining cellular homeostasis whereby cytosolic materials are sequestered in a double-membrane autophagosome and subsequently delivered to lysosomes, where they are broken down. In multicellular organisms, newly formed autophagosomes undergo a process called 'maturation', in which they fuse with vesicles originating from endolysosomal compartments, including early/late endosomes and lysosomes, to form amphisomes, which eventually become degradative autolysosomes. This fusion process requires the concerted actions of multiple regulators of membrane dynamics, including SNAREs, tethering proteins and RAB GTPases, and also transport of autophagosomes and late endosomes/lysosomes towards each other. Multiple mechanisms modulate autophagosome maturation, including post-translational modification of key components, spatial distribution of phosphoinositide lipid species on membranes, RAB protein dynamics, and biogenesis and function of lysosomes. Nutrient status and various stresses integrate into the autophagosome maturation machinery to coordinate the progression of autophagic flux. Impaired autophagosome maturation is linked to the pathogenesis of various human diseases, including neurodegenerative disorders, cancer and myopathies. Furthermore, invading pathogens exploit various strategies to block autophagosome maturation, thus evading destruction and even subverting autophagic vacuoles (autophagosomes, amphisomes and autolysosomes) for survival, growth and/or release. Here, we discuss the recent progress in our understanding of the machinery and regulation of autophagosome maturation, the relevance of these mechanisms to human pathophysiology and how they are harnessed by pathogens for their benefit. We also provide perspectives on targeting autophagosome maturation therapeutically.
MeSH term(s)	Autophagosomes/genetics ; Autophagy/genetics ; Endosomes/genetics ; Humans ; Lysosomes/genetics ; Neurodegenerative Diseases/genetics ; Neurodegenerative Diseases/pathology ; Phagosomes/genetics ; Protein Processing, Post-Translational/genetics ; SNARE Proteins/genetics ; Transport Vesicles/genetics ; rab GTP-Binding Proteins/genetics
Chemical Substances	SNARE Proteins ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2021-07-23
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2031313-5
ISSN	1471-0080 ; 1471-0072
ISSN (online)	1471-0080
ISSN	1471-0072
DOI	10.1038/s41580-021-00392-4
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Zs.A 5446: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 26: Show issues

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Article ; Online: Core autophagy genes and human diseases.

Zhao, Yan G / Zhang, Hong

Current opinion in cell biology

2019 Volume 61, Page(s) 117–125

Abstract: Autophagy involves the formation of double-membrane autophagosomes and their delivery to lysosomes for degradation. In response to various endogenous and exogenous stimuli, autophagy recycles cellular constituents and removes cytotoxic threats such as ... ...

Abstract	Autophagy involves the formation of double-membrane autophagosomes and their delivery to lysosomes for degradation. In response to various endogenous and exogenous stimuli, autophagy recycles cellular constituents and removes cytotoxic threats such as protein aggregates and damaged organelles to maintain cellular homeostasis. Dysfunctional autophagy has been linked with multiple human diseases, including neurodegenerative diseases, tumorigenesis, diabetes, and immune diseases. Here we focus on human genetic disorders caused by hypomorphic or regulatory mutations in early acting autophagy genes or by mutations in genes acting at autophagosome maturation. Protein aggregates assembled via liquid-liquid phase separation (LLPS) exhibit distinct biophysical properties that are modulated by disease-related mutations. Abnormal phase transition of protein aggregates affects their removal and is associated with the pathogenesis of various neurodegenerative diseases.
MeSH term(s)	Animals ; Autophagosomes/metabolism ; Autophagy/genetics ; Autophagy/physiology ; Carcinogenesis/pathology ; Diabetes Mellitus/pathology ; Homeostasis ; Humans ; Immune System Diseases/pathology ; Lysosomes/metabolism ; Mice ; Mutation ; Neurodegenerative Diseases/pathology ; Protein Aggregates/genetics ; Protein Aggregates/physiology
Chemical Substances	Protein Aggregates
Language	English
Publishing date	2019-08-31
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1026381-0
ISSN	1879-0410 ; 0955-0674
ISSN (online)	1879-0410
ISSN	0955-0674
DOI	10.1016/j.ceb.2019.08.003
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Zs.A 2963: Show issues

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Article ; Online: Autophagosome maturation: An epic journey from the ER to lysosomes.

Zhao, Yan G / Zhang, Hong

The Journal of cell biology

2018 Volume 218, Issue 3, Page(s) 757–770

Abstract: Macroautophagy involves the sequestration of cytoplasmic contents in a double-membrane autophagosome and their delivery to lysosomes for degradation. In multicellular organisms, nascent autophagosomes fuse with vesicles originating from endolysosomal ... ...

Abstract	Macroautophagy involves the sequestration of cytoplasmic contents in a double-membrane autophagosome and their delivery to lysosomes for degradation. In multicellular organisms, nascent autophagosomes fuse with vesicles originating from endolysosomal compartments before forming degradative autolysosomes, a process known as autophagosome maturation. ATG8 family members, tethering factors, Rab GTPases, and SNARE proteins act coordinately to mediate fusion of autophagosomes with endolysosomal vesicles. The machinery mediating autophagosome maturation is under spatiotemporal control and provides regulatory nodes to integrate nutrient availability with autophagy activity. Dysfunction of autophagosome maturation is associated with various human diseases, including neurodegenerative diseases, Vici syndrome, cancer, and lysosomal storage disorders. Understanding the molecular mechanisms underlying autophagosome maturation will provide new insights into the pathogenesis and treatment of these diseases.
MeSH term(s)	Animals ; Autophagic Cell Death ; Autophagosomes/metabolism ; Autophagosomes/pathology ; Biological Transport, Active ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum/pathology ; Humans ; Lysosomes/metabolism ; Lysosomes/pathology ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/pathology
Language	English
Publishing date	2018-12-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.201810099
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Article ; Online: Formation and maturation of autophagosomes in higher eukaryotes: a social network.

Zhao, Yan G / Zhang, Hong

Current opinion in cell biology

2018 Volume 53, Page(s) 29–36

Abstract: Autophagy, a self-eating process conserved from yeast to mammals, is critical for maintaining cell homeostasis. It involves the formation of a double-membrane structure, called the autophagosome, and its subsequent delivery to lysosomes for degradation ... ...

Abstract	Autophagy, a self-eating process conserved from yeast to mammals, is critical for maintaining cell homeostasis. It involves the formation of a double-membrane structure, called the autophagosome, and its subsequent delivery to lysosomes for degradation of sequestrated materials. Our knowledge about autophagy has greatly expanded over the last two decades, mainly due to studies of a set of autophagy-related (ATG) genes identified from yeast genetic screens. Autophagy in higher eukaryotes is far more complicated, because it involves steps that are not present in yeast. These include the formation of extensive contacts between the ER and the isolation membrane (IM, autophagosome precursor), and the maturation of nascent autophagosomes into degradative autolysosomes via fusion with vesicles generated from the endolysosomal compartment. Recent studies have discovered factors that act at these unique steps, greatly advancing our molecular understanding of autophagy in higher eukaryotes.
MeSH term(s)	Animals ; Autophagosomes/metabolism ; Autophagy ; Endosomes/metabolism ; Eukaryotic Cells/cytology ; Eukaryotic Cells/metabolism ; Humans ; Lysosomes/metabolism ; Saccharomyces cerevisiae/metabolism
Language	English
Publishing date	2018-05-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1026381-0
ISSN	1879-0410 ; 0955-0674
ISSN (online)	1879-0410
ISSN	0955-0674
DOI	10.1016/j.ceb.2018.04.003
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Article ; Online: The ER-localized autophagy protein EPG-3/VMP1 regulates ER contacts with other organelles by modulating ATP2A/SERCA activity.

Zhao, Yan G / Zhang, Hong

Autophagy

2018 Volume 14, Issue 2, Page(s) 362–363

Abstract: The ER forms contacts with other endomembrane systems to exchange materials (e.g., calcium and lipids) and also to modulate dynamic organelle processes, including fission, cargo sorting and movement. During autophagosome formation, dynamic contacts ... ...

Abstract	The ER forms contacts with other endomembrane systems to exchange materials (e.g., calcium and lipids) and also to modulate dynamic organelle processes, including fission, cargo sorting and movement. During autophagosome formation, dynamic contacts between the ER and the phagophore membrane are crucial for phagophore expansion and closure. Little is known about the mechanisms underlying the formation and disassembly of the ER contacts. We found that the ER-localized autophagy protein EPG-3/VMP1 plays an essential role in controlling ER-phagophore dissociation and also the disassembly of ER contacts with LDs, mitochondria and endolysosomes. VMP1 regulates the ER contact by activating the ER calcium channel ATP2A/SERCA (ATPase sarcoplasmic/endoplasmic reticulum Ca2+ transporting). CALM (calmodulin) acts as one of the downstream calcium effectors that controls the PIK3C3/VPS34 phosphatidylinositol (PtdIns) 3-kinase (PtdIns3K) activity to maintain these contacts. Our study provides insights into the molecular mechanisms which regulate ER contacts and generate autophagosomes.
MeSH term(s)	Animals ; Autophagosomes/metabolism ; Autophagy/physiology ; Calmodulin/metabolism ; Endoplasmic Reticulum/metabolism ; Endosomes/metabolism ; Humans ; Lysosomes/metabolism ; Membrane Proteins/metabolism ; Mitochondria/metabolism ; Protein Transport ; Sarcoplasmic Reticulum Calcium-Transporting ATPases/metabolism
Chemical Substances	Calmodulin ; Membrane Proteins ; Sarcoplasmic Reticulum Calcium-Transporting ATPases (EC 3.6.3.8)
Language	English
Publishing date	2018-03-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2017.1415591
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Article ; Online: DMV biogenesis during β-coronavirus infection requires autophagy proteins VMP1 and TMEM41B.

Ji, Mingming / Li, Meng / Sun, Long / Deng, Hongyu / Zhao, Yan G

Autophagy

2022 Volume 19, Issue 2, Page(s) 737–738

Abstract: Upon entering host cells, β-coronaviruses specifically induce generation of replication organelles (ROs) from the endoplasmic reticulum (ER) through their nonstructural protein 3 (nsp3) and nsp4 for viral genome transcription and replication. The most ... ...

Abstract	Upon entering host cells, β-coronaviruses specifically induce generation of replication organelles (ROs) from the endoplasmic reticulum (ER) through their nonstructural protein 3 (nsp3) and nsp4 for viral genome transcription and replication. The most predominant ROs are double-membrane vesicles (DMVs). The ER-resident proteins VMP1 and TMEM41B, which form a complex to regulate autophagosome and lipid droplet (LD) formation, were recently shown to be essential for β-coronavirus infection. Here we report that VMP1 and TMEM41B contribute to DMV generation but function at different steps. TMEM41B facilitates nsp3-nsp4 interaction and ER zippering, while VMP1 is required for subsequent closing of the paired ER into DMVs. Additionally, inhibition of phosphatidylserine (PS) formation by
MeSH term(s)	Autophagy ; Coronavirus ; Coronavirus Infections ; Endoplasmic Reticulum ; Membrane Proteins ; Reactive Oxygen Species ; Virus Replication
Chemical Substances	Membrane Proteins ; Reactive Oxygen Species
Language	English
Publishing date	2022-07-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2022.2103783
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Article ; Online: LLPS of FXR proteins drives replication organelle clustering for β-coronaviral proliferation.

Li, Meng / Hou, Yali / Zhou, Yuzheng / Yang, Zhenni / Zhao, Hongyu / Jian, Tao / Yu, Qianxi / Zeng, Fuxing / Liu, Xiaotian / Zhang, Zheng / Zhao, Yan G

The Journal of cell biology

2024 Volume 223, Issue 6

Abstract: β-Coronaviruses remodel host endomembranes to form double-membrane vesicles (DMVs) as replication organelles (ROs) that provide a shielded microenvironment for viral RNA synthesis in infected cells. DMVs are clustered, but the molecular underpinnings and ...

Abstract	β-Coronaviruses remodel host endomembranes to form double-membrane vesicles (DMVs) as replication organelles (ROs) that provide a shielded microenvironment for viral RNA synthesis in infected cells. DMVs are clustered, but the molecular underpinnings and pathophysiological functions remain unknown. Here, we reveal that host fragile X-related (FXR) family proteins (FXR1/FXR2/FMR1) are required for DMV clustering induced by expression of viral non-structural proteins (Nsps) Nsp3 and Nsp4. Depleting FXRs results in DMV dispersion in the cytoplasm. FXR1/2 and FMR1 are recruited to DMV sites via specific interaction with Nsp3. FXRs form condensates driven by liquid-liquid phase separation, which is required for DMV clustering. FXR1 liquid droplets concentrate Nsp3 and Nsp3-decorated liposomes in vitro. FXR droplets facilitate recruitment of translation machinery for efficient translation surrounding DMVs. In cells depleted of FXRs, SARS-CoV-2 replication is significantly attenuated. Thus, SARS-CoV-2 exploits host FXR proteins to cluster viral DMVs via phase separation for efficient viral replication.
MeSH term(s)	Humans ; Cell Proliferation ; Cluster Analysis ; COVID-19/metabolism ; COVID-19/virology ; Cytoplasm ; Fragile X Mental Retardation Protein/metabolism ; HeLa Cells ; Liposomes/metabolism ; Organelles ; RNA-Binding Proteins/metabolism ; SARS-CoV-2 ; Viral Nonstructural Proteins/metabolism
Chemical Substances	Fragile X Mental Retardation Protein (139135-51-6) ; Liposomes ; RNA-Binding Proteins ; FXR1 protein, human ; FXR2 protein, human ; FMR1 protein, human ; Viral Nonstructural Proteins
Language	English
Publishing date	2024-04-08
Publishing country	United States
Document type	Journal Article
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202309140
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