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Article ; Online: Molecular Insights into Aggrephagy: Their Cellular Functions in the Context of Neurodegenerative Diseases.

Cóppola-Segovia, Valentín / Reggiori, Fulvio

2024 , Page(s) 168493

Abstract: Protein homeostasis or proteostasis is an equilibrium of biosynthetic production, folding and transport of proteins, and their timely and efficient degradation. Proteostasis is guaranteed by a network of protein quality control systems aimed at ... ...

Abstract	Protein homeostasis or proteostasis is an equilibrium of biosynthetic production, folding and transport of proteins, and their timely and efficient degradation. Proteostasis is guaranteed by a network of protein quality control systems aimed at maintaining the proteome function and avoiding accumulation of potentially cytotoxic proteins. Terminal unfolded and dysfunctional proteins can be directly turned over by the ubiquitin-proteasome system (UPS) or first amassed into aggregates prior to degradation. Aggregates can also be disposed into lysosomes by a selective type of autophagy known as aggrephagy, which relies on a set of so-called selective autophagy receptors (SARs) and adaptor proteins. Failure in eliminating aggregates, also due to defects in aggrephagy, can have devastating effects as underscored by several neurodegenerative diseases or proteinopathies, which are characterized by the accumulation of aggregates mostly formed by a specific disease-associated, aggregate-prone protein depending on the clinical pathology. Despite its medical relevance, however, the process of aggrephagy is far from being understood. Here we review the findings that have helped in assigning a possible function to specific SARs and adaptor proteins in aggrephagy in the context of proteinopathies, and also highlight the interplay between aggrephagy and the pathogenesis of proteinopathies.
Language	English
Publishing date	2024-02-14
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2024.168493
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Article ; Online: Phagophore closure, autophagosome maturation and autophagosome fusion during macroautophagy in the yeast Saccharomyces cerevisiae

Kraft, Claudine / Reggiori, Fulvio

FEBS Letters. 2024 Jan., v. 598, no. 1 p.73-83

2024

Abstract: Macroautophagy, hereafter referred to as autophagy, is a complex process in which multiple membrane‐remodeling events lead to the formation of a cisterna known as the phagophore, which then expands and closes into a double‐membrane vesicle termed the ... ...

Abstract	Macroautophagy, hereafter referred to as autophagy, is a complex process in which multiple membrane‐remodeling events lead to the formation of a cisterna known as the phagophore, which then expands and closes into a double‐membrane vesicle termed the autophagosome. During the past decade, enormous progress has been made in understanding the molecular function of the autophagy‐related proteins and their role in generating these phagophores. In this Review, we discuss the current understanding of three membrane remodeling steps in autophagy that remain to be largely characterized; namely, the closure of phagophores, the maturation of the resulting autophagosomes into fusion‐competent vesicles, and their fusion with vacuoles/lysosomes. Our review will mainly focus on the yeast Saccharomyces cerevisiae, which has been the leading model system for the study of molecular events in autophagy and has led to the discovery of the major mechanistic concepts, which have been found to be mostly conserved in higher eukaryotes.
Keywords	Saccharomyces cerevisiae ; autophagosomes ; eukaryotic cells ; lysosomes ; macroautophagy ; yeasts
Language	English
Dates of publication	2024-01
Size	p. 73-83.
Publishing place	John Wiley & Sons, Ltd
Document type	Article ; Online
Note	REVIEW
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1002/1873-3468.14720
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Phagophore closure, autophagosome maturation and autophagosome fusion during macroautophagy in the yeast Saccharomyces cerevisiae.

Kraft, Claudine / Reggiori, Fulvio

FEBS letters

2023 Volume 598, Issue 1, Page(s) 73–83

Abstract: Macroautophagy, hereafter referred to as autophagy, is a complex process in which multiple membrane-remodeling events lead to the formation of a cisterna known as the phagophore, which then expands and closes into a double-membrane vesicle termed the ... ...

Abstract	Macroautophagy, hereafter referred to as autophagy, is a complex process in which multiple membrane-remodeling events lead to the formation of a cisterna known as the phagophore, which then expands and closes into a double-membrane vesicle termed the autophagosome. During the past decade, enormous progress has been made in understanding the molecular function of the autophagy-related proteins and their role in generating these phagophores. In this Review, we discuss the current understanding of three membrane remodeling steps in autophagy that remain to be largely characterized; namely, the closure of phagophores, the maturation of the resulting autophagosomes into fusion-competent vesicles, and their fusion with vacuoles/lysosomes. Our review will mainly focus on the yeast Saccharomyces cerevisiae, which has been the leading model system for the study of molecular events in autophagy and has led to the discovery of the major mechanistic concepts, which have been found to be mostly conserved in higher eukaryotes.
MeSH term(s)	Autophagosomes/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Macroautophagy ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Vacuoles/metabolism ; Autophagy/genetics ; Autophagy-Related Proteins/genetics ; Autophagy-Related Proteins/metabolism
Chemical Substances	Saccharomyces cerevisiae Proteins ; Autophagy-Related Proteins
Language	English
Publishing date	2023-08-23
Publishing country	England
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1002/1873-3468.14720
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Article ; Online: Wait, can you remind me just why we need another journal focused on autophagy?

Klionsky, Daniel J / Reggiori, Fulvio

Autophagy reports

2023 Volume 1, Issue 1, Page(s) 1–4

Abstract: Well, because you ask that question, we are going to attempt to explain exactly why we do indeed need another journal focused on autophagy. If you are reading this far, you presumably know what "autophagy" means, so we do not have to impress upon you the ...

Abstract	Well, because you ask that question, we are going to attempt to explain exactly why we do indeed need another journal focused on autophagy. If you are reading this far, you presumably know what "autophagy" means, so we do not have to impress upon you the importance of this topic, and how autophagic dysfunction is associated with numerous diseases in humans (okay, we felt compelled to slip that in anyway). Nor do we think that you need to be introduced to the journal
Language	English
Publishing date	2023-12-18
Publishing country	United States
Document type	Journal Article
ISSN	2769-4127
ISSN (online)	2769-4127
DOI	10.1080/27694127.2022.2034253
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: The yeast dynamin-like GTPase Vps1 mediates Atg9 transport to the phagophore assembly site in

Hu, Yan / Reggiori, Fulvio

Autophagy reports

2023 Volume 2, Issue 1, Page(s) 2247309

Abstract: Macroautophagy/autophagy is a degradative pathway that plays an important role in maintaining cellular homeostasis in eukaryotes. During autophagy, cisternal compartments called phagophores are generated to sequester intracellular components; these ... ...

Abstract	Macroautophagy/autophagy is a degradative pathway that plays an important role in maintaining cellular homeostasis in eukaryotes. During autophagy, cisternal compartments called phagophores are generated to sequester intracellular components; these structures mature into autophagosomes, which deliver the cargo into lysosomes/vacuoles for degradation. Numerous autophagy-related (Atg) proteins are part of the core machinery that mediates autophagosome biogenesis. Atg9, a lipid scramblase and the only multispanning transmembrane protein among the core Atg machinery, traffics between cytoplasmic reservoirs and the phagophore assembly site (PAS) to provide membranes, recruit other Atg proteins and rearrange lipids on the phagophore membrane. However, the factors mediating Atg9 trafficking remain to be fully understood. In our recent study, we found that the yeast dynamin-like GTPase Vps1 (vacuolar protein sorting 1) is involved in autophagy and is important for Atg9 transport to the PAS. Moreover, we showed that Vps1 function in autophagy requires its GTPase and oligomerization activities. Interestingly, specific mutations in DNM2 (dynamin 2), one of the human homologs of Vps1 that have been linked with specific human diseases such as microcytic anemia and Charcot-Marie-Tooth, also impairs Atg9 transport to the PAS, suggesting that a defect in autophagy may underlay the pathophysiology of these severe human pathologies.
Language	English
Publishing date	2023-12-14
Publishing country	United States
Document type	Journal Article
ISSN	2769-4127
ISSN (online)	2769-4127
DOI	10.1080/27694127.2023.2247309
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: The Organization and Function of the Phagophore-ER Membrane Contact Sites.

Vargas Duarte, Prado / Reggiori, Fulvio

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

2023 Volume 6, Page(s) 25152564231183898

Abstract: Macroautophagy is characterized by ... ...

Abstract	Macroautophagy is characterized by the
Language	English
Publishing date	2023-07-12
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	2964312-0
ISSN	2515-2564 ; 2515-2564
ISSN (online)	2515-2564
ISSN	2515-2564
DOI	10.1177/25152564231183898
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Beyond the C-terminal glycine of ATG8 proteins - The story of some neglected amino acids.

Barz, Saskia / Hofmann, Kay / Reggiori, Fulvio / Kraft, Claudine

Journal of molecular biology

2024 , Page(s) 168588

Abstract: ATG8 proteins form a family of small ubiquitin-like modifiers, well-known for their importance in both macroautophagy and autophagy-independent processes. A unique feature of this protein family is their conjugation to membrane lipids through the ... ...

Abstract	ATG8 proteins form a family of small ubiquitin-like modifiers, well-known for their importance in both macroautophagy and autophagy-independent processes. A unique feature of this protein family is their conjugation to membrane lipids through the covalent attachment of a glycine residue at the C-terminus of ATG8 proteins. Notably, most ATG8 proteins are expressed with additional amino acids at their C-terminus, shielding the key glycine residue. Consequently, lipidation requires the activation of the ATG8 precursors through proteolytic cleavage, known as priming. ATG4 proteases catalyze this priming process, and under physiological conditions, unprimed forms of ATG8 are not detected. This raises the question about the purpose of the C-terminal extension of ATG8 proteins. While the roles of lipidated and free, primed ATG8 proteins have been extensively studied, the potential function of their precursor form or the priming process itself remains largely unexplored. Here, we summarize information from existing literature and our own experiments to contribute to the understanding of these neglected amino acids.
Language	English
Publishing date	2024-04-23
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2024.168588
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Article ; Online: Membrane Contact Sites in Autophagy.

Zwilling, Emma / Reggiori, Fulvio

Cells

2022 Volume 11, Issue 23

Abstract: Eukaryotes utilize different communication strategies to coordinate processes between different cellular compartments either indirectly, through vesicular transport, or directly, via membrane contact sites (MCSs). MCSs have been implicated in lipid ... ...

Abstract	Eukaryotes utilize different communication strategies to coordinate processes between different cellular compartments either indirectly, through vesicular transport, or directly, via membrane contact sites (MCSs). MCSs have been implicated in lipid metabolism, calcium signaling and the regulation of organelle biogenesis in various cell types. Several studies have shown that MCSs play a crucial role in the regulation of macroautophagy, an intracellular catabolic transport route that is characterized by the delivery of cargoes (proteins, protein complexes or aggregates, organelles and pathogens) to yeast and plant vacuoles or mammalian lysosomes, for their degradation and recycling into basic metabolites. Macroautophagy is characterized by the de novo formation of double-membrane vesicles called autophagosomes, and their biogenesis requires an enormous amount of lipids. MCSs appear to have a central role in this supply, as well as in the organization of the autophagy-related (ATG) machinery. In this review, we will summarize the evidence for the participation of specific MCSs in autophagosome formation, with a focus on the budding yeast and mammalian systems.
Language	English
Publishing date	2022-11-28
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/cells11233813
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Molecular regulation of autophagosome formation.

Hu, Yan / Reggiori, Fulvio

Biochemical Society transactions

2022 Volume 50, Issue 1, Page(s) 55–69

Abstract: Macroautophagy, hereafter autophagy, is a degradative process conserved among eukaryotes, which is essential to maintain cellular homeostasis. Defects in autophagy lead to numerous human diseases, including various types of cancer and neurodegenerative ... ...

Abstract	Macroautophagy, hereafter autophagy, is a degradative process conserved among eukaryotes, which is essential to maintain cellular homeostasis. Defects in autophagy lead to numerous human diseases, including various types of cancer and neurodegenerative disorders. The hallmark of autophagy is the de novo formation of autophagosomes, which are double-membrane vesicles that sequester and deliver cytoplasmic materials to lysosomes/vacuoles for degradation. The mechanism of autophagosome biogenesis entered a molecular era with the identification of autophagy-related (ATG) proteins. Although there are many unanswered questions and aspects that have raised some controversies, enormous advances have been done in our understanding of the process of autophagy in recent years. In this review, we describe the current knowledge about the molecular regulation of autophagosome formation, with a particular focus on budding yeast and mammalian cells.
MeSH term(s)	Animals ; Autophagosomes/metabolism ; Autophagy ; Autophagy-Related Proteins/genetics ; Autophagy-Related Proteins/metabolism ; Humans ; Lysosomes/metabolism ; Macroautophagy ; Mammals/metabolism
Chemical Substances	Autophagy-Related Proteins
Language	English
Publishing date	2022-01-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST20210819
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Article ; Online: ER-phagy: mechanisms, regulation, and diseases connected to the lysosomal clearance of the endoplasmic reticulum.

Reggiori, Fulvio / Molinari, Maurizio

Physiological reviews

2022 Volume 102, Issue 3, Page(s) 1393–1448

Abstract: ER-phagy (reticulophagy) defines the degradation of portions of the endoplasmic reticulum (ER) within lysosomes or vacuoles. It is part of the self-digestion (i.e., autophagic) programs recycling cytoplasmic material and organelles, which rapidly ... ...

Abstract	ER-phagy (reticulophagy) defines the degradation of portions of the endoplasmic reticulum (ER) within lysosomes or vacuoles. It is part of the self-digestion (i.e., autophagic) programs recycling cytoplasmic material and organelles, which rapidly mobilize metabolites in cells confronted with nutrient shortage. Moreover, selective clearance of ER subdomains participates in the control of ER size and activity during ER stress, the reestablishment of ER homeostasis after ER stress resolution, and the removal of ER parts in which aberrant and potentially cytotoxic material has been segregated. ER-phagy relies on the individual and/or concerted activation of the ER-phagy receptors, ER peripheral or integral membrane proteins that share the presence of LC3/Atg8-binding motifs in their cytosolic domains. ER-phagy involves the physical separation of portions of the ER from the bulk ER network and their delivery to the endolysosomal/vacuolar catabolic district. This last step is accomplished by a variety of mechanisms including macro-ER-phagy (in which ER fragments are sequestered by double-membrane autophagosomes that eventually fuse with lysosomes/vacuoles), micro-ER-phagy (in which ER fragments are directly engulfed by endosomes/lysosomes/vacuoles), or direct fusion of ER-derived vesicles with lysosomes/vacuoles. ER-phagy is dysfunctional in specific human diseases, and its regulators are subverted by pathogens, highlighting its crucial role for cell and organism life.
MeSH term(s)	Autophagy ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum Stress ; Humans ; Lysosomes/metabolism ; Membrane Proteins/metabolism
Chemical Substances	Membrane Proteins
Language	English
Publishing date	2022-02-21
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	209902-0
ISSN	1522-1210 ; 0031-9333
ISSN (online)	1522-1210
ISSN	0031-9333
DOI	10.1152/physrev.00038.2021
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