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Article: Regulation of Autophagy in Cells Infected With Oncogenic Human Viruses and Its Impact on Cancer Development.

Vescovo, Tiziana / Pagni, Benedetta / Piacentini, Mauro / Fimia, Gian Maria / Antonioli, Manuela

Frontiers in cell and developmental biology

2020 Volume 8, Page(s) 47

Abstract: About 20% of total cancer cases are associated to infections. To date, seven human viruses have been directly linked to cancer development: high-risk human papillomaviruses (hrHPVs), Merkel cell polyomavirus (MCPyV), hepatitis B virus (HBV), hepatitis C ... ...

Abstract	About 20% of total cancer cases are associated to infections. To date, seven human viruses have been directly linked to cancer development: high-risk human papillomaviruses (hrHPVs), Merkel cell polyomavirus (MCPyV), hepatitis B virus (HBV), hepatitis C virus (HCV), Epstein-Barr virus (EBV), Kaposi's sarcoma-associated herpesvirus (KSHV), and human T-lymphotropic virus 1 (HTLV-1). These viruses impact on several molecular mechanisms in the host cells, often resulting in chronic inflammation, uncontrolled proliferation, and cell death inhibition, and mechanisms, which favor viral life cycle but may indirectly promote tumorigenesis. Recently, the ability of oncogenic viruses to alter autophagy, a catabolic process activated during the innate immune response to infections, is emerging as a key event for the onset of human cancers. Here, we summarize the current understanding of the molecular mechanisms by which human oncogenic viruses regulate autophagy and how this negative regulation impacts on cancer development. Finally, we highlight novel autophagy-related candidates for the treatment of virus-related cancers.
Language	English
Publishing date	2020-02-28
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2737824-X
ISSN	2296-634X
ISSN	2296-634X
DOI	10.3389/fcell.2020.00047
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Article ; Online: TRIM proteins in autophagy: selective sensors in cell damage and innate immune responses.

Di Rienzo, Martina / Romagnoli, Alessandra / Antonioli, Manuela / Piacentini, Mauro / Fimia, Gian Maria

Cell death and differentiation

2020 Volume 27, Issue 3, Page(s) 887–902

Abstract: Autophagy, a main intracellular catabolic process, is induced in response to a variety of cellular stresses to promptly degrade harmful agents and to coordinate the activity of prosurvival and prodeath processes in order to determine the fate of the ... ...

Abstract	Autophagy, a main intracellular catabolic process, is induced in response to a variety of cellular stresses to promptly degrade harmful agents and to coordinate the activity of prosurvival and prodeath processes in order to determine the fate of the injured cells. While the main components of the autophagy machinery are well characterized, the molecular mechanisms that confer selectivity to this process both in terms of stress detection and cargo engulfment have only been partly elucidated. Here, we discuss the emerging role played by the E3 ubiquitin ligases of the TRIM family in regulating autophagy in physiological and pathological conditions, such as inflammation, infection, tumorigenesis, and muscle atrophy. TRIM proteins employ different strategies to regulate the activity of the core autophagy machinery, acting either as scaffold proteins or via ubiquitin-mediated mechanisms. Moreover, they confer high selectivity to the autophagy-mediated degradation as described for the innate immune response, where TRIM proteins mediate both the engulfment of pathogens within autophagosomes and modulate the immune response by controlling the stability of signaling regulators. Importantly, the elucidation of the molecular mechanisms underlying the regulation of autophagy by TRIMs is providing important insights into how selective types of autophagy are altered under pathological conditions, as recently shown in cancer and muscular dystrophy.
MeSH term(s)	Animals ; Autophagy ; Cells/pathology ; Humans ; Immunity, Innate ; Models, Biological ; Signal Transduction ; Tripartite Motif Proteins/metabolism
Chemical Substances	Tripartite Motif Proteins
Language	English
Publishing date	2020-01-22
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1225672-9
ISSN	1476-5403 ; 1350-9047
ISSN (online)	1476-5403
ISSN	1350-9047
DOI	10.1038/s41418-020-0495-2
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Zs.A 4230: 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)
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Article ; Online: NAADP-Evoked Ca

Pereira, Cássia Arruda de Souza / Medaglia, Natalia de Castro / Ureshino, Rodrigo Portes / Bincoletto, Claudia / Antonioli, Manuela / Fimia, Gian Maria / Piacentini, Mauro / Pereira, Gustavo José da Silva / Erustes, Adolfo Garcia / Smaili, Soraya Soubhi

International journal of molecular sciences

2023 Volume 24, Issue 6

Abstract: Huntington's disease (HD) is a progressive neurodegenerative disease characterized by mutations in the huntingtin gene (mHtt), causing an unstable repeat of the CAG trinucleotide, leading to abnormal long repeats of polyglutamine (poly-Q) in the N- ... ...

Abstract	Huntington's disease (HD) is a progressive neurodegenerative disease characterized by mutations in the huntingtin gene (mHtt), causing an unstable repeat of the CAG trinucleotide, leading to abnormal long repeats of polyglutamine (poly-Q) in the N-terminal region of the huntingtin, which form abnormal conformations and aggregates. Alterations in Ca
MeSH term(s)	Mice ; Animals ; Calcium Channels/metabolism ; Astrocytes/metabolism ; Neurodegenerative Diseases/metabolism ; NADP/metabolism ; Lysosomes/metabolism ; Autophagy ; Calcium/metabolism ; Huntingtin Protein/genetics ; Huntingtin Protein/metabolism
Chemical Substances	Calcium Channels ; NAADP (5502-96-5) ; NADP (53-59-8) ; Calcium (SY7Q814VUP) ; Huntingtin Protein
Language	English
Publishing date	2023-03-15
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/ijms24065593
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Article: Emerging Mechanisms in Initiating and Terminating Autophagy.

Antonioli, Manuela / Di Rienzo, Martina / Piacentini, Mauro / Fimia, Gian Maria

Trends in biochemical sciences

2017 Volume 42, Issue 1, Page(s) 28–41

Abstract: Autophagy is a major degradative process activated in a rapid and transient manner to cope with stress conditions. Whether autophagy is beneficial or detrimental depends upon the rate of induction and the appropriateness of the duration. Alterations in ... ...

Abstract	Autophagy is a major degradative process activated in a rapid and transient manner to cope with stress conditions. Whether autophagy is beneficial or detrimental depends upon the rate of induction and the appropriateness of the duration. Alterations in both autophagy initiation and termination predispose the cell to death, and affect the execution of other inducible processes such as inflammation. In this review we discuss how stress signaling pathways dynamically control the activity of the autophagy machinery by mediating post-translational modifications and regulatory protein interactions. In particular, we highlight the emerging role of TRIM and CULLIN families of ubiquitin ligases which play opposite roles in the autophagy response by promoting or inhibiting, respectively, the activity of the autophagy initiation complex.
MeSH term(s)	Animals ; Autophagy/physiology ; Humans ; Protein Processing, Post-Translational ; Signal Transduction ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2017-01
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	194216-5
ISSN	1362-4326 ; 0968-0004 ; 0376-5067
ISSN (online)	1362-4326
ISSN	0968-0004 ; 0376-5067
DOI	10.1016/j.tibs.2016.09.008
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Article ; Online: The interplay between SARS-CoV-2 infected airway epithelium and immune cells modulates regulatory/inflammatory signals.

Bordoni, Veronica / Matusali, Giulia / Mariotti, Davide / Antonioli, Manuela / Cimini, Eleonora / Sacchi, Alessandra / Tartaglia, Eleonora / Casetti, Rita / Grassi, Germana / Notari, Stefania / Castilletti, Concetta / Fimia, Gian Maria / Capobianchi, Maria Rosaria / Ippolito, Giuseppe / Agrati, Chiara

iScience

2022 Volume 25, Issue 2, Page(s) 103854

Abstract: To assess the cross-talk between immune cells and respiratory tract during SARS-CoV-2 infection, we analyzed the relationships between the inflammatory response induced by SARS-CoV-2 replication and immune cells phenotype in a reconstituted organotypic ... ...

Abstract	To assess the cross-talk between immune cells and respiratory tract during SARS-CoV-2 infection, we analyzed the relationships between the inflammatory response induced by SARS-CoV-2 replication and immune cells phenotype in a reconstituted organotypic human airway epithelium (HAE). The results indicated that immune cells failed to inhibit SARS-CoV-2 replication in the HAE model. In contrast, immune cells strongly affected the inflammatory profile induced by SARS-CoV-2 infection, dampening the production of several immunoregulatory/inflammatory signals (e.g., IL-35, IL-27, and IL-34). Moreover, these mediators were found inversely correlated with innate immune cell frequency (NK and γδ T cells) and directly with CD8 T cells. The enriched signals associated with NK and CD8 T cells highlighted the modulation of pathways induced by SARS-CoV-2 infected HAE. These findings are useful to depict the cell-cell communication mechanisms necessary to develop novel therapeutic strategies aimed to promote an effective immune response.
Language	English
Publishing date	2022-01-31
Publishing country	United States
Document type	Journal Article
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2022.103854
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Article: Emerging Mechanisms in Initiating and Terminating Autophagy

Antonioli, Manuela / Gian Maria Fimia / Martina Di Rienzo / Mauro Piacentini

Trends in biochemical sciences. 2017 Jan., v. 42, no. 1

2017

Abstract	Autophagy is a major degradative process activated in a rapid and transient manner to cope with stress conditions. Whether autophagy is beneficial or detrimental depends upon the rate of induction and the appropriateness of the duration. Alterations in both autophagy initiation and termination predispose the cell to death, and affect the execution of other inducible processes such as inflammation. In this review we discuss how stress signaling pathways dynamically control the activity of the autophagy machinery by mediating post-translational modifications and regulatory protein interactions. In particular, we highlight the emerging role of TRIM and CULLIN families of ubiquitin ligases which play opposite roles in the autophagy response by promoting or inhibiting, respectively, the activity of the autophagy initiation complex.
Keywords	autophagy ; inflammation ; post-translational modification ; regulatory proteins ; signal transduction ; ubiquitin-protein ligase
Language	English
Dates of publication	2017-01
Size	p. 28-41.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	194220-7
ISSN	0968-0004 ; 0376-5067
ISSN	0968-0004 ; 0376-5067
DOI	10.1016/j.tibs.2016.09.008
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Article ; Online: AMBRA1-regulated autophagy in vertebrate development.

Antonioli, Manuela / Albiero, Federica / Fimia, Gian María / Piacentini, Mauro

The International journal of developmental biology

2015 Volume 59, Issue 1-3, Page(s) 109–117

Abstract: Autophagy is a catabolic process that mediates the lysosomal turn over of organelles and macromolecules, and is strongly activated in stress conditions to ensure cell survival. Autophagy core genes are highly conserved from yeast to mammals, with an ... ...

Abstract	Autophagy is a catabolic process that mediates the lysosomal turn over of organelles and macromolecules, and is strongly activated in stress conditions to ensure cell survival. Autophagy core genes are highly conserved from yeast to mammals, with an increasing number of positive and negative regulators that have evolved in higher eukaryotes. Autophagy takes part in different stages of development, as revealed by alterations in cell proliferation, differentiation and survival during the embryogenesis of organisms carrying mutations in autophagy genes. These defects are ascribed to the ability of autophagy to provide elements for new synthesis or energy production in limiting conditions during embryogenesis, as well as to contribute to the profound cell remodeling that occurs during differentiation. However, many differences have been observed in the phenotypes of autophagy mutant organisms, indicating that these genes have acquired specific functions in particular tissues, which may reflect the ability of autophagy to crosstalk with the main developmental processes. In this review, we discuss the role of upstream regulators of autophagy in the development of different model systems, focusing, in particular, on AMBRA1 (autophagy/beclin-1 regulator-1) and its role in the central nervous system.
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Apoptosis/physiology ; Apoptosis Regulatory Proteins/metabolism ; Autophagy/physiology ; Autophagy-Related Protein-1 Homolog ; Beclin-1 ; Central Nervous System/embryology ; Intracellular Signaling Peptides and Proteins/metabolism ; Membrane Proteins/metabolism ; Microtubule-Associated Proteins/metabolism ; Protein Serine-Threonine Kinases/metabolism ; Vertebrates/embryology
Chemical Substances	AMBRA1 protein, human ; Adaptor Proteins, Signal Transducing ; Apoptosis Regulatory Proteins ; BECN1 protein, human ; Beclin-1 ; Intracellular Signaling Peptides and Proteins ; MAP1LC3A protein, human ; Membrane Proteins ; Microtubule-Associated Proteins ; Autophagy-Related Protein-1 Homolog (EC 2.7.11.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; ULK1 protein, human (EC 2.7.11.1)
Language	English
Publishing date	2015-09-29
Publishing country	Spain
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1036070-0
ISSN	1696-3547 ; 0214-6282
ISSN (online)	1696-3547
ISSN	0214-6282
DOI	10.1387/ijdb.150057mp
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Article: Temporal regulation of autophagy response by the CULLIN 4-AMBRA1-CULLIN 5 axis.

Antonioli, Manuela / Albiero, Federica / Piacentini, Mauro / Fimia, Gian Maria

Molecular & cellular oncology

2015 Volume 3, Issue 5, Page(s) e1008304

Abstract: Autophagy controls cell homeostasis and provides a rapid response to a variety of stresses. Although many steps of the autophagy process have been elucidated, how they are temporally regulated is less well characterized. Recently, we reported that ... ...

Abstract	Autophagy controls cell homeostasis and provides a rapid response to a variety of stresses. Although many steps of the autophagy process have been elucidated, how they are temporally regulated is less well characterized. Recently, we reported that dynamic interaction of the pro-autophagic factor AMBRA1 with CULLIN E3 ubiquitin ligases ensures the timely onset and termination of the autophagy response.
Language	English
Publishing date	2015-02-03
Publishing country	United States
Document type	Journal Article
ISSN	2372-3556
ISSN	2372-3556
DOI	10.1080/23723556.2015.1008304
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Article: Proteomic analysis identifies a signature of disease severity in the plasma of COVID-19 pneumonia patients associated to neutrophil, platelet and complement activation.

Ciccosanti, Fabiola / Antonioli, Manuela / Sacchi, Alessandra / Notari, Stefania / Farina, Anna / Beccacece, Alessia / Fusto, Marisa / Vergori, Alessandra / D'Offizi, Gianpiero / Taglietti, Fabrizio / Antinori, Andrea / Nicastri, Emanuele / Marchioni, Luisa / Palmieri, Fabrizio / Ippolito, Giuseppe / Piacentini, Mauro / Agrati, Chiara / Fimia, Gian Maria

Clinical proteomics

2022 Volume 19, Issue 1, Page(s) 38

Abstract: Most patients infected with SARS-CoV-2 display mild symptoms with good prognosis, while 20% of patients suffer from severe viral pneumonia and up to 5% may require intensive care unit (ICU) admission due to severe acute respiratory syndrome, which could ... ...

Abstract	Most patients infected with SARS-CoV-2 display mild symptoms with good prognosis, while 20% of patients suffer from severe viral pneumonia and up to 5% may require intensive care unit (ICU) admission due to severe acute respiratory syndrome, which could be accompanied by multiorgan failure.Plasma proteomics provide valuable and unbiased information about disease progression and therapeutic candidates. Recent proteomic studies have identified molecular changes in plasma of COVID-19 patients that implied significant dysregulation of several aspects of the inflammatory response accompanied by a general metabolic suppression. However, which of these plasma alterations are associated with disease severity remains only partly characterized.A known limitation of proteomic studies of plasma samples is the large difference in the macromolecule abundance, with concentration spanning at least 10 orders of magnitude. To improve the coverage of plasma contents, we performed a deep proteomic analysis of plasma from 10 COVID-19 patients with severe/fatal pneumonia compared to 10 COVID-19 patients with pneumonia who did not require ICU admission (non-ICU). To this aim, plasma samples were first depleted of the most abundant proteins, trypsin digested and peptides subjected to a high pH reversed-phase peptide fractionation before LC-MS analysis.These results highlighted an increase of proteins involved in neutrophil and platelet activity and acute phase response, which is significantly higher in severe/fatal COVID-19 patients when compared to non-ICU ones. Importantly, these changes are associated with a selective induction of complement cascade factors in severe/fatal COVID-19 patients. Data are available via ProteomeXchange with identifier PXD036491. Among these alterations, we confirmed by ELISA that higher levels of the neutrophil granule proteins DEFA3 and LCN2 are present in COVID-19 patients requiring ICU admission when compared to non-ICU and healthy donors.Altogether, our study provided an in-depth view of plasma proteome changes that occur in COVID-19 patients in relation to disease severity, which can be helpful to identify therapeutic strategies to improve the disease outcome.
Language	English
Publishing date	2022-11-08
Publishing country	England
Document type	Journal Article
ZDB-ID	2205154-5
ISSN	1542-6416
ISSN	1542-6416
DOI	10.1186/s12014-022-09377-7
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Article ; Online: AMBRA1 phosphorylation by CDK1 and PLK1 regulates mitotic spindle orientation.

Cellular and molecular life sciences : CMLS

2023 Volume 80, Issue 9, Page(s) 251

Abstract: AMBRA1 is a crucial factor for nervous system development, and its function has been mainly associated with autophagy. It has been also linked to cell proliferation control, through its ability to regulate c-Myc and D-type cyclins protein levels, thus ... ...

Abstract	AMBRA1 is a crucial factor for nervous system development, and its function has been mainly associated with autophagy. It has been also linked to cell proliferation control, through its ability to regulate c-Myc and D-type cyclins protein levels, thus regulating G1-S transition. However, it remains still unknown whether AMBRA1 is differentially regulated during the cell cycle, and if this pro-autophagy protein exerts a direct role in controlling mitosis too. Here we show that AMBRA1 is phosphorylated during mitosis on multiple sites by CDK1 and PLK1, two mitotic kinases. Moreover, we demonstrate that AMBRA1 phosphorylation at mitosis is required for a proper spindle function and orientation, driven by NUMA1 protein. Indeed, we show that the localization and/or dynamics of NUMA1 are strictly dependent on AMBRA1 presence, phosphorylation and binding ability. Since spindle orientation is critical for tissue morphogenesis and differentiation, our findings could account for an additional role of AMBRA1 in development and cancer ontogenesis.
MeSH term(s)	Humans ; Phosphorylation ; Protein Serine-Threonine Kinases/genetics ; Protein Serine-Threonine Kinases/metabolism ; Spindle Apparatus/metabolism ; Cell Cycle Proteins/metabolism ; Mitosis ; Cell Cycle ; HeLa Cells ; CDC2 Protein Kinase/metabolism ; Adaptor Proteins, Signal Transducing/metabolism
Chemical Substances	Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Cell Cycle Proteins ; CDK1 protein, human (EC 2.7.11.22) ; CDC2 Protein Kinase (EC 2.7.11.22) ; AMBRA1 protein, human ; Adaptor Proteins, Signal Transducing
Language	English
Publishing date	2023-08-16
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-023-04878-6
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