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Article ; Online: Type 2 transglutaminase in the nucleus: the new epigenetic face of a cytoplasmic enzyme

Rossin, Federica / Ciccosanti, Fabiola / D'Eletto, Manuela / Occhigrossi, Luca / Fimia, Gian Maria / Piacentini, Mauro

Cell. Mol. Life Sci.. 2023 Feb., v. 80, no. 2 p.52-52

2023

Abstract: One of the major mysteries in science is how it is possible to pack the cellular chromatin with a total length of over 1 m, into a small sphere with a diameter of 5 mm "the nucleus", and even more difficult to envisage how to make it functional. Although ...

Abstract	One of the major mysteries in science is how it is possible to pack the cellular chromatin with a total length of over 1 m, into a small sphere with a diameter of 5 mm "the nucleus", and even more difficult to envisage how to make it functional. Although we know that compaction is achieved through the histones, however, the DNA needs to be accessible to the transcription machinery and this is allowed thanks to a variety of very complex epigenetic mechanisms. Either DNA (methylation) or post-translational modifications of histone proteins (acetylation, methylation, ubiquitination and sumoylation) play a crucial role in chromatin remodelling and consequently on gene expression. Recently the serotonylation and dopaminylation of the histone 3, catalyzed by the Transglutaminase type 2 (TG2), has been reported. These novel post-translational modifications catalyzed by a predominantly cytoplasmic enzyme opens a new avenue for future investigations on the enzyme function itself and for the possibility that other biological amines, substrate of TG2, can influence the genome regulation under peculiar cellular conditions. In this review we analyzed the nuclear TG2's biology by discussing both its post-translational modification of various transcription factors and the implications of its epigenetic new face. Finally, we will focus on the potential impact of these events in human diseases.
Keywords	DNA ; acetylation ; chromatin ; epigenetics ; gene expression ; genome ; histones ; humans ; methylation ; protein-glutamine gamma-glutamyltransferase ; sumoylation
Language	English
Dates of publication	2023-02
Size	p. 52.
Publishing place	Springer International Publishing
Document type	Article ; Online
Note	Review
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-023-04698-8
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Type 2 transglutaminase in the nucleus: the new epigenetic face of a cytoplasmic enzyme.

Rossin, Federica / Ciccosanti, Fabiola / D'Eletto, Manuela / Occhigrossi, Luca / Fimia, Gian Maria / Piacentini, Mauro

Cellular and molecular life sciences : CMLS

2023 Volume 80, Issue 2, Page(s) 52

Abstract	One of the major mysteries in science is how it is possible to pack the cellular chromatin with a total length of over 1 m, into a small sphere with a diameter of 5 mm "the nucleus", and even more difficult to envisage how to make it functional. Although we know that compaction is achieved through the histones, however, the DNA needs to be accessible to the transcription machinery and this is allowed thanks to a variety of very complex epigenetic mechanisms. Either DNA (methylation) or post-translational modifications of histone proteins (acetylation, methylation, ubiquitination and sumoylation) play a crucial role in chromatin remodelling and consequently on gene expression. Recently the serotonylation and dopaminylation of the histone 3, catalyzed by the Transglutaminase type 2 (TG2), has been reported. These novel post-translational modifications catalyzed by a predominantly cytoplasmic enzyme opens a new avenue for future investigations on the enzyme function itself and for the possibility that other biological amines, substrate of TG2, can influence the genome regulation under peculiar cellular conditions. In this review we analyzed the nuclear TG2's biology by discussing both its post-translational modification of various transcription factors and the implications of its epigenetic new face. Finally, we will focus on the potential impact of these events in human diseases.
MeSH term(s)	Humans ; Acetylation ; Chromatin ; DNA/genetics ; DNA Methylation ; Epigenesis, Genetic ; Histones/metabolism ; Protein Processing, Post-Translational ; Transglutaminases/genetics ; Transglutaminases/metabolism ; Cytoplasm/enzymology ; Cytoplasm/genetics ; Cytoplasm/metabolism ; Cell Nucleus/enzymology ; Cell Nucleus/genetics ; Cell Nucleus/metabolism ; Chromatin Assembly and Disassembly/genetics ; Chromatin Assembly and Disassembly/physiology
Chemical Substances	Chromatin ; DNA (9007-49-2) ; Histones ; Transglutaminases (EC 2.3.2.13) ; TGM2 protein, human
Language	English
Publishing date	2023-01-25
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-023-04698-8
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: A TRIM32-AMBRA1-ULK1 complex initiates the autophagy response in atrophic muscle cells.

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

Autophagy

2019 Volume 15, Issue 9, Page(s) 1674–1676

Abstract: The Ser/Thr protein kinase ULK1 is an upstream macroautophagy/autophagy regulator that is rapidly activated to ensure a proper adaptive response to stress conditions. Signaling pathways modulating ULK1 activity have been extensively characterized in ... ...

Abstract	The Ser/Thr protein kinase ULK1 is an upstream macroautophagy/autophagy regulator that is rapidly activated to ensure a proper adaptive response to stress conditions. Signaling pathways modulating ULK1 activity have been extensively characterized in response to nutrient/energy shortage, which mainly act by mediating ULK1 post-translational modifications, such as phosphorylation, acetylation and ubiquitination. Less characterized is how tissue-specific stress signals are able to activate ULK1 to induce autophagy. Our recent study has uncovered the E3 ubiquitin ligase TRIM32 as a novel ULK1 activator that regulates autophagy in muscle cells upon atrophy induction. TRIM32 is conveyed to ULK1 by the autophagy cofactor AMBRA1 to stimulate its kinase activity through unanchored K63-linked polyubiquitin chains. Notably, mutations in TRIM32 responsible for limb-girdle muscular dystrophy 2H disrupt its ability to bind ULK1 and to induce autophagy in muscle cells, resulting in a dysregulated activation of the atrophic process. In conclusion, we have identified a novel molecular mechanism by which autophagy is regulated in muscles, whose alteration is associated with the development of muscular dystrophy.
MeSH term(s)	Adaptor Proteins, Signal Transducing ; Atrophy ; Autophagy ; Autophagy-Related Protein-1 Homolog ; Humans ; Intracellular Signaling Peptides and Proteins ; Muscular Dystrophies, Limb-Girdle ; Transcription Factors ; Tripartite Motif Proteins ; Ubiquitin-Protein Ligases ; Ubiquitination
Chemical Substances	AMBRA1 protein, human ; Adaptor Proteins, Signal Transducing ; Intracellular Signaling Peptides and Proteins ; Transcription Factors ; Tripartite Motif Proteins ; TRIM32 protein, human (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Autophagy-Related Protein-1 Homolog (EC 2.7.11.1) ; ULK1 protein, human (EC 2.7.11.1)
Language	English
Publishing date	2019-06-28
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	10.1080/15548627.2019.1635385
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Article ; Online: Analysis of Secreted Proteins from Prepubertal Ovarian Tissues Exposed In Vitro to Cisplatin and LH.

Marcozzi, Serena / Ciccosanti, Fabiola / Fimia, Gian Maria / Piacentini, Mauro / Caggiano, Cinzia / Sette, Claudio / De Felici, Massimo / Klinger, Francesca Gioia

Cells

2022 Volume 11, Issue 7

Abstract: It is well known that secreted and exosomal proteins are associated with a broad range of physiological processes involving tissue homeostasis and differentiation. In the present paper, our purpose was to characterize the proteome of the culture medium ... ...

Abstract	It is well known that secreted and exosomal proteins are associated with a broad range of physiological processes involving tissue homeostasis and differentiation. In the present paper, our purpose was to characterize the proteome of the culture medium in which the oocytes within the primordial/primary follicles underwent apoptosis induced by cisplatin (CIS) or were, for the most part, protected by LH against the drug. To this aim, prepubertal ovarian tissues were cultured under control and in the presence of CIS, LH, and CIS + LH. The culture media were harvested after 2, 12, and 24 h from chemotherapeutic drug treatment and analyzed by liquid chromatography-mass spectrometry (LC-MS). We found that apoptotic conditions generated by CIS in the cultured ovarian tissues and/or oocytes are reflected in distinct changes in the extracellular microenvironment in which they were cultured. These changes became evident mainly from 12 h onwards and were characterized by the inhibition or decreased release of a variety of compounds, such as the proteases Htra1 and Prss23, the antioxidants Prdx2 and Hbat1, the metabolic regulators Ldha and Pkm, and regulators of apoptotic pathways such as Tmsb4x. Altogether, these results confirm the biological relevance of the LH action on prepuberal ovaries and provide novel information about the proteins released by the ovarian tissues exposed to CIS and LH in the surrounding microenvironment. These data might represent a valuable resource for future studies aimed to clarify the effects and identify biomarkers of these compounds' action on the developing ovary.
MeSH term(s)	Animals ; Apoptosis ; Cisplatin/metabolism ; Cisplatin/pharmacology ; Female ; Oocytes/metabolism ; Ovarian Follicle/metabolism ; Ovary/metabolism
Chemical Substances	Cisplatin (Q20Q21Q62J)
Language	English
Publishing date	2022-04-03
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells11071208
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Article: Mitochondrial Interactome: A Focus on Antiviral Signaling Pathways.

Refolo, Giulia / Vescovo, Tiziana / Piacentini, Mauro / Fimia, Gian Maria / Ciccosanti, Fabiola

Frontiers in cell and developmental biology

2020 Volume 8, Page(s) 8

Abstract: In the last years, proteomics has represented a valuable approach to elucidate key aspects in the regulation of type I/III interferons (IFNs) and autophagy, two main processes involved in the response to viral infection, to unveil the molecular ... ...

Abstract	In the last years, proteomics has represented a valuable approach to elucidate key aspects in the regulation of type I/III interferons (IFNs) and autophagy, two main processes involved in the response to viral infection, to unveil the molecular strategies that viruses have evolved to counteract these processes. Besides their main metabolic roles, mitochondria are well recognized as pivotal organelles in controlling signaling pathways essential to restrain viral infections. In particular, a major role in antiviral defense is played by mitochondrial antiviral signaling (MAVS) protein, an adaptor protein that coordinates the activation of IFN inducing pathways and autophagy at the mitochondrial level. Here, we provide an overview of how mass spectrometry-based studies of protein-protein interactions and post-translational modifications (PTMs) have fostered our understanding of the molecular mechanisms that control the mitochondria-mediated antiviral immunity.
Language	English
Publishing date	2020-02-14
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2737824-X
ISSN	2296-634X
ISSN	2296-634X
DOI	10.3389/fcell.2020.00008
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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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Article ; Online: The STING/TBK1/IRF3/IFN type I pathway is defective in cystic fibrosis.

Occhigrossi, Luca / Rossin, Federica / Villella, Valeria Rachela / Esposito, Speranza / Abbate, Carlo / D'Eletto, Manuela / Farrace, Maria Grazia / Tosco, Antonella / Nardacci, Roberta / Fimia, Gian Maria / Raia, Valeria / Piacentini, Mauro

Frontiers in immunology

2023 Volume 14, Page(s) 1093212

Abstract: Cystic fibrosis (CF) is a rare autosomal recessive disease caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) gene. The most common mutation is F508del-CFTR (ΔF) which leads the encoded ion channel towards misfolding ... ...

Abstract	Cystic fibrosis (CF) is a rare autosomal recessive disease caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) gene. The most common mutation is F508del-CFTR (ΔF) which leads the encoded ion channel towards misfolding and premature degradation. The disease is characterized by chronic bronchopulmonary obstruction, inflammation and airways colonization by bacteria, which are the major cause of morbidity and mortality. The STING pathway is the main signaling route activated in the presence of both self and pathogen DNA, leading to Type I Interferon (IFN I) production and the innate immune response. In this study, we show for the first time the relationship existing in CF between resistant and recurrent opportunistic infections by
MeSH term(s)	Mice ; Animals ; Cystic Fibrosis/microbiology ; Cystic Fibrosis Transmembrane Conductance Regulator ; Immunity, Innate/genetics ; Interferon Type I/metabolism ; Macrophages ; Protein Serine-Threonine Kinases/metabolism ; Interferon Regulatory Factor-3/genetics ; Interferon Regulatory Factor-3/metabolism
Chemical Substances	Cystic Fibrosis Transmembrane Conductance Regulator (126880-72-6) ; Interferon Type I ; Tbk1 protein, mouse (EC 2.7.1.-) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Irf3 protein, mouse ; Interferon Regulatory Factor-3
Language	English
Publishing date	2023-02-27
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2023.1093212
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Article ; Online: The ubiquitin ligase TRIM32 promotes the autophagic response to Mycobacterium tuberculosis infection in macrophages.

Romagnoli, Alessandra / Di Rienzo, Martina / Petruccioli, Elisa / Fusco, Carmela / Palucci, Ivana / Micale, Lucia / Mazza, Tommaso / Delogu, Giovanni / Merla, Giuseppe / Goletti, Delia / Piacentini, Mauro / Fimia, Gian Maria

Cell death & disease

2023 Volume 14, Issue 8, Page(s) 505

Abstract: Mycobacterium tuberculosis (Mtb) is known to evade host immune responses and persist in macrophages for long periods. A mechanism that the host uses to combat Mtb is xenophagy, a selective form of autophagy that targets intracellular pathogens for ... ...

Abstract	Mycobacterium tuberculosis (Mtb) is known to evade host immune responses and persist in macrophages for long periods. A mechanism that the host uses to combat Mtb is xenophagy, a selective form of autophagy that targets intracellular pathogens for degradation. Ubiquitination of Mtb or Mtb-containing compartments is a key event to recruit the autophagy machinery and mediate the bacterial delivery to the lysosome. This event relies on the coordinated and complementary activity of different ubiquitin ligases, including PARKIN, SMURF1, and TRIM16. Because each of these factors is responsible for the ubiquitination of a subset of the Mtb population, it is likely that additional ubiquitin ligases are employed by macrophages to trigger a full xenophagic response during Mtb infection. In this study, we investigated the role TRIM proteins whose expression is modulated in response to Mtb or BCG infection of primary macrophages. These TRIMs were ectopically expressed in THP1 macrophage cell line to assess their impact on Mtb replication. This screening identified TRIM32 as a novel player involved in the intracellular response to Mtb infection, which promotes autophagy-mediated Mtb degradation. The role of TRIM32 in xenophagy was further confirmed by silencing TRIM32 expression in THP1 cells, which causes increased intracellular growth of Mtb associated to impaired Mtb ubiquitination, reduced recruitment of the autophagy proteins NDP52/CALCOCO2 and BECLIN 1/BECN1 to Mtb and autophagosome formation. Overall, these findings suggest that TRIM32 plays an important role in the host response to Mtb infection through the induction of autophagy, representing a promising target for host-directed tuberculosis therapies.
MeSH term(s)	Humans ; Ubiquitin/metabolism ; Macrophages/metabolism ; Tuberculosis/genetics ; Autophagy/physiology ; Mycobacterium tuberculosis ; Tripartite Motif Proteins/genetics ; Tripartite Motif Proteins/metabolism ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; Transcription Factors/metabolism
Chemical Substances	Ubiquitin ; TRIM16 protein, human (EC 2.3.2.27) ; Tripartite Motif Proteins ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; TRIM32 protein, human (EC 2.3.2.27) ; Transcription Factors ; SMURF1 protein, human (EC 2.3.2.26)
Language	English
Publishing date	2023-08-05
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/s41419-023-06026-1
Database	MEDical Literature Analysis and Retrieval System OnLINE

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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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