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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 ...

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
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Article ; Online: The Multifaceted Role of HSF1 in Pathophysiology: Focus on Its Interplay with TG2.

Occhigrossi, Luca / D'Eletto, Manuela / Barlev, Nickolai / Rossin, Federica

International journal of molecular sciences

2021 Volume 22, Issue 12

Abstract: The cellular environment needs to be strongly regulated and the maintenance of protein homeostasis is crucial for cell function and survival. HSF1 is the main regulator of the heat shock response (HSR), the master pathway required to maintain ... ...

Abstract	The cellular environment needs to be strongly regulated and the maintenance of protein homeostasis is crucial for cell function and survival. HSF1 is the main regulator of the heat shock response (HSR), the master pathway required to maintain proteostasis, as involved in the expression of the heat shock proteins (HSPs). HSF1 plays numerous physiological functions; however, the main role concerns the modulation of HSPs synthesis in response to stress. Alterations in HSF1 function impact protein homeostasis and are strongly linked to diseases, such as neurodegenerative disorders, metabolic diseases, and different types of cancers. In this context, type 2 Transglutaminase (TG2), a ubiquitous enzyme activated during stress condition has been shown to promote HSF1 activation. HSF1-TG2 axis regulates the HSR and its function is evolutionary conserved and implicated in pathological conditions. In this review, we discuss the role of HSF1 in the maintenance of proteostasis with regard to the HSF1-TG2 axis and we dissect the stress response pathways implicated in physiological and pathological conditions.
MeSH term(s)	Animals ; Embryonic Development ; GTP-Binding Proteins/metabolism ; Heat Shock Transcription Factors/metabolism ; Heat-Shock Response ; Humans ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/pathology ; Transglutaminases/metabolism
Chemical Substances	Heat Shock Transcription Factors ; transglutaminase 2 (EC 2.3.2.-) ; Transglutaminases (EC 2.3.2.13) ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	2021-06-14
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms22126366
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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 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
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Article ; Online: The Multifaceted Role of HSF1 in Pathophysiology

Luca Occhigrossi / Manuela D’Eletto / Nickolai Barlev / Federica Rossin

International Journal of Molecular Sciences, Vol 22, Iss 6366, p

Focus on Its Interplay with TG2

2021 Volume 6366

Abstract	The cellular environment needs to be strongly regulated and the maintenance of protein homeostasis is crucial for cell function and survival. HSF1 is the main regulator of the heat shock response (HSR), the master pathway required to maintain proteostasis, as involved in the expression of the heat shock proteins (HSPs). HSF1 plays numerous physiological functions; however, the main role concerns the modulation of HSPs synthesis in response to stress. Alterations in HSF1 function impact protein homeostasis and are strongly linked to diseases, such as neurodegenerative disorders, metabolic diseases, and different types of cancers. In this context, type 2 Transglutaminase (TG2), a ubiquitous enzyme activated during stress condition has been shown to promote HSF1 activation. HSF1-TG2 axis regulates the HSR and its function is evolutionary conserved and implicated in pathological conditions. In this review, we discuss the role of HSF1 in the maintenance of proteostasis with regard to the HSF1-TG2 axis and we dissect the stress response pathways implicated in physiological and pathological conditions.
Keywords	HSF1 ; heat shock proteins ; Transglutaminase 2 ; diseases ; development ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
Subject code	570
Language	English
Publishing date	2021-06-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
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Article ; Online: Cysteamine/Cystamine Exert Anti-

Palucci, Ivana / Salustri, Alessandro / De Maio, Flavio / Pereyra Boza, Maria Del Carmen / Paglione, Francesco / Sali, Michela / Occhigrossi, Luca / D'Eletto, Manuela / Rossin, Federica / Goletti, Delia / Sanguinetti, Maurizio / Piacentini, Mauro / Delogu, Giovanni

International journal of molecular sciences

2023 Volume 24, Issue 2

Abstract: Host-directed therapies are emerging as a promising tool in the curing of difficult-to-treat infections, such as those caused by drug-resistant bacteria. In this study, we aim to test the potential activity of the FDA- and EMA-approved drugs cysteamine ... ...

Abstract	Host-directed therapies are emerging as a promising tool in the curing of difficult-to-treat infections, such as those caused by drug-resistant bacteria. In this study, we aim to test the potential activity of the FDA- and EMA-approved drugs cysteamine and cystamine against
MeSH term(s)	Humans ; Amikacin/pharmacology ; Anti-Bacterial Agents/pharmacology ; Anti-Bacterial Agents/therapeutic use ; Cysteamine/pharmacology ; Cysteamine/therapeutic use ; Cystamine/pharmacology ; Cystamine/therapeutic use ; Mycobacterium abscessus ; Leukocytes, Mononuclear ; Mycobacterium Infections, Nontuberculous/drug therapy ; Mycobacterium Infections, Nontuberculous/microbiology ; Microbial Sensitivity Tests
Chemical Substances	Amikacin (84319SGC3C) ; Anti-Bacterial Agents ; Cysteamine (5UX2SD1KE2) ; Cystamine (R110LV8L02)
Language	English
Publishing date	2023-01-07
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/ijms24021203
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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: Transglutaminase Type 2-MITF axis regulates phenotype switching in skin cutaneous melanoma.

Muccioli, Silvia / Brillo, Valentina / Varanita, Tatiana / Rossin, Federica / Zaltron, Elisabetta / Velle, Angelo / Alessio, Giorgia / Angi, Beatrice / Severin, Filippo / Tosi, Anna / D'Eletto, Manuela / Occhigrossi, Luca / Falasca, Laura / Checchetto, Vanessa / Ciaccio, Roberto / Fascì, Amelia / Chieregato, Leonardo / Rebelo, Ana Paula / Giacomello, Marta /

Rosato, Antonio / Szabò, Ildikò / Romualdi, Chiara / Piacentini, Mauro / Leanza, Luigi

Cell death & disease

2023 Volume 14, Issue 10, Page(s) 704

Abstract: Skin cutaneous melanoma (SKCM) is the deadliest form of skin cancer due to its high heterogeneity that drives tumor aggressiveness. Melanoma plasticity consists of two distinct phenotypic states that co-exist in the tumor niche, the proliferative and the ...

Abstract	Skin cutaneous melanoma (SKCM) is the deadliest form of skin cancer due to its high heterogeneity that drives tumor aggressiveness. Melanoma plasticity consists of two distinct phenotypic states that co-exist in the tumor niche, the proliferative and the invasive, respectively associated with a high and low expression of MITF, the master regulator of melanocyte lineage. However, despite efforts, melanoma research is still far from exhaustively dissecting this phenomenon. Here, we discovered a key function of Transglutaminase Type-2 (TG2) in regulating melanogenesis by modulating MITF transcription factor expression and its transcriptional activity. Importantly, we demonstrated that TG2 expression affects melanoma invasiveness, highlighting its positive value in SKCM. These results suggest that TG2 may have implications in the regulation of the phenotype switching by promoting melanoma differentiation and impairing its metastatic potential. Our findings offer potential perspectives to unravel melanoma vulnerabilities via tuning intra-tumor heterogeneity.
MeSH term(s)	Humans ; Melanoma/pathology ; Skin Neoplasms/genetics ; Skin Neoplasms/metabolism ; Transglutaminases/genetics ; Transglutaminases/metabolism ; Gene Expression Regulation, Neoplastic ; Melanocytes/metabolism ; Phenotype ; Microphthalmia-Associated Transcription Factor/genetics ; Cell Line, Tumor ; Melanoma, Cutaneous Malignant
Chemical Substances	Transglutaminases (EC 2.3.2.13) ; Microphthalmia-Associated Transcription Factor ; MITF protein, human
Language	English
Publishing date	2023-10-28
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/s41419-023-06223-y
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Article ; Online: Transglutaminase Type 2 regulates the Wnt/β-catenin pathway in vertebrates.

Rossin, Federica / Costa, Roberto / Bordi, Matteo / D'Eletto, Manuela / Occhigrossi, Luca / Farrace, Maria Grazia / Barlev, Nickolai / Ciccosanti, Fabiola / Muccioli, Silvia / Chieregato, Leonardo / Szabo, Ildiko / Fimia, Gian Maria / Piacentini, Mauro / Leanza, Luigi

Cell death & disease

2021 Volume 12, Issue 3, Page(s) 249

Abstract: TG2 is a multifunctional enzyme involved in several cellular processes and has emerging as a potential regulator of gene expression. In this regard, we have recently shown that TG2 is able to activate HSF1, the master transcriptional regulator of the ... ...

Abstract	TG2 is a multifunctional enzyme involved in several cellular processes and has emerging as a potential regulator of gene expression. In this regard, we have recently shown that TG2 is able to activate HSF1, the master transcriptional regulator of the stress-responsive genes; however, its effect on the overall gene expression remains unclear. To address this point, we analyzed, by RNA-seq, the effect of TG2 on the overall transcriptome as well as we characterized the TG2 interactome in the nucleus. The data obtained from these omics approaches reveal that TG2 markedly influences the overall cellular transcriptome profile and specifically the Wnt and HSF1 pathways. In particular, its ablation leads to a drastic downregulation of many key members of these pathways. Interestingly, we found that key components of the Wnt/β-catenin pathway are also downregulated in cells lacking HSF1, thus confirming that TG2 regulates the HSF1 and this axis controls the Wnt signaling. Mechanistic studies revealed that TG2 can regulate the Wnt pathway by physically interacts with β-catenin and its nuclear interactome includes several proteins known to be involved in the regulation of the Wnt signaling. In order to verify whether this effect is playing a role in vivo, we ablated TG2 in Danio rerio. Our data show that the zebrafish lacking TG2 cannot complete the development and their death is associated with an evident downregulation of the Wnt pathway and a defective heat-shock response. Our findings show for the first time that TG2 is essential for the correct embryonal development of lower vertebrates, and its action is mediated by the Wnt/HSF1 axis.
MeSH term(s)	Animals ; Cells, Cultured ; Fibroblasts/enzymology ; GTP-Binding Proteins/genetics ; GTP-Binding Proteins/metabolism ; Gene Expression Regulation, Developmental ; Heat Shock Transcription Factors/genetics ; Heat Shock Transcription Factors/metabolism ; Heat-Shock Response ; Mice, Inbred C57BL ; Mice, Knockout ; Protein Glutamine gamma Glutamyltransferase 2 ; Transcription, Genetic ; Transcriptome ; Transglutaminases/genetics ; Transglutaminases/metabolism ; Wnt Proteins/genetics ; Wnt Proteins/metabolism ; Wnt Signaling Pathway ; Zebrafish/embryology ; Zebrafish/genetics ; Zebrafish/metabolism ; Zebrafish Proteins/genetics ; Zebrafish Proteins/metabolism ; beta Catenin/genetics ; beta Catenin/metabolism ; Mice
Chemical Substances	CTNNB1 protein, mouse ; Heat Shock Transcription Factors ; Hsf1 protein, mouse ; Wnt Proteins ; Zebrafish Proteins ; beta Catenin ; Protein Glutamine gamma Glutamyltransferase 2 (EC 2.3.2.13) ; Transglutaminases (EC 2.3.2.13) ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	2021-03-05
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/s41419-021-03485-2
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Article ; Online: Transglutaminase 2 Regulates Innate Immunity by Modulating the STING/TBK1/IRF3 Axis.

Occhigrossi, Luca / Rossin, Federica / D'Eletto, Manuela / Farrace, Maria Grazia / Ciccosanti, Fabiola / Petrone, Linda / Sacchi, Alessandra / Nardacci, Roberta / Falasca, Laura / Del Nonno, Franca / Palucci, Ivana / Smirnov, Evgeni / Barlev, Nick / Agrati, Chiara / Goletti, Delia / Delogu, Giovanni / Fimia, Gian Maria / Piacentini, Mauro

Journal of immunology (Baltimore, Md. : 1950)

2021 Volume 206, Issue 10, Page(s) 2420–2429

Abstract: We have recently shown that type 2 transglutaminase (TG2) plays a key role in the host's inflammatory response during bacterial infections. In this study, we investigated whether the enzyme is involved in the regulation of the STING pathway, which is the ...

Abstract	We have recently shown that type 2 transglutaminase (TG2) plays a key role in the host's inflammatory response during bacterial infections. In this study, we investigated whether the enzyme is involved in the regulation of the STING pathway, which is the main signaling activated in the presence of both self- and pathogen DNA in the cytoplasm, leading to type I IFN (IFN I) production. In this study, we demonstrated that TG2 negatively regulates STING signaling by impairing IRF3 phosphorylation in bone marrow-derived macrophages, isolated from wild-type and TG2 knockout mice. In the absence of TG2, we found an increase in the IFN-β production and in the downstream JAK/STAT pathway activation. Interestingly, proteomic analysis revealed that TG2 interacts with TBK1, affecting its interactome composition. Indeed, TG2 ablation facilitates the TBK1-IRF3 interaction, thus indicating that the enzyme plays a negative regulatory effect on IRF3 recruitment in the STING/TBK1 complex. In keeping with these findings, we observed an increase in the IFNβ production in bronchoalveolar lavage fluids from COVID-19-positive dead patients paralleled by a dramatic decrease of the TG2 expression in the lung pneumocytes. Taken together, these results suggest that TG2 plays a negative regulation on the IFN-β production associated with the innate immunity response to the cytosolic presence of both self- and pathogen DNA.
MeSH term(s)	Animals ; COVID-19/genetics ; COVID-19/immunology ; COVID-19/pathology ; GTP-Binding Proteins/genetics ; GTP-Binding Proteins/immunology ; Humans ; Immunity, Innate ; Interferon Regulatory Factor-3/genetics ; Interferon Regulatory Factor-3/immunology ; Interferon-beta/genetics ; Interferon-beta/immunology ; Membrane Proteins/genetics ; Membrane Proteins/immunology ; Mice ; Mice, Knockout ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/immunology ; SARS-CoV-2/immunology ; Signal Transduction/genetics ; Signal Transduction/immunology ; Transglutaminases/genetics ; Transglutaminases/immunology
Chemical Substances	Interferon Regulatory Factor-3 ; Irf3 protein, mouse ; Membrane Proteins ; Sting1 protein, mouse ; Interferon-beta (77238-31-4) ; transglutaminase 2 (EC 2.3.2.-) ; Transglutaminases (EC 2.3.2.13) ; Tbk1 protein, mouse (EC 2.7.1.-) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	2021-05-03
Publishing country	United States
Document type	Journal Article
ZDB-ID	3056-9
ISSN	1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
ISSN (online)	1550-6606
ISSN	0022-1767 ; 1048-3233 ; 1047-7381
DOI	10.4049/jimmunol.2001122
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Article ; Online: Transglutaminase Type 2 Regulates ER-Mitochondria Contact Sites by Interacting with GRP75.

D'Eletto, Manuela / Rossin, Federica / Occhigrossi, Luca / Farrace, Maria Grazia / Faccenda, Danilo / Desai, Radha / Marchi, Saverio / Refolo, Giulia / Falasca, Laura / Antonioli, Manuela / Ciccosanti, Fabiola / Fimia, Gian Maria / Pinton, Paolo / Campanella, Michelangelo / Piacentini, Mauro

Cell reports

2018 Volume 25, Issue 13, Page(s) 3573–3581.e4

Abstract: Transglutaminase type 2 (TG2) is a multifunctional enzyme that plays a key role in mitochondria homeostasis under stressful cellular conditions. TG2 interactome analysis reveals an enzyme interaction with GRP75 (glucose-regulated protein 75). GRP75 ... ...

Abstract	Transglutaminase type 2 (TG2) is a multifunctional enzyme that plays a key role in mitochondria homeostasis under stressful cellular conditions. TG2 interactome analysis reveals an enzyme interaction with GRP75 (glucose-regulated protein 75). GRP75 localizes in mitochondria-associated membranes (MAMs) and acts as a bridging molecule between the two organelles by assembling the IP3R-GRP75-VDAC complex, which is involved in the transport of Ca
MeSH term(s)	Animals ; Calcium/metabolism ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum/ultrastructure ; Fibroblasts/metabolism ; GTP-Binding Proteins/metabolism ; HEK293 Cells ; HSP70 Heat-Shock Proteins/metabolism ; Humans ; Inositol 1,4,5-Trisphosphate Receptors/metabolism ; Membrane Proteins/metabolism ; Mice, Inbred C57BL ; Mitochondria/metabolism ; Mitochondria/ultrastructure ; Mitochondrial Membranes/metabolism ; Mitochondrial Proteins/metabolism ; Protein Binding ; Transglutaminases/metabolism
Chemical Substances	HSP70 Heat-Shock Proteins ; Inositol 1,4,5-Trisphosphate Receptors ; Membrane Proteins ; Mitochondrial Proteins ; glucose-regulated proteins ; transglutaminase 2 (EC 2.3.2.-) ; Transglutaminases (EC 2.3.2.13) ; GTP-Binding Proteins (EC 3.6.1.-) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2018-12-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2018.11.094
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