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Article ; Online: Tryptophanyl-Transfer RNA Synthetase Is Involved in a Negative Feedback Loop Mitigating Interferon-γ-Induced Gene Expression.

Lazar, Ikrame / Livneh, Ido / Ciechanover, Aaron / Fabre, Bertrand

2024 Volume 13, Issue 2

Abstract: Aminoacyl-tRNA synthetases (aaRSs) are essential enzymes responsible for linking a transfer RNA (tRNA) with its cognate amino acid present in all the kingdoms of life. Besides their aminoacyl-tRNA synthetase activity, it was described that many of these ... ...

Abstract	Aminoacyl-tRNA synthetases (aaRSs) are essential enzymes responsible for linking a transfer RNA (tRNA) with its cognate amino acid present in all the kingdoms of life. Besides their aminoacyl-tRNA synthetase activity, it was described that many of these enzymes can carry out non-canonical functions. They were shown to be involved in important biological processes such as metabolism, immunity, development, angiogenesis and tumorigenesis. In the present work, we provide evidence that tryptophanyl-tRNA synthetase might be involved in a negative feedback loop mitigating the expression of certain interferon-γ-induced genes. Mining the available TCGA and Gtex data, we found that
MeSH term(s)	Humans ; Tryptophan-tRNA Ligase/genetics ; Interferon-gamma/pharmacology ; Feedback ; Melanoma/genetics ; Skin Neoplasms ; Amino Acyl-tRNA Synthetases ; RNA, Transfer ; Gene Expression ; Apolipoprotein L1
Chemical Substances	Tryptophan-tRNA Ligase (EC 6.1.1.2) ; Interferon-gamma (82115-62-6) ; Amino Acyl-tRNA Synthetases (EC 6.1.1.-) ; RNA, Transfer (9014-25-9) ; APOL1 protein, human ; Apolipoprotein L1
Language	English
Publishing date	2024-01-17
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells13020180
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Article ; Online: CALPA-IN NF1.

Lazar, Ikrame / Ronai, Ze'ev A

Oncotarget

2018 Volume 9, Issue 69, Page(s) 33051

Language	English
Publishing date	2018-09-04
Publishing country	United States
Document type	News ; Comment
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.25990
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Article ; Online: Regulation of nucleo-cytosolic 26S proteasome translocation by aromatic amino acids via mTOR is essential for cell survival under stress.

Livneh, Ido / Cohen-Kaplan, Victoria / Fabre, Bertrand / Abramovitch, Ifat / Lulu, Chen / Nataraj, Nishanth Belugali / Lazar, Ikrame / Ziv, Tamar / Yarden, Yosef / Zohar, Yaniv / Gottlieb, Eyal / Ciechanover, Aaron

Molecular cell

2023 Volume 83, Issue 18, Page(s) 3333–3346.e5

Abstract: The proteasome is responsible for removal of ubiquitinated proteins. Although several aspects of its regulation (e.g., assembly, composition, and post-translational modifications) have been unraveled, studying its adaptive compartmentalization in ... ...

Abstract	The proteasome is responsible for removal of ubiquitinated proteins. Although several aspects of its regulation (e.g., assembly, composition, and post-translational modifications) have been unraveled, studying its adaptive compartmentalization in response to stress is just starting to emerge. We found that following amino acid starvation, the proteasome is translocated from its large nuclear pool to the cytoplasm-a response regulated by newly identified mTOR-agonistic amino acids-Tyr, Trp, and Phe (YWF). YWF relay their signal upstream of mTOR through Sestrin3 by disrupting its interaction with the GATOR2 complex. The triad activates mTOR toward its downstream substrates p62 and transcription factor EB (TFEB), affecting both proteasomal and autophagic activities. Proteasome translocation stimulates cytosolic proteolysis which replenishes amino acids, thus enabling cell survival. In contrast, nuclear sequestration of the proteasome following mTOR activation by YWF inhibits this proteolytic adaptive mechanism, leading to cell death, which establishes this newly identified pathway as a key stress-coping mechanism.
MeSH term(s)	Proteasome Endopeptidase Complex ; Amino Acids, Aromatic ; Cell Survival ; Amino Acids ; TOR Serine-Threonine Kinases/genetics
Chemical Substances	ATP dependent 26S protease (EC 3.4.99.-) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Amino Acids, Aromatic ; Amino Acids ; TOR Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2023-09-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2023.08.016
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Article ; Online: Obesity and melanoma: could fat be fueling malignancy?

Clement, Emily / Lazar, Ikrame / Muller, Catherine / Nieto, Laurence

Pigment cell & melanoma research

2017 Volume 30, Issue 3, Page(s) 294–306

Abstract: Over the last decade, it has become increasingly clear that adipose tissue, and particularly adipocytes, contributes to tumor progression. Obesity, an ever-increasing worldwide phenomenon, exacerbates this effect. The influence of obesity on melanoma ... ...

Abstract	Over the last decade, it has become increasingly clear that adipose tissue, and particularly adipocytes, contributes to tumor progression. Obesity, an ever-increasing worldwide phenomenon, exacerbates this effect. The influence of obesity on melanoma remains poorly studied, although recent data do underline an association between the two diseases in both humans and murine models. Herein, we review the impact of obesity on melanoma incidence and progression and discuss the underlying mechanisms known to be involved. Adipose tissue favors the proliferation and aggressiveness of melanoma cells through a direct dialog, mediated by soluble factors and by exosomes, and through remodeling of the tumor microenvironment. This knowledge could, in the future, help to design new personalized therapeutic options for obese melanoma patients.
MeSH term(s)	Adipose Tissue/pathology ; Adiposity ; Animals ; Disease Progression ; Humans ; Melanoma/complications ; Melanoma/pathology ; Models, Biological ; Obesity/complications ; Obesity/pathology
Language	English
Publishing date	2017-04-20
Publishing country	England
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	2409570-9
ISSN	1755-148X ; 1600-0749 ; 0893-5785 ; 1755-1471
ISSN (online)	1755-148X ; 1600-0749
ISSN	0893-5785 ; 1755-1471
DOI	10.1111/pcmr.12584
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Article ; Online: A new role for extracellular vesicles: how small vesicles can feed tumors' big appetite.

Lazar, Ikrame / Clement, Emily / Attane, Camille / Muller, Catherine / Nieto, Laurence

Journal of lipid research

2018 Volume 59, Issue 10, Page(s) 1793–1804

Abstract: Cancer cells must adapt their metabolism in order to meet the energy requirements for cell proliferation, survival in nutrient-deprived environments, and dissemination. In particular, FA metabolism is emerging as a critical process for tumors. FA ... ...

Abstract	Cancer cells must adapt their metabolism in order to meet the energy requirements for cell proliferation, survival in nutrient-deprived environments, and dissemination. In particular, FA metabolism is emerging as a critical process for tumors. FA metabolism can be modulated through intrinsic changes in gene expression or signaling between tumor cells and also in response to signals from the surrounding microenvironment. Among these signals, extracellular vesicles (EVs) could play an important role in FA metabolism remodeling. In this review, we will present the role of EVs in tumor progression and especially in metabolic reprogramming. Particular attention will be granted to adipocytes. These cells, which are specialized in storing and releasing FAs, are able to shift tumor metabolism toward the use of FAs and, subsequently, increase tumor aggressiveness. Recent work demonstrates the involvement of EVs in this metabolic symbiosis.
MeSH term(s)	Adipocytes/metabolism ; Adipocytes/pathology ; Animals ; Carcinogenesis ; Disease Progression ; Extracellular Vesicles/metabolism ; Humans ; Neoplasms/metabolism ; Neoplasms/pathology
Language	English
Publishing date	2018-04-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	80154-9
ISSN	1539-7262 ; 0022-2275
ISSN (online)	1539-7262
ISSN	0022-2275
DOI	10.1194/jlr.R083725
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Article: Arginyl‐tRNA‐protein transferase 1 (ATE1) promotes melanoma cell growth and migration

Lazar, Ikrame / Fabre, Bertrand / Feng, Yongmei / Khateb, Ali / Frit, Philippe / Kashina, Anna / Zhang, Tongwu / Avitan‐Hersh, Emily / Kim, Hyungsoo / Brown, Kevin / Topisirovic, Ivan / Ronai, Ze’ev A.

FEBS letters. 2022 June, v. 596, no. 11

2022

Abstract: Arginyl‐tRNA‐protein transferase 1 (ATE1) catalyses N‐terminal protein arginylation, a post‐translational modification implicated in cell migration, invasion and the cellular stress response. Herein, we report that ATE1 is overexpressed in NRAS‐mutant ... ...

Abstract	Arginyl‐tRNA‐protein transferase 1 (ATE1) catalyses N‐terminal protein arginylation, a post‐translational modification implicated in cell migration, invasion and the cellular stress response. Herein, we report that ATE1 is overexpressed in NRAS‐mutant melanomas, while it is downregulated in BRAF‐mutant melanomas. ATE1 expression was higher in metastatic tumours, compared with primary tumours. Consistent with these findings, ATE1 depletion reduced melanoma cell viability, migration and colony formation. Reduced ATE1 expression also affected cell responses to mTOR and MEK inhibitors and to serum deprivation. Among putative ATE1 substrates is the tumour suppressor AXIN1, pointing to the possibility that ATE1 may fine‐tune AXIN1 function in melanoma. Our findings highlight an unexpected role for ATE1 in melanoma cell aggressiveness and suggest that ATE1 constitutes a potential new therapeutic target.
Keywords	blood serum ; cell growth ; cell movement ; cell viability ; melanoma ; metastasis ; post-translational modification ; stress response ; therapeutics
Language	English
Dates of publication	2022-06
Size	p. 1468-1480.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	JOURNAL ARTICLE
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1002/1873-3468.14376
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Article ; Online: Adipocyte Extracellular Vesicles Decrease p16

Lazar, Ikrame / Clement, Emily / Carrié, Lorry / Esteve, David / Dauvillier, Stéphanie / Moutahir, Mohamed / Dalle, Stéphane / Delmas, Véronique / Andrieu-Abadie, Nathalie / Larue, Lionel / Muller, Catherine / Nieto, Laurence

The Journal of investigative dermatology

2022 Volume 142, Issue 9, Page(s) 2488–2498.e8

Abstract: Obesity is a recognized factor for increased risk and poor prognosis of many cancers, including melanoma. In this study, using genetically engineered mouse models of melanoma ( ... ...

Abstract	Obesity is a recognized factor for increased risk and poor prognosis of many cancers, including melanoma. In this study, using genetically engineered mouse models of melanoma (Nras
MeSH term(s)	Adipocytes/metabolism ; Animals ; Cyclin-Dependent Kinase Inhibitor p16/genetics ; Extracellular Vesicles/metabolism ; Melanoma/genetics ; Melanoma/metabolism ; Mice ; Obesity/genetics ; Obesity/metabolism ; beta Catenin/metabolism
Chemical Substances	Cdkn2a protein, mouse ; Cyclin-Dependent Kinase Inhibitor p16 ; beta Catenin
Language	English
Publishing date	2022-02-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80136-7
ISSN	1523-1747 ; 0022-202X
ISSN (online)	1523-1747
ISSN	0022-202X
DOI	10.1016/j.jid.2022.01.026
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Article ; Online: Arginyl-tRNA-protein transferase 1 (ATE1) promotes melanoma cell growth and migration.

Lazar, Ikrame / Fabre, Bertrand / Feng, Yongmei / Khateb, Ali / Frit, Philippe / Kashina, Anna / Zhang, Tongwu / Avitan-Hersh, Emily / Kim, Hyungsoo / Brown, Kevin / Topisirovic, Ivan / Ronai, Ze'ev A

FEBS letters

2022 Volume 596, Issue 11, Page(s) 1468–1480

Abstract: Arginyl-tRNA-protein transferase 1 (ATE1) catalyses N-terminal protein arginylation, a post-translational modification implicated in cell migration, invasion and the cellular stress response. Herein, we report that ATE1 is overexpressed in NRAS-mutant ... ...

Abstract	Arginyl-tRNA-protein transferase 1 (ATE1) catalyses N-terminal protein arginylation, a post-translational modification implicated in cell migration, invasion and the cellular stress response. Herein, we report that ATE1 is overexpressed in NRAS-mutant melanomas, while it is downregulated in BRAF-mutant melanomas. ATE1 expression was higher in metastatic tumours, compared with primary tumours. Consistent with these findings, ATE1 depletion reduced melanoma cell viability, migration and colony formation. Reduced ATE1 expression also affected cell responses to mTOR and MEK inhibitors and to serum deprivation. Among putative ATE1 substrates is the tumour suppressor AXIN1, pointing to the possibility that ATE1 may fine-tune AXIN1 function in melanoma. Our findings highlight an unexpected role for ATE1 in melanoma cell aggressiveness and suggest that ATE1 constitutes a potential new therapeutic target.
MeSH term(s)	Aminoacyltransferases/genetics ; Aminoacyltransferases/metabolism ; Cell Movement ; Cell Proliferation ; Humans ; Melanoma/genetics ; Protein Processing, Post-Translational ; RNA, Transfer/metabolism
Chemical Substances	RNA, Transfer (9014-25-9) ; Aminoacyltransferases (EC 2.3.2.-)
Language	English
Publishing date	2022-05-20
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1002/1873-3468.14376
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Article ; Online: Comparison of Drosophila melanogaster Embryo and Adult Proteome by SWATH-MS Reveals Differential Regulation of Protein Synthesis, Degradation Machinery, and Metabolism Modules.

Fabre, Bertrand / Korona, Dagmara / Lees, Jonathan G / Lazar, Ikrame / Livneh, Ido / Brunet, Manon / Orengo, Christine A / Russell, Steven / Lilley, Kathryn S

Journal of proteome research

2019 Volume 18, Issue 6, Page(s) 2525–2534

Abstract: An important area of modern biology consists of understanding the relationship between genotype and phenotype. However, to understand this relationship it is essential to investigate one of the principal links between them: the proteome. With the ... ...

Abstract	An important area of modern biology consists of understanding the relationship between genotype and phenotype. However, to understand this relationship it is essential to investigate one of the principal links between them: the proteome. With the development of recent mass-spectrometry approaches, it is now possible to quantify entire proteomes and thus relate them to different phenotypes. Here, we present a comparison of the proteome of two extreme developmental states in the well-established model organism Drosophila melanogaster: adult and embryo. Protein modules such as ribosome, proteasome, tricarboxylic acid cycle, glycolysis, or oxidative phosphorylation were found differentially expressed between the two developmental stages. Analysis of post-translation modifications of the proteins identified in this study indicates that they generally follow the same trend as their corresponding protein. Comparison between changes in the proteome and the transcriptome highlighted patterns of post-transcriptional regulation for the subunits of protein complexes such as the ribosome and the proteasome, whereas protein from modules such as TCA cycle, glycolysis, and oxidative phosphorylation seem to be coregulated at the transcriptional level. Finally, the impact of the endosymbiont Wolbachia pipientis on the proteome of both developmental states was also investigated.
MeSH term(s)	Animals ; Drosophila melanogaster/genetics ; Drosophila melanogaster/growth & development ; Drosophila melanogaster/metabolism ; Drosophila melanogaster/microbiology ; Embryo, Nonmammalian/metabolism ; Embryo, Nonmammalian/microbiology ; Gene Expression Regulation, Developmental/genetics ; Protein Biosynthesis/genetics ; Proteolysis ; Proteome/genetics ; Proteome/metabolism ; Proteomics/methods ; Transcriptome/genetics ; Wolbachia/pathogenicity
Chemical Substances	Proteome
Language	English
Publishing date	2019-05-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2078618-9
ISSN	1535-3907 ; 1535-3893
ISSN (online)	1535-3907
ISSN	1535-3893
DOI	10.1021/acs.jproteome.9b00076
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Article: Comparison of Drosophila melanogaster Embryo and Adult Proteome by SWATH-MS Reveals Differential Regulation of Protein Synthesis, Degradation Machinery, and Metabolism Modules

Fabre, Bertrand / Korona, Dagmara / Lees, Jonathan G / Lazar, Ikrame / Livneh, Ido / Brunet, Manon / Orengo, Christine A / Russell, Steven / Lilley, Kathryn S

Journal of proteome research. 2019 May 14, v. 18, no. 6

2019

Abstract	An important area of modern biology consists of understanding the relationship between genotype and phenotype. However, to understand this relationship it is essential to investigate one of the principal links between them: the proteome. With the development of recent mass-spectrometry approaches, it is now possible to quantify entire proteomes and thus relate them to different phenotypes. Here, we present a comparison of the proteome of two extreme developmental states in the well-established model organism Drosophila melanogaster: adult and embryo. Protein modules such as ribosome, proteasome, tricarboxylic acid cycle, glycolysis, or oxidative phosphorylation were found differentially expressed between the two developmental stages. Analysis of post-translation modifications of the proteins identified in this study indicates that they generally follow the same trend as their corresponding protein. Comparison between changes in the proteome and the transcriptome highlighted patterns of post-transcriptional regulation for the subunits of protein complexes such as the ribosome and the proteasome, whereas protein from modules such as TCA cycle, glycolysis, and oxidative phosphorylation seem to be coregulated at the transcriptional level. Finally, the impact of the endosymbiont Wolbachia pipientis on the proteome of both developmental states was also investigated.
Keywords	Drosophila melanogaster ; Wolbachia pipientis ; adults ; endosymbionts ; gene expression regulation ; genotype ; glycolysis ; mass spectrometry ; models ; oxidative phosphorylation ; phenotype ; proteasome endopeptidase complex ; protein synthesis ; proteins ; proteome ; ribosomes ; transcription (genetics) ; transcriptome ; tricarboxylic acid cycle
Language	English
Dates of publication	2019-0514
Size	p. 2525-2534.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	2078618-9
ISSN	1535-3907 ; 1535-3893
ISSN (online)	1535-3907
ISSN	1535-3893
DOI	10.1021/acs.jproteome.9b00076
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