LIVIVO - Search results -

Search results

Result 1 - 10 of total 36

Search options

Article ; Online: BAG Family Members as Mitophagy Regulators in Mammals.

Pattingre, Sophie / Turtoi, Andrei

2022 Volume 11, Issue 4

Abstract: The BCL-2-associated athanogene (BAG) family is a multifunctional group of co-chaperones that are evolutionarily conserved from yeast to mammals. In addition to their common BAG domain, these proteins contain, in their sequences, many specific domains/ ... ...

Abstract	The BCL-2-associated athanogene (BAG) family is a multifunctional group of co-chaperones that are evolutionarily conserved from yeast to mammals. In addition to their common BAG domain, these proteins contain, in their sequences, many specific domains/motifs required for their various functions in cellular quality control, such as autophagy, apoptosis, and proteasomal degradation of misfolded proteins. The BAG family includes six members (BAG1 to BAG6). Recent studies reported their roles in autophagy and/or mitophagy through interaction with the autophagic machinery (LC3, Beclin 1, P62) or with the PINK1/Parkin signaling pathway. This review describes the mechanisms underlying BAG family member functions in autophagy and mitophagy and the consequences in physiopathology.
MeSH term(s)	Animals ; Autophagy ; Mammals/metabolism ; Mitophagy ; Molecular Chaperones/genetics ; Multigene Family ; Saccharomyces cerevisiae/metabolism
Chemical Substances	Molecular Chaperones
Language	English
Publishing date	2022-02-15
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells11040681
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Article: Remembering Beth Levine – the autophagy pioneer and woman extraordinaire

Sebti, Salwa / He, Congcong / Pattingre, Sophie / Meléndez, Alicia / Cuervo, Ana Maria / Hardwick, J. Marie / Griffin, Diane E

FEBS journal. 2020 Oct., v. 287, no. 20

2020

Abstract: Beth Levine was a remarkable scientist who launched the burgeoning field of autophagy. The biological process of autophagy was beginning to gain attention through new genetic studies in yeast when Beth Levine's transformative work on the genetics of ... ...

Abstract	Beth Levine was a remarkable scientist who launched the burgeoning field of autophagy. The biological process of autophagy was beginning to gain attention through new genetic studies in yeast when Beth Levine's transformative work on the genetics of autophagy in mammals made a major splash. Beth was also an extraordinary woman with an extraordinary persona. Here, several of her women trainees, colleagues, and mentors came together to share both sides of Beth Levine: the pioneer in science and the private person who exuded love of family and friends as intensely as her love of science.
Keywords	autophagy ; genetics ; scientists ; women ; yeasts
Language	English
Dates of publication	2020-10
Size	p. 4314-4321.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	NAL-AP-2-clean ; JOURNAL ARTICLE
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.15502
Database	NAL-Catalogue (AGRICOLA)

In stock of ZB MED Bonn / Germany

Z 2006/704: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: L’autophagie : le yin et le yang des cancers.

Joffre, Carine / Djavaheri-Mergny, Mojgan / Pattingre, Sophie / Giuriato, Sylvie

Medecine sciences : M/S

2017 Volume 33, Issue 3, Page(s) 328–334

Abstract: Autophagy is a self-cannibalism process essential for tissue homeostasis, which can be activated following different environmental stressful conditions. In normal cells, autophagy could act as a brake to prevent tumorigenesis, but cancer cells are able ... ...

Title translation	The yin and the yang of autophagy in cancer cells.
Abstract	Autophagy is a self-cannibalism process essential for tissue homeostasis, which can be activated following different environmental stressful conditions. In normal cells, autophagy could act as a brake to prevent tumorigenesis, but cancer cells are able to hijack this process to their own benefit, to promote tumor growth and/or tumor resistance to anti-cancer therapies. Scientists and clinicians attempt to modulate this process to improve therapies, using autophagy inhibitors or activators, some of them being tested currently in clinical trials against several types of tumors. Thus, it appears that autophagy is at the center of a showdown between cancer cells and anti-cancer therapies. In this review, we focus on the mechanisms by which autophagy could be either the yin or the yang of cancers.
MeSH term(s)	Animals ; Autophagy/physiology ; Cell Survival ; Cell Transformation, Neoplastic/pathology ; Humans ; Neoplasms/pathology
Language	French
Publishing date	2017-03
Publishing country	France
Document type	Journal Article ; Review
ZDB-ID	632733-3
ISSN	1958-5381 ; 0767-0974
ISSN (online)	1958-5381
ISSN	0767-0974
DOI	10.1051/medsci/20173303021
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.B 2872: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: HIV-1 Env induces pexophagy and an oxidative stress leading to uninfected CD4

Daussy, Coralie F / Galais, Mathilde / Pradel, Baptiste / Robert-Hebmann, Véronique / Sagnier, Sophie / Pattingre, Sophie / Biard-Piechaczyk, Martine / Espert, Lucile

Autophagy

2020 Volume 17, Issue 9, Page(s) 2465–2474

Abstract: The immunodeficiency observed in HIV-1-infected patients is mainly due to uninfected bystander ... ...

Abstract	The immunodeficiency observed in HIV-1-infected patients is mainly due to uninfected bystander CD4
MeSH term(s)	Autophagy ; CD4-Positive T-Lymphocytes ; Cell Death ; HIV-1 ; Humans ; Macroautophagy ; Oxidative Stress ; T-Lymphocytes
Language	English
Publishing date	2020-10-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2020.1831814
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 6741: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: BAG6 promotes PINK1 signaling pathway and is essential for mitophagy.

Ragimbeau, Romain / El Kebriti, Leila / Sebti, Salwa / Fourgous, Elise / Boulahtouf, Abdelhay / Arena, Giuseppe / Espert, Lucile / Turtoi, Andrei / Gongora, Céline / Houédé, Nadine / Pattingre, Sophie

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

2021 Volume 35, Issue 2, Page(s) e21361

Abstract: Bcl-2-associated athanogen-6 (BAG6) is a nucleocytoplasmic shuttling protein involved in protein quality control. We previously demonstrated that BAG6 is essential for autophagy by regulating the intracellular localization of the acetyltransferase EP300, ...

Abstract	Bcl-2-associated athanogen-6 (BAG6) is a nucleocytoplasmic shuttling protein involved in protein quality control. We previously demonstrated that BAG6 is essential for autophagy by regulating the intracellular localization of the acetyltransferase EP300, and thus, modifying accessibility to its substrates (TP53 in the nucleus and autophagy-related proteins in the cytoplasm). Here, we investigated BAG6 localization and function in the cytoplasm. First, we demonstrated that BAG6 is localized in the mitochondria. Specifically, BAG6 is expressed in the mitochondrial matrix under basal conditions, and translocates to the outer mitochondrial membrane after mitochondrial depolarization with carbonyl cyanide m-chlorophenyl hydrazine, a mitochondrial uncoupler that induces mitophagy. In SW480 cells, the deletion of BAG6 expression abrogates its ability to induce mitophagy and PINK1 accumulation. On the reverse, its ectopic expression in LoVo colon cancer cells, which do not express endogenous BAG6, reduces the size of the mitochondria, induces mitophagy, leads to the activation of the PINK1/PARKIN pathway and to the phospho-ubiquitination of mitochondrial proteins. Finally, BAG6 contains two LIR (LC3-interacting Region) domains specifically found in receptors for selective autophagy and responsible for the interaction with LC3 and for autophagosome selectivity. Site-directed mutagenesis showed that BAG6 requires wild-type LIRs domains for its ability to stimulate mitophagy. In conclusion, we propose that BAG6 is a novel mitophagy receptor or adaptor that induces PINK1/PARKIN signaling and mitophagy in a LIR-dependent manner.
MeSH term(s)	Binding Sites ; Cell Line, Tumor ; Humans ; Mitochondria/metabolism ; Mitophagy ; Molecular Chaperones/chemistry ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Protein Binding ; Protein Kinases/metabolism ; Signal Transduction ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	BAG6 protein, human ; Molecular Chaperones ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; parkin protein (EC 2.3.2.27) ; Protein Kinases (EC 2.7.-) ; PTEN-induced putative kinase (EC 2.7.11.1)
Language	English
Publishing date	2021-01-31
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	639186-2
ISSN	1530-6860 ; 0892-6638
ISSN (online)	1530-6860
ISSN	0892-6638
DOI	10.1096/fj.202000930R
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 2266: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 296: Show issues

Order via subito

Details ▾

Article: L'autophagie et le dernier soupir de la cellule.

Pattingre, Sophie / Codogno, Patrice

Medecine sciences : M/S

2007 Volume 23, Issue 8-9, Page(s) 696–698

Title translation	Autophagy and clearence of apoptotic cells.
MeSH term(s)	Apoptosis/physiology ; Autophagy/physiology ; Cell Aggregation ; Cell Differentiation ; Cell Physiological Phenomena ; Cells/cytology ; Humans ; Models, Biological
Language	French
Publishing date	2007-08
Publishing country	France
Document type	Journal Article
ZDB-ID	632733-3
ISSN	1958-5381 ; 0767-0974
ISSN (online)	1958-5381
ISSN	0767-0974
DOI	10.1051/medsci/20072389696
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.B 2872: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Bcl-2 inhibition of autophagy: a new route to cancer?

Pattingre, Sophie / Levine, Beth

Cancer research

2006 Volume 66, Issue 6, Page(s) 2885–2888

Abstract: Bcl-2 was the first identified cellular protein that functions as an oncogene by blocking apoptotic cell death. Beclin 1, the first identified mammalian autophagy gene product, is a haploinsufficient tumor suppressor that was originally isolated as a Bcl- ...

Abstract	Bcl-2 was the first identified cellular protein that functions as an oncogene by blocking apoptotic cell death. Beclin 1, the first identified mammalian autophagy gene product, is a haploinsufficient tumor suppressor that was originally isolated as a Bcl-2-interacting protein. We recently showed that Bcl-2 negatively regulates Beclin 1-dependent autophagy and Beclin 1-dependent autophagic cell death. These findings raise the possibility that Bcl-2 family members may function as oncogenes not only by blocking apoptosis but also by blocking autophagy.
MeSH term(s)	Animals ; Apoptosis Regulatory Proteins ; Autophagy/genetics ; Autophagy/physiology ; Beclin-1 ; Genes, bcl-2/physiology ; HeLa Cells ; Humans ; Membrane Proteins ; Neoplasms/genetics ; Neoplasms/pathology ; Oncogenes/physiology ; Proteins/antagonists & inhibitors ; Proteins/genetics ; Proteins/physiology ; Proto-Oncogene Proteins c-bcl-2/genetics ; Proto-Oncogene Proteins c-bcl-2/physiology
Chemical Substances	Apoptosis Regulatory Proteins ; BECN1 protein, human ; Beclin-1 ; Membrane Proteins ; Proteins ; Proto-Oncogene Proteins c-bcl-2
Language	English
Publishing date	2006-03-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1432-1
ISSN	1538-7445 ; 0008-5472
ISSN (online)	1538-7445
ISSN	0008-5472
DOI	10.1158/0008-5472.CAN-05-4412
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uh III Zs.135/5: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Ceramide-induced autophagy: to junk or to protect cells?

Pattingre, Sophie / Bauvy, Chantal / Levade, Thierry / Levine, Beth / Codogno, Patrice

Autophagy

2009 Volume 5, Issue 4, Page(s) 558–560

Abstract: Ceramide is a sphingolipid bioactive molecule that induces apoptosis and other forms of cell death, and triggers macroautophagy (referred to below as autophagy). Like amino acid starvation, ceramide triggers autophagy by interfering with the mTOR- ... ...

Abstract	Ceramide is a sphingolipid bioactive molecule that induces apoptosis and other forms of cell death, and triggers macroautophagy (referred to below as autophagy). Like amino acid starvation, ceramide triggers autophagy by interfering with the mTOR-signaling pathway, and by dissociating the Beclin 1:Bcl-2 complex in a c-Jun N-terminal kinase 1 (JNK1)-mediated Bcl-2 phosphorylation-dependent manner. Dissociation of the Beclin 1:Bcl-2 complex, and the subsequent stimulation of autophagy have been observed in various contexts in which the cellular level of long-chain ceramides was increased. It is notable that the conversion of short-chain ceramides (C(2)-ceramide and C(6)-ceramide) into long-chain ceramide via the activity of ceramide synthase is required to trigger autophagy. The dissociation of the Beclin 1:Bcl-2 complex has also been observed in response to tamoxifen and PDMP (an inhibitor of the enzyme that converts ceramide to glucosylceramide), drugs that increase the intracellular level of long-chain ceramides. However, and in contrast to starvation, overexpression of Bcl-2 does not blunt ceramide-induced autophagy. Whether this autophagy that is unchecked by forced dissociation of the Beclin 1:Bcl-2 complex is related to the ability of ceramide to trigger cell death remains an open question. More generally, the question of whether ceramide-induced autophagy is a dedicated cell death mechanism deserves closer scrutiny.
MeSH term(s)	Autophagy/drug effects ; Ceramides/pharmacology ; Cytoprotection/drug effects ; Humans ; Models, Biological
Chemical Substances	Ceramides
Language	English
Publishing date	2009-05-10
Publishing country	United States
Document type	Journal Article
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.4161/auto.5.4.8390
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 6741: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: Rôle des PI3 kinases dans le contrôle de l'autophagie.

Meley, Daniel / Pattingre, Sophie / Codogno, Patrice

Bulletin du cancer

2006 Volume 93, Issue 5, Page(s) 439–444

Abstract: Macroautophagy or autophagy is a degradative pathway terminating in the lysosomal compartment after the formation of a cytoplasmic vacuole that engulfs macromolecules and organelles. The recent discovery of the molecular controls of autophagy that are ... ...

Title translation	PI3 kinases and the control of autophagia.
Abstract	Macroautophagy or autophagy is a degradative pathway terminating in the lysosomal compartment after the formation of a cytoplasmic vacuole that engulfs macromolecules and organelles. The recent discovery of the molecular controls of autophagy that are common to eukaryotic cells from yeast to human suggests that the role of autophagy in cell functioning is far beyond its nonselective degradative capacity. The downregulation of autophagy observed in cancer cells is associated with tumor progression. The regulation of autophagy by signalling pathways overlaps with the control of cell growth, proliferation, cell survival and death. Two of these pathways play an important role in control of autophagy, the class I and III PI3K pathways. Several tumor suppressor genes (PTEN, TSC1 and 2, p53) involved in the class I PI3K mTOR signalling network have been shown to stimulate autophagy. In contrast, the oncoproteins involved in this network (Ras, class I PI3K and Akt) have the opposite effect. These findings, together with the discovery that Beclin 1, which forms a complex with the class III PI3K to initiate autophagy, is a tumor suppressor gene product give credibility of the idea that autophagy is a tumor suppressor mechanism. However, cancer cells sometimes mobilize autophagic capacities in response to various stimuli, suggesting that they can also exploit autophagy for their own benefit.
MeSH term(s)	Animals ; Autophagy/genetics ; Autophagy/physiology ; Enzyme Activation ; Genes, Tumor Suppressor ; Humans ; Neoplasms/enzymology ; Neoplasms/etiology ; Neoplasms/physiopathology ; PTEN Phosphohydrolase/physiology ; Phosphatidylinositol 3-Kinases/physiology ; Phosphotransferases (Phosphate Group Acceptor)/physiology ; Protein Kinases/physiology ; TOR Serine-Threonine Kinases
Chemical Substances	Protein Kinases (EC 2.7.-) ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; MTOR protein, human (EC 2.7.1.1) ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; AMP-dependent kinase (ATP-forming) (EC 2.7.4.-) ; Phosphotransferases (Phosphate Group Acceptor) (EC 2.7.4.-) ; PTEN Phosphohydrolase (EC 3.1.3.67)
Language	French
Publishing date	2006-05
Publishing country	France
Document type	English Abstract ; Journal Article ; Review
ZDB-ID	213270-9
ISSN	1769-6917 ; 0007-4551
ISSN (online)	1769-6917
ISSN	0007-4551
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uh III Zs.15: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Regulation of macroautophagy by mTOR and Beclin 1 complexes.

Pattingre, Sophie / Espert, Lucile / Biard-Piechaczyk, Martine / Codogno, Patrice

Biochimie

2008 Volume 90, Issue 2, Page(s) 313–323

Abstract: Macroautophagy or autophagy is a vacuolar degradative pathway terminating in the lysosomal compartment after forming a cytoplasmic vacuole or autophagosome that engulfs macromolecules and organelles. The original discovery that ATG (AuTophaGy related) ... ...

Abstract	Macroautophagy or autophagy is a vacuolar degradative pathway terminating in the lysosomal compartment after forming a cytoplasmic vacuole or autophagosome that engulfs macromolecules and organelles. The original discovery that ATG (AuTophaGy related) genes in yeast are involved in the formation of autophagosomes has greatly increased our knowledge of the molecular basis of autophagy, and its role in cell function that extends far beyond non-selective degradation. The regulation of autophagy by signaling pathways overlaps the control of cell growth, proliferation, cell survival and death. The evolutionarily conserved TOR (Target of Rapamycin) kinase complex 1 plays an important role upstream of the Atg1 complex in the control of autophagy by growth factors, nutrients, calcium signaling and in response to stress situations, including hypoxia, oxidative stress and low energy. The Beclin 1 (Atg6) complex, which is involved in the initial step of autophagosome formation, is directly targeted by signaling pathways. Taken together, these data suggest that multiple signaling checkpoints are involved in regulating autophagosome formation.
MeSH term(s)	Animals ; Apoptosis Regulatory Proteins ; Autophagy ; Beclin-1 ; Membrane Proteins/metabolism ; Protein Kinases/metabolism ; Proteins/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; TOR Serine-Threonine Kinases
Chemical Substances	Apoptosis Regulatory Proteins ; Beclin 1 protein, S cerevisiae ; Beclin-1 ; Becn1 protein, mouse ; Membrane Proteins ; Proteins ; Saccharomyces cerevisiae Proteins ; Protein Kinases (EC 2.7.-) ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; mTOR protein, mouse (EC 2.7.1.1)
Language	English
Publishing date	2008-02
Publishing country	France
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	120345-9
ISSN	0300-9084
ISSN	0300-9084
DOI	10.1016/j.biochi.2007.08.014
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.135: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

To top

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito