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Article ; Online: La protéine VAP-A - fil conducteur de la communication entre organelles.

Subra, Mélody / Mesmin, Bruno

2023 Volume 39, Issue 6-7, Page(s) 504–506

Title translation	VAP-A: A thread to weave communication between organelles.
MeSH term(s)	Humans ; Communication ; Software ; Organelles
Language	French
Publishing date	2023-06-30
Publishing country	France
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	632733-3
ISSN	1958-5381 ; 0767-0974
ISSN (online)	1958-5381
ISSN	0767-0974
DOI	10.1051/medsci/2023085
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Article ; Online: New insights into the OSBP‒VAP cycle.

Subra, Mélody / Antonny, Bruno / Mesmin, Bruno

Current opinion in cell biology

2023 Volume 82, Page(s) 102172

Abstract: VAP-A is a major endoplasmic reticulum (ER) receptor that allows this organelle to engage numerous membrane contact sites with other organelles. One highly studied example is the formation of contact sites through VAP-A interaction with Oxysterol-binding ...

Abstract	VAP-A is a major endoplasmic reticulum (ER) receptor that allows this organelle to engage numerous membrane contact sites with other organelles. One highly studied example is the formation of contact sites through VAP-A interaction with Oxysterol-binding protein (OSBP). This lipid transfer protein transports cholesterol from the ER to the trans-Golgi network owing to the counter-exchange of the phosphoinositide PI(4)P. In this review, we highlight recent studies that advance our understanding of the OSBP cycle and extend the model of lipid exchange to other cellular contexts and other physiological and pathological conditions.
MeSH term(s)	trans-Golgi Network/metabolism ; Cholesterol/metabolism ; Biological Transport ; Endoplasmic Reticulum/metabolism ; Receptors, Steroid/metabolism
Chemical Substances	Cholesterol (97C5T2UQ7J) ; Receptors, Steroid
Language	English
Publishing date	2023-05-26
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1026381-0
ISSN	1879-0410 ; 0955-0674
ISSN (online)	1879-0410
ISSN	0955-0674
DOI	10.1016/j.ceb.2023.102172
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Article ; Online: Stranger Twins

Subra, Mélody / Grimanelli, Zoé / Gautier, Romain / Mesmin, Bruno

Contact (Thousand Oaks (Ventura County, Calif.))

2023 Volume 6, Page(s) 25152564231183897

Abstract: When considering the vesicle-associated membrane protein-associated protein (VAP) family, major receptors at the surface of the endoplasmic reticulum (ER), it appears that VAP-A and VAP-B paralogs largely overlap in structure and function, and that ... ...

Abstract	When considering the vesicle-associated membrane protein-associated protein (VAP) family, major receptors at the surface of the endoplasmic reticulum (ER), it appears that VAP-A and VAP-B paralogs largely overlap in structure and function, and that specific features to distinguish these two proteins hardly exist or are poorly documented. Here, we question the degree of redundancy between VAP-A and VAP-B: is one simply a backup plan, in case of loss of function of one of the two genes, or are there molecular and functional divergences that would explain their maintenance during evolution?
Language	English
Publishing date	2023-07-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	2964312-0
ISSN	2515-2564 ; 2515-2564
ISSN (online)	2515-2564
ISSN	2515-2564
DOI	10.1177/25152564231183897
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Article ; Online: Mitochondrial lipid transport and biosynthesis: A complex balance.

Mesmin, Bruno

The Journal of cell biology

2016 Volume 214, Issue 1, Page(s) 9–11

Abstract: Little is known about how mitochondrial lipids reach inner membrane-localized metabolic enzymes for phosphatidylethanolamine synthesis. Aaltonen et al. (2016. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201602007) and Miyata et al. (2016. J. Cell Biol. ... ...

Abstract	Little is known about how mitochondrial lipids reach inner membrane-localized metabolic enzymes for phosphatidylethanolamine synthesis. Aaltonen et al. (2016. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201602007) and Miyata et al. (2016. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201601082) now report roles for two mitochondrial complexes, Ups2-Mdm35 and mitochondrial contact site and cristae organizing system, in the biosynthesis and transport of mitochondrial lipids.
MeSH term(s)	Animals ; Biological Transport ; Humans ; Lipid Metabolism ; Lipids/biosynthesis ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism ; Models, Biological ; Saccharomyces cerevisiae/metabolism
Chemical Substances	Lipids
Language	English
Publishing date	2016-07-04
Publishing country	United States
Document type	Journal Article
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.201606069
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Article ; Online: [No title information]

Mélody Subra / Zoé Grimanelli / Romain Gautier / Bruno Mesmin

Contact, Vol

A Tale of Resemblance and Contrast Between VAP Proteins

2023 Volume 6

Abstract	When considering the vesicle-associated membrane protein-associated protein (VAP) family, major receptors at the surface of the endoplasmic reticulum (ER), it appears that VAP-A and VAP-B paralogs largely overlap in structure and function, and that specific features to distinguish these two proteins hardly exist or are poorly documented. Here, we question the degree of redundancy between VAP-A and VAP-B: is one simply a backup plan, in case of loss of function of one of the two genes, or are there molecular and functional divergences that would explain their maintenance during evolution?
Keywords	Biology (General) ; QH301-705.5 ; Biochemistry ; QD415-436
Language	English
Publishing date	2023-07-01T00:00:00Z
Publisher	SAGE Publishing
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Un marché d’échange de lipides - Transport vectoriel du cholestérol par la protéine OSBP.

Bigay, Joëlle / Mesmin, Bruno / Antonny, Bruno

Medecine sciences : M/S

2020 Volume 36, Issue 2, Page(s) 130–136

Abstract: Cholesterol is synthesized in the endoplasmic reticulum (RE) and then transported to cellular compartments whose functions require high cholesterol levels. Here, we describe the mechanism by which cholesterol is transported from the RE to the trans-Golgi ...

Title translation	A lipid exchange market : vectorial cholesterol transport by the protein OSBP.
Abstract	Cholesterol is synthesized in the endoplasmic reticulum (RE) and then transported to cellular compartments whose functions require high cholesterol levels. Here, we describe the mechanism by which cholesterol is transported from the RE to the trans-Golgi network (TGN) by the protein OSBP (Oxysterol-Binding Protein). OSBP has two complementary activities. First, it tethers the RE to the TGN by forming a contact site where the two membranes are about twenty nanometers away. Then, it exchanges RE cholesterol for a TGN lipid, phosphatidylinositol 4-phosphate (PI4P). Eventually, PI4P is hydrolyzed at the RE, making the exchange cycle irreversible. Thus, OSBP is at the center of a lipid exchange market where a transported cholesterol "costs" a PI4P. Antiviral or anti-cancer molecules target OSBP, suggesting the importance of the OSBP cycle in different physiopathological contexts. The general principles of this cycle are shared by other lipid-transfer proteins.
MeSH term(s)	Animals ; Biological Transport ; Cholesterol/metabolism ; Endoplasmic Reticulum/metabolism ; Humans ; Lipid Metabolism/physiology ; Phosphatidylinositol Phosphates/metabolism ; Receptors, Steroid/metabolism ; Receptors, Steroid/physiology
Chemical Substances	Phosphatidylinositol Phosphates ; Receptors, Steroid ; oxysterol binding protein ; phosphatidylinositol 4-phosphate ; Cholesterol (97C5T2UQ7J)
Language	French
Publishing date	2020-03-04
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/2020009
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Article ; Online: Lipid exchange at ER-trans-Golgi contact sites governs polarized cargo sorting.

Kovács, Dávid / Gay, Anne-Sophie / Debayle, Delphine / Abélanet, Sophie / Patel, Amanda / Mesmin, Bruno / Luton, Frédéric / Antonny, Bruno

The Journal of cell biology

2023 Volume 223, Issue 1

Abstract: Oxysterol binding protein (OSBP) extracts cholesterol from the ER to deliver it to the TGN via counter exchange and subsequent hydrolysis of the phosphoinositide PI(4)P. Here, we show that this pathway is essential in polarized epithelial cells where it ... ...

Abstract	Oxysterol binding protein (OSBP) extracts cholesterol from the ER to deliver it to the TGN via counter exchange and subsequent hydrolysis of the phosphoinositide PI(4)P. Here, we show that this pathway is essential in polarized epithelial cells where it contributes not only to the proper subcellular distribution of cholesterol but also to the trans-Golgi sorting and trafficking of numerous plasma membrane cargo proteins with apical or basolateral localization. Reducing the expression of OSBP, blocking its activity, or inhibiting a PI4Kinase that fuels OSBP with PI(4)P abolishes the epithelial phenotype. Waves of cargo enrichment in the TGN in phase with OSBP and PI(4)P dynamics suggest that OSBP promotes the formation of lipid gradients along the TGN, which helps cargo sorting. During their transient passage through the trans-Golgi, polarized plasma membrane proteins get close to OSBP but fail to be sorted when OSBP is silenced. Thus, OSBP lipid exchange activity is decisive for polarized cargo sorting and distribution in epithelial cells.
MeSH term(s)	Cell Movement ; Cholesterol/metabolism ; Epithelial Cells/metabolism ; Golgi Apparatus/metabolism ; Membrane Proteins/metabolism ; Phosphatidylinositols/metabolism ; Humans ; Animals ; Dogs ; A549 Cells ; Madin Darby Canine Kidney Cells ; Endoplasmic Reticulum/metabolism ; Receptors, Steroid/metabolism
Chemical Substances	Cholesterol (97C5T2UQ7J) ; Membrane Proteins ; Phosphatidylinositols ; oxysterol binding protein ; Receptors, Steroid
Language	English
Publishing date	2023-11-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202307051
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Article: The counterflow transport of sterols and PI4P.

Mesmin, Bruno / Antonny, Bruno

Biochimica et biophysica acta

2016 Volume 1861, Issue 8 Pt B, Page(s) 940–951

Abstract: Cholesterol levels in intracellular membranes are constantly adjusted to match with specific organelle functions. Cholesterol is kept high in the plasma membrane (PM) because it is essential for its barrier function, while low levels are found in the ... ...

Abstract	Cholesterol levels in intracellular membranes are constantly adjusted to match with specific organelle functions. Cholesterol is kept high in the plasma membrane (PM) because it is essential for its barrier function, while low levels are found in the endoplasmic reticulum (ER) where cholesterol mediates feedback control of its own synthesis by sterol-sensor proteins. The ER→Golgi→PM concentration gradient of cholesterol in mammalian cells, and ergosterol in yeast, appears to be sustained by specific intracellular transport processes, which are mostly mediated by lipid transfer proteins (LTPs). Here we review a recently described function of two LTPs, OSBP and its yeast homolog Osh4p, which consists in creating a sterol gradient between membranes by vectorial transport. OSBP also contributes to the formation of ER/Golgi membrane contact sites, which are important hubs for the transfer of several lipid species. OSBP and Osh4p organize a counterflow transport of lipids whereby sterols are exchanged for the phosphoinositide PI4P, which is used as a fuel to drive sterol transport. This article is part of a Special Issue entitled: The cellular lipid landscape edited by Tim P. Levine and Anant K. Menon.
MeSH term(s)	Animals ; Biological Transport, Active ; Carrier Proteins/metabolism ; Cholesterol/metabolism ; Endoplasmic Reticulum/metabolism ; Golgi Apparatus/metabolism ; Humans ; Intracellular Membranes/metabolism ; Membrane Proteins/metabolism ; Phosphatidylinositol Phosphates/metabolism ; Receptors, Steroid/metabolism ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	Carrier Proteins ; KES1 protein, S cerevisiae ; Membrane Proteins ; Phosphatidylinositol Phosphates ; Receptors, Steroid ; Saccharomyces cerevisiae Proteins ; lipid transfer protein ; oxysterol binding protein ; phosphatidylinositol 4-phosphate ; Cholesterol (97C5T2UQ7J)
Language	English
Publishing date	2016-08
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbalip.2016.02.024
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Article ; Online: The Oxysterol-Binding Protein Cycle: Burning Off PI(4)P to Transport Cholesterol.

Antonny, Bruno / Bigay, Joëlle / Mesmin, Bruno

Annual review of biochemistry

2018 Volume 87, Page(s) 809–837

Abstract: To maintain an asymmetric distribution of ions across membranes, protein pumps displace ions against their concentration gradient by using chemical energy. Here, we describe a functionally analogous but topologically opposite process that applies to the ... ...

Abstract	To maintain an asymmetric distribution of ions across membranes, protein pumps displace ions against their concentration gradient by using chemical energy. Here, we describe a functionally analogous but topologically opposite process that applies to the lipid transfer protein (LTP) oxysterol-binding protein (OSBP). This multidomain protein exchanges cholesterol for the phosphoinositide phosphatidylinositol 4-phosphate [PI(4)P] between two apposed membranes. Because of the subsequent hydrolysis of PI(4)P, this counterexchange is irreversible and contributes to the establishment of a cholesterol gradient along organelles of the secretory pathway. The facts that some natural anti-cancer molecules block OSBP and that many viruses hijack the OSBP cycle for the formation of intracellular replication organelles highlight the importance and potency of OSBP-mediated lipid exchange. The architecture of some LTPs is similar to that of OSBP, suggesting that the principles of the OSBP cycle-burning PI(4)P for the vectorial transfer of another lipid-might be general.
MeSH term(s)	Biological Transport, Active ; Carrier Proteins/metabolism ; Cholesterol/metabolism ; Golgi Apparatus/metabolism ; Humans ; Ligands ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism ; Models, Biological ; Models, Molecular ; Oxysterols/metabolism ; Phosphatidylinositol Phosphates/metabolism ; Protein Interaction Domains and Motifs ; Receptors, Steroid/chemistry ; Receptors, Steroid/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/metabolism ; Virus Replication/physiology
Chemical Substances	Carrier Proteins ; KES1 protein, S cerevisiae ; Ligands ; Membrane Proteins ; Oxysterols ; Phosphatidylinositol Phosphates ; Receptors, Steroid ; Saccharomyces cerevisiae Proteins ; lipid transfer protein ; oxysterol binding protein ; phosphatidylinositol 4-phosphate ; Cholesterol (97C5T2UQ7J)
Language	English
Publishing date	2018-03-29
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	207924-0
ISSN	1545-4509 ; 0066-4154
ISSN (online)	1545-4509
ISSN	0066-4154
DOI	10.1146/annurev-biochem-061516-044924
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Article: The counterflow transport of sterols and PI4P

Mesmin, Bruno / Bruno Antonny

Biochimica et biophysica acta. 2016 Aug., v. 1861, no. 8

2016

Abstract	Cholesterol levels in intracellular membranes are constantly adjusted to match with specific organelle functions. Cholesterol is kept high in the plasma membrane (PM) because it is essential for its barrier function, while low levels are found in the endoplasmic reticulum (ER) where cholesterol mediates feedback control of its own synthesis by sterol-sensor proteins. The ER→Golgi→PM concentration gradient of cholesterol in mammalian cells, and ergosterol in yeast, appears to be sustained by specific intracellular transport processes, which are mostly mediated by lipid transfer proteins (LTPs). Here we review a recently described function of two LTPs, OSBP and its yeast homolog Osh4p, which consists in creating a sterol gradient between membranes by vectorial transport. OSBP also contributes to the formation of ER/Golgi membrane contact sites, which are important hubs for the transfer of several lipid species. OSBP and Osh4p organize a counterflow transport of lipids whereby sterols are exchanged for the phosphoinositide PI4P, which is used as a fuel to drive sterol transport. This article is part of a Special Issue entitled: The cellular lipid landscape edited by Tim P. Levine and Anant K. Menon.
Keywords	cholesterol ; endoplasmic reticulum ; ergosterol ; fuels ; landscapes ; lipid transfer proteins ; mammals ; plasma membrane ; yeasts
Language	English
Dates of publication	2016-08
Size	p. 940-951.
Publishing place	Elsevier B.V.
Document type	Article
ISSN	1388-1981
DOI	10.1016/j.bbalip.2016.02.024
Database	NAL-Catalogue (AGRICOLA)

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