The Experts below are selected from a list of 87 Experts worldwide ranked by ideXlab platform
Christian Rosenmund - One of the best experts on this subject based on the ideXlab platform.
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orp osh mediate cross talk between er plasma Membrane Contact Site components and plasma Membrane snares
Cellular and Molecular Life Sciences, 2021Co-Authors: Thorsten Trimbuch, Saundarya Shah, Jussi Jäntti, Vesa M. Olkkonen, Marion Weberboyvat, Christian RosenmundAbstract:OSBP-homologous proteins (ORPs, Oshp) are lipid binding/transfer proteins. Several ORP/Oshp localize to Membrane Contacts between the endoplasmic reticulum (ER) and the plasma Membrane, where they mediate lipid transfer or regulate lipid-modifying enzymes. A common way in which they target Contacts is by binding to the ER proteins, VAP/Scs2p, while the second Membrane is targeted by other interactions with lipids or proteins.We have studied the cross-talk of secretory SNARE proteins and their regulators with ORP/Oshp and VAPA/Scs2p at ER-plasma Membrane Contact Sites in yeast and murine primary neurons. We show that Oshp-Scs2p interactions depend on intact secretory SNARE proteins, especially Sec9p. SNAP-25/Sec9p directly interact with ORP/Osh proteins and their disruption destabilized the ORP/Osh proteins, associated with dysfunction of VAPA/Scs2p. Deleting OSH1-3 in yeast or knocking down ORP2 in primary neurons reduced the oligomerization of VAPA/Scs2p and affected their multiple interactions with SNAREs. These observations reveal a novel cross-talk between the machineries of ER-plasma Membrane Contact Sites and those driving exocytosis.
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ORP/Osh mediate cross-talk between ER-plasma Membrane Contact Site components and plasma Membrane SNAREs.
Cellular and molecular life sciences : CMLS, 2020Co-Authors: Marion Weber-boyvat, Thorsten Trimbuch, Saundarya Shah, Jussi Jäntti, Vesa M. Olkkonen, Christian RosenmundAbstract:OSBP-homologous proteins (ORPs, Oshp) are lipid binding/transfer proteins. Several ORP/Oshp localize to Membrane Contacts between the endoplasmic reticulum (ER) and the plasma Membrane, where they mediate lipid transfer or regulate lipid-modifying enzymes. A common way in which they target Contacts is by binding to the ER proteins, VAP/Scs2p, while the second Membrane is targeted by other interactions with lipids or proteins.We have studied the cross-talk of secretory SNARE proteins and their regulators with ORP/Oshp and VAPA/Scs2p at ER-plasma Membrane Contact Sites in yeast and murine primary neurons. We show that Oshp-Scs2p interactions depend on intact secretory SNARE proteins, especially Sec9p. SNAP-25/Sec9p directly interact with ORP/Osh proteins and their disruption destabilized the ORP/Osh proteins, associated with dysfunction of VAPA/Scs2p. Deleting OSH1-3 in yeast or knocking down ORP2 in primary neurons reduced the oligomerization of VAPA/Scs2p and affected their multiple interactions with SNAREs. These observations reveal a novel cross-talk between the machineries of ER-plasma Membrane Contact Sites and those driving exocytosis.
Marie-lise Lacombe - One of the best experts on this subject based on the ideXlab platform.
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mitochondrial cardiolipin phospholipid trafficking the role of Membrane Contact Site complexes and lipid transfer proteins
Chemistry and Physics of Lipids, 2014Co-Authors: Uwe Schlattner, Denis Rousseau, Mathieu Boissan, Carmen A. Mannella, Richard M. Epand, Malgorzata Tokarskaschlattner, Marie-lise LacombeAbstract:Historically, cellular trafficking of lipids has received much less attention than protein trafficking, mostly because its biological importance was underestimated, involved sorting and translocation mechanisms were not known, and analytical tools were limiting. This has changed during the last decade, and we discuss here some progress made in respect to mitochondria and the trafficking of phospholipids, in particular cardiolipin. Different Membrane Contact Site or junction complexes and putative lipid transfer proteins for intra- and interMembrane lipid translocation have been described, involving mitochondrial inner and outer Membrane, and the adjacent Membranes of the endoplasmic reticulum. An image emerges how cardiolipin precursors, remodeling intermediates, mature cardiolipin and its oxidation products could migrate between Membranes, and how this trafficking is involved in cardiolipin biosynthesis and cell signaling events. Particular emphasis in this review is given to mitochondrial nucleoside diphosphate kinase D and mitochondrial creatine kinases, which emerge to have roles in both, Membrane junction formation and lipid transfer.
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Mitochondrial cardiolipin/phospholipid trafficking: the role of Membrane Contact Site complexes and lipid transfer proteins.
Chemistry and physics of lipids, 2013Co-Authors: Uwe Schlattner, Malgorzata Tokarska-schlattner, Denis Rousseau, Mathieu Boissan, Carmen A. Mannella, Richard M. Epand, Marie-lise LacombeAbstract:Historically, cellular trafficking of lipids has received much less attention than protein trafficking, mostly because its biological importance was underestimated, involved sorting and translocation mechanisms were not known, and analytical tools were limiting. This has changed during the last decade, and we discuss here some progress made in respect to mitochondria and the trafficking of phospholipids, in particular cardiolipin. Different Membrane Contact Site or junction complexes and putative lipid transfer proteins for intra- and interMembrane lipid translocation have been described, involving mitochondrial inner and outer Membrane, and the adjacent Membranes of the endoplasmic reticulum. An image emerges how cardiolipin precursors, remodeling intermediates, mature cardiolipin and its oxidation products could migrate between Membranes, and how this trafficking is involved in cardiolipin biosynthesis and cell signaling events. Particular emphasis in this review is given to mitochondrial nucleoside diphosphate kinase D and mitochondrial creatine kinases, which emerge to have roles in both, Membrane junction formation and lipid transfer.
Uwe Schlattner - One of the best experts on this subject based on the ideXlab platform.
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mitochondrial cardiolipin phospholipid trafficking the role of Membrane Contact Site complexes and lipid transfer proteins
Chemistry and Physics of Lipids, 2014Co-Authors: Uwe Schlattner, Denis Rousseau, Mathieu Boissan, Carmen A. Mannella, Richard M. Epand, Malgorzata Tokarskaschlattner, Marie-lise LacombeAbstract:Historically, cellular trafficking of lipids has received much less attention than protein trafficking, mostly because its biological importance was underestimated, involved sorting and translocation mechanisms were not known, and analytical tools were limiting. This has changed during the last decade, and we discuss here some progress made in respect to mitochondria and the trafficking of phospholipids, in particular cardiolipin. Different Membrane Contact Site or junction complexes and putative lipid transfer proteins for intra- and interMembrane lipid translocation have been described, involving mitochondrial inner and outer Membrane, and the adjacent Membranes of the endoplasmic reticulum. An image emerges how cardiolipin precursors, remodeling intermediates, mature cardiolipin and its oxidation products could migrate between Membranes, and how this trafficking is involved in cardiolipin biosynthesis and cell signaling events. Particular emphasis in this review is given to mitochondrial nucleoside diphosphate kinase D and mitochondrial creatine kinases, which emerge to have roles in both, Membrane junction formation and lipid transfer.
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Mitochondrial cardiolipin/phospholipid trafficking: the role of Membrane Contact Site complexes and lipid transfer proteins.
Chemistry and physics of lipids, 2013Co-Authors: Uwe Schlattner, Malgorzata Tokarska-schlattner, Denis Rousseau, Mathieu Boissan, Carmen A. Mannella, Richard M. Epand, Marie-lise LacombeAbstract:Historically, cellular trafficking of lipids has received much less attention than protein trafficking, mostly because its biological importance was underestimated, involved sorting and translocation mechanisms were not known, and analytical tools were limiting. This has changed during the last decade, and we discuss here some progress made in respect to mitochondria and the trafficking of phospholipids, in particular cardiolipin. Different Membrane Contact Site or junction complexes and putative lipid transfer proteins for intra- and interMembrane lipid translocation have been described, involving mitochondrial inner and outer Membrane, and the adjacent Membranes of the endoplasmic reticulum. An image emerges how cardiolipin precursors, remodeling intermediates, mature cardiolipin and its oxidation products could migrate between Membranes, and how this trafficking is involved in cardiolipin biosynthesis and cell signaling events. Particular emphasis in this review is given to mitochondrial nucleoside diphosphate kinase D and mitochondrial creatine kinases, which emerge to have roles in both, Membrane junction formation and lipid transfer.
Vesa M. Olkkonen - One of the best experts on this subject based on the ideXlab platform.
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orp osh mediate cross talk between er plasma Membrane Contact Site components and plasma Membrane snares
Cellular and Molecular Life Sciences, 2021Co-Authors: Thorsten Trimbuch, Saundarya Shah, Jussi Jäntti, Vesa M. Olkkonen, Marion Weberboyvat, Christian RosenmundAbstract:OSBP-homologous proteins (ORPs, Oshp) are lipid binding/transfer proteins. Several ORP/Oshp localize to Membrane Contacts between the endoplasmic reticulum (ER) and the plasma Membrane, where they mediate lipid transfer or regulate lipid-modifying enzymes. A common way in which they target Contacts is by binding to the ER proteins, VAP/Scs2p, while the second Membrane is targeted by other interactions with lipids or proteins.We have studied the cross-talk of secretory SNARE proteins and their regulators with ORP/Oshp and VAPA/Scs2p at ER-plasma Membrane Contact Sites in yeast and murine primary neurons. We show that Oshp-Scs2p interactions depend on intact secretory SNARE proteins, especially Sec9p. SNAP-25/Sec9p directly interact with ORP/Osh proteins and their disruption destabilized the ORP/Osh proteins, associated with dysfunction of VAPA/Scs2p. Deleting OSH1-3 in yeast or knocking down ORP2 in primary neurons reduced the oligomerization of VAPA/Scs2p and affected their multiple interactions with SNAREs. These observations reveal a novel cross-talk between the machineries of ER-plasma Membrane Contact Sites and those driving exocytosis.
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ORP/Osh mediate cross-talk between ER-plasma Membrane Contact Site components and plasma Membrane SNAREs.
Cellular and molecular life sciences : CMLS, 2020Co-Authors: Marion Weber-boyvat, Thorsten Trimbuch, Saundarya Shah, Jussi Jäntti, Vesa M. Olkkonen, Christian RosenmundAbstract:OSBP-homologous proteins (ORPs, Oshp) are lipid binding/transfer proteins. Several ORP/Oshp localize to Membrane Contacts between the endoplasmic reticulum (ER) and the plasma Membrane, where they mediate lipid transfer or regulate lipid-modifying enzymes. A common way in which they target Contacts is by binding to the ER proteins, VAP/Scs2p, while the second Membrane is targeted by other interactions with lipids or proteins.We have studied the cross-talk of secretory SNARE proteins and their regulators with ORP/Oshp and VAPA/Scs2p at ER-plasma Membrane Contact Sites in yeast and murine primary neurons. We show that Oshp-Scs2p interactions depend on intact secretory SNARE proteins, especially Sec9p. SNAP-25/Sec9p directly interact with ORP/Osh proteins and their disruption destabilized the ORP/Osh proteins, associated with dysfunction of VAPA/Scs2p. Deleting OSH1-3 in yeast or knocking down ORP2 in primary neurons reduced the oligomerization of VAPA/Scs2p and affected their multiple interactions with SNAREs. These observations reveal a novel cross-talk between the machineries of ER-plasma Membrane Contact Sites and those driving exocytosis.
Marion Weberboyvat - One of the best experts on this subject based on the ideXlab platform.
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orp osh mediate cross talk between er plasma Membrane Contact Site components and plasma Membrane snares
Cellular and Molecular Life Sciences, 2021Co-Authors: Thorsten Trimbuch, Saundarya Shah, Jussi Jäntti, Vesa M. Olkkonen, Marion Weberboyvat, Christian RosenmundAbstract:OSBP-homologous proteins (ORPs, Oshp) are lipid binding/transfer proteins. Several ORP/Oshp localize to Membrane Contacts between the endoplasmic reticulum (ER) and the plasma Membrane, where they mediate lipid transfer or regulate lipid-modifying enzymes. A common way in which they target Contacts is by binding to the ER proteins, VAP/Scs2p, while the second Membrane is targeted by other interactions with lipids or proteins.We have studied the cross-talk of secretory SNARE proteins and their regulators with ORP/Oshp and VAPA/Scs2p at ER-plasma Membrane Contact Sites in yeast and murine primary neurons. We show that Oshp-Scs2p interactions depend on intact secretory SNARE proteins, especially Sec9p. SNAP-25/Sec9p directly interact with ORP/Osh proteins and their disruption destabilized the ORP/Osh proteins, associated with dysfunction of VAPA/Scs2p. Deleting OSH1-3 in yeast or knocking down ORP2 in primary neurons reduced the oligomerization of VAPA/Scs2p and affected their multiple interactions with SNAREs. These observations reveal a novel cross-talk between the machineries of ER-plasma Membrane Contact Sites and those driving exocytosis.