The Experts below are selected from a list of 246 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.
J. Wolff - One of the best experts on this subject based on the ideXlab platform.
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Plasma Membrane tubulin.
Biochimica et biophysica acta, 2009Co-Authors: J. WolffAbstract:The association of tubulin with the Plasma Membrane comprises multiple levels of penetration into the bilayer: from integral Membrane protein, to attachment via palmitoylation, to surface binding, and to microtubules attached by linker proteins to proteins in the Membrane. Here we discuss the soundness and weaknesses of the chemical and biochemical evidence marshaled to support these associations, as well as the mechanisms by which tubulin or microtubules may regulate functions at the Plasma Membrane.
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Plasma Membrane localization of palmitoylated tubulin.
Biochemical and biophysical research communications, 2001Co-Authors: Anna Maria Zambito, J. WolffAbstract:Abstract PC12 pheochromocytoma cells incorporate [3H]palmitic acid into tubulin in a time- and cell-density-dependent manner. The Plasma Membrane-enriched fraction contains most of the radioactivity of the Membrane pellet. While palmitoylated tubulin is found in both the cytoplasm and particulate fraction, the bulk of [3H]palmitic acid bound to tubulin is present in the crude Membrane pellet and the tubulin extracted from the Plasma Membrane is more heavily palmitoylated than that extracted from endoplasmic reticulum. Detergent-extracted tubulin from Plasma Membrane is, to a large extent, polymerization competent; a substantial fraction, increasing as a function of labeling time, is not hydroxylamine-labile. The requirement for detergent extraction, the accompanying changes in tubulin properties and the present findings of preferential incorporation of labeled tubulin into Plasma Membranes, make it clear that direct incorporation of tubulin into the Plasma Membrane can occur.
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.
Marina Pitto - One of the best experts on this subject based on the ideXlab platform.
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Proteomics of Plasma Membrane microdomains.
Expert Review of Proteomics, 2005Co-Authors: Francesca Raimondo, Paolo Ceppi, Katia Guidi, Massimo Masserini, Claudia Foletti, Marina PittoAbstract:Plasma Membrane microdomains represent subcompartments of the Plasma Membrane characterized by a specific lipid and protein composition. The recognition of microdomains in nearly all the eukaryotic Membranes has accredited them with specialized functions in health and disease. Several proteomic studies have recently addressed the specific composition of Plasma Membrane microdomains, and will be reviewed in this paper. Peculiar information has been obtained, but a comprehensive view of the main protein classes required to define the microdomain proteome is still missing. The achievement of this information is slowed by the difficulties encountered in resolving and analyzing hydrophobic proteins, but it could help in understanding the overall function of Plasma Membrane microdomains and their involvement in human pathology.
