The Experts below are selected from a list of 72 Experts worldwide ranked by ideXlab platform
Esther Asan - One of the best experts on this subject based on the ideXlab platform.
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The BEACH Protein LRBA Promotes the Localization of the Heterotrimeric G-Protein G_olf to Olfactory Cilia
Scientific Reports, 2017Co-Authors: Stefan Kurtenbach, Andreas Gießl, Siv Strömberg, Jan Kremers, Jenny Atorf, Sebastian Rasche, Eva M. Neuhaus, Denis Hervé, Johann Helmut Brandstätter, Esther AsanAbstract:BEACH domain Proteins are involved in membrane Protein traffic and human diseases, but their molecular mechanisms are not understood. The BEACH Protein LRBA has been implicated in immune response and cell proliferation, and human LRBA mutations cause severe immune deficiency. Here, we report a first functional and molecular phenotype outside the immune system of LRBA-knockout mice: compromised olfaction, manifesting in reduced electro-olfactogram response amplitude, impaired food-finding efficiency, and smaller olfactory bulbs. LRBA is prominently expressed in olfactory and vomeronasal chemosensory neurons of wild-type mice. Olfactory impairment in the LRBA-KO is explained by markedly reduced concentrations (20–40% of wild-type levels) of all three subunits α_olf, β_1 and γ_13 of the olfactory heterotrimeric G-Protein, G_olf, in the sensory cilia of olfactory neurons. In contrast, cilia morphology and the concentrations of many other Proteins of olfactory cilia are not or only slightly affected. LRBA is also highly expressed in photoreceptor cells, another cell type with a specialized sensory cilium and heterotrimeric G-Protein-based signalling; however, visual function appeared unimpaired by the LRBA-KO. To our knowledge, this is the first observation that a BEACH Protein is required for the efficient subcellular localization of a Lipid-Anchored Protein, and of a ciliary Protein.
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The BEACH Protein LRBA Promotes the Localization of the Heterotrimeric G-Protein Golf to Olfactory Cilia
Scientific Reports, 2017Co-Authors: Stefan Kurtenbach, Andreas Gießl, Siv Strömberg, Jan Kremers, Jenny Atorf, Sebastian Rasche, Eva M. Neuhaus, Denis Hervé, Johann Helmut Brandstätter, Esther AsanAbstract:BEACH domain Proteins are involved in membrane Protein traffic and human diseases, but their molecular mechanisms are not understood. The BEACH Protein LRBA has been implicated in immune response and cell proliferation, and human LRBA mutations cause severe immune deficiency. Here, we report a first functional and molecular phenotype outside the immune system of LRBA-knockout mice: compromised olfaction, manifesting in reduced electro-olfactogram response amplitude, impaired food-finding efficiency, and smaller olfactory bulbs. LRBA is prominently expressed in olfactory and vomeronasal chemosensory neurons of wild-type mice. Olfactory impairment in the LRBA-KO is explained by markedly reduced concentrations (20–40% of wild-type levels) of all three subunits αolf, β1 and γ13 of the olfactory heterotrimeric G-Protein, Golf, in the sensory cilia of olfactory neurons. In contrast, cilia morphology and the concentrations of many other Proteins of olfactory cilia are not or only slightly affected. LRBA is also highly expressed in photoreceptor cells, another cell type with a specialized sensory cilium and heterotrimeric G-Protein-based signalling; however, visual function appeared unimpaired by the LRBA-KO. To our knowledge, this is the first observation that a BEACH Protein is required for the efficient subcellular localization of a Lipid-Anchored Protein, and of a ciliary Protein.
Stefan Kurtenbach - One of the best experts on this subject based on the ideXlab platform.
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The BEACH Protein LRBA Promotes the Localization of the Heterotrimeric G-Protein G_olf to Olfactory Cilia
Scientific Reports, 2017Co-Authors: Stefan Kurtenbach, Andreas Gießl, Siv Strömberg, Jan Kremers, Jenny Atorf, Sebastian Rasche, Eva M. Neuhaus, Denis Hervé, Johann Helmut Brandstätter, Esther AsanAbstract:BEACH domain Proteins are involved in membrane Protein traffic and human diseases, but their molecular mechanisms are not understood. The BEACH Protein LRBA has been implicated in immune response and cell proliferation, and human LRBA mutations cause severe immune deficiency. Here, we report a first functional and molecular phenotype outside the immune system of LRBA-knockout mice: compromised olfaction, manifesting in reduced electro-olfactogram response amplitude, impaired food-finding efficiency, and smaller olfactory bulbs. LRBA is prominently expressed in olfactory and vomeronasal chemosensory neurons of wild-type mice. Olfactory impairment in the LRBA-KO is explained by markedly reduced concentrations (20–40% of wild-type levels) of all three subunits α_olf, β_1 and γ_13 of the olfactory heterotrimeric G-Protein, G_olf, in the sensory cilia of olfactory neurons. In contrast, cilia morphology and the concentrations of many other Proteins of olfactory cilia are not or only slightly affected. LRBA is also highly expressed in photoreceptor cells, another cell type with a specialized sensory cilium and heterotrimeric G-Protein-based signalling; however, visual function appeared unimpaired by the LRBA-KO. To our knowledge, this is the first observation that a BEACH Protein is required for the efficient subcellular localization of a Lipid-Anchored Protein, and of a ciliary Protein.
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The BEACH Protein LRBA Promotes the Localization of the Heterotrimeric G-Protein Golf to Olfactory Cilia
Scientific Reports, 2017Co-Authors: Stefan Kurtenbach, Andreas Gießl, Siv Strömberg, Jan Kremers, Jenny Atorf, Sebastian Rasche, Eva M. Neuhaus, Denis Hervé, Johann Helmut Brandstätter, Esther AsanAbstract:BEACH domain Proteins are involved in membrane Protein traffic and human diseases, but their molecular mechanisms are not understood. The BEACH Protein LRBA has been implicated in immune response and cell proliferation, and human LRBA mutations cause severe immune deficiency. Here, we report a first functional and molecular phenotype outside the immune system of LRBA-knockout mice: compromised olfaction, manifesting in reduced electro-olfactogram response amplitude, impaired food-finding efficiency, and smaller olfactory bulbs. LRBA is prominently expressed in olfactory and vomeronasal chemosensory neurons of wild-type mice. Olfactory impairment in the LRBA-KO is explained by markedly reduced concentrations (20–40% of wild-type levels) of all three subunits αolf, β1 and γ13 of the olfactory heterotrimeric G-Protein, Golf, in the sensory cilia of olfactory neurons. In contrast, cilia morphology and the concentrations of many other Proteins of olfactory cilia are not or only slightly affected. LRBA is also highly expressed in photoreceptor cells, another cell type with a specialized sensory cilium and heterotrimeric G-Protein-based signalling; however, visual function appeared unimpaired by the LRBA-KO. To our knowledge, this is the first observation that a BEACH Protein is required for the efficient subcellular localization of a Lipid-Anchored Protein, and of a ciliary Protein.
Robin F. Irvine - One of the best experts on this subject based on the ideXlab platform.
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Mobility of Proteins associated with the plasma membrane by interaction with inositol lipids
Journal of Cell Science, 2005Co-Authors: David Brough, Farzana Bhatti, Robin F. IrvineAbstract:Translocation of a Protein to the plasma membrane in response to the generation of polyphosphoinositol lipids is believed to be an important component of cellular regulation, in part because it increases the effective concentration of that Protein relative to other Proteins in the same membrane by restricting it to a two-dimensional space. However, such a concept assumes that, once translocated, a Protein retains the free mobility it had in the cytoplasm, and also that the possible existence of partitioned pools of inositol lipids does not restrict its sphere of influence. We have explored by fluorescence recovery after photobleaching (FRAP) the mobility of four green-fluorescent-Protein-tagged Proteins, GAP1 IP4BP and GAP1 m , when they are either cytoplasmic or attached to the plasma membrane, and the PH domain of PI-PLCδ 1 and ICAM as representative of, respectively, another inositol-Lipid-Anchored Protein and a single-transmembrane-span-domain Protein. The data from GAP1 m and the PI-PLCδ 1 PH domain show that, when Proteins associate with inositol lipids in the plasma membrane, they retain a mobility similar to that in the cytoplasm, and probably also similar to the inositol lipid to which they are attached, suggesting a free diffusion within the plane of the membrane. Moreover, this free diffusion is similar whether they are bound to PtdIns(3,4,5) P 3 or to PtdIns(4,5) P 2 , and no evidence was found by these criteria for restricted pools of PtdIns(4,5) P 2 . The mobility of GAP1 IP4BP , which has been reported to associate with PtdIns(4,5) P 2 in the plasma membrane, is much lower, suggesting that it might interact with other cellular components. Moreover, the mobility of GAP1 IP4BP is not detectably altered by the generation of either of its two potential regulators, Ins(1,3,4,5) P 4 or PtdIns(3,4,5) P 3 .
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Mobility of Proteins associated with the plasma membrane by interaction with inositol lipids.
Journal of cell science, 2005Co-Authors: David Brough, Farzana Bhatti, Robin F. IrvineAbstract:Translocation of a Protein to the plasma membrane in response to the generation of polyphosphoinositol lipids is believed to be an important component of cellular regulation, in part because it increases the effective concentration of that Protein relative to other Proteins in the same membrane by restricting it to a two-dimensional space. However, such a concept assumes that, once translocated, a Protein retains the free mobility it had in the cytoplasm, and also that the possible existence of partitioned pools of inositol lipids does not restrict its sphere of influence. We have explored by fluorescence recovery after photobleaching (FRAP) the mobility of four green-fluorescent-Protein-tagged Proteins, GAP1(IP4BP) and GAP1(m), when they are either cytoplasmic or attached to the plasma membrane, and the PH domain of PI-PLCdelta(1) and ICAM as representative of, respectively, another inositol-Lipid-Anchored Protein and a single-transmembrane-span-domain Protein. The data from GAP1(m) and the PI-PLCdelta(1) PH domain show that, when Proteins associate with inositol lipids in the plasma membrane, they retain a mobility similar to that in the cytoplasm, and probably also similar to the inositol lipid to which they are attached, suggesting a free diffusion within the plane of the membrane. Moreover, this free diffusion is similar whether they are bound to PtdIns(3,4,5)P(3) or to PtdIns(4,5)P(2), and no evidence was found by these criteria for restricted pools of PtdIns(4,5)P(2). The mobility of GAP1(IP4BP), which has been reported to associate with PtdIns(4,5)P(2) in the plasma membrane, is much lower, suggesting that it might interact with other cellular components. Moreover, the mobility of GAP1(IP4BP) is not detectably altered by the generation of either of its two potential regulators, Ins(1,3,4,5)P(4) or PtdIns(3,4,5)P(3).
Eva M. Neuhaus - One of the best experts on this subject based on the ideXlab platform.
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The BEACH Protein LRBA Promotes the Localization of the Heterotrimeric G-Protein G_olf to Olfactory Cilia
Scientific Reports, 2017Co-Authors: Stefan Kurtenbach, Andreas Gießl, Siv Strömberg, Jan Kremers, Jenny Atorf, Sebastian Rasche, Eva M. Neuhaus, Denis Hervé, Johann Helmut Brandstätter, Esther AsanAbstract:BEACH domain Proteins are involved in membrane Protein traffic and human diseases, but their molecular mechanisms are not understood. The BEACH Protein LRBA has been implicated in immune response and cell proliferation, and human LRBA mutations cause severe immune deficiency. Here, we report a first functional and molecular phenotype outside the immune system of LRBA-knockout mice: compromised olfaction, manifesting in reduced electro-olfactogram response amplitude, impaired food-finding efficiency, and smaller olfactory bulbs. LRBA is prominently expressed in olfactory and vomeronasal chemosensory neurons of wild-type mice. Olfactory impairment in the LRBA-KO is explained by markedly reduced concentrations (20–40% of wild-type levels) of all three subunits α_olf, β_1 and γ_13 of the olfactory heterotrimeric G-Protein, G_olf, in the sensory cilia of olfactory neurons. In contrast, cilia morphology and the concentrations of many other Proteins of olfactory cilia are not or only slightly affected. LRBA is also highly expressed in photoreceptor cells, another cell type with a specialized sensory cilium and heterotrimeric G-Protein-based signalling; however, visual function appeared unimpaired by the LRBA-KO. To our knowledge, this is the first observation that a BEACH Protein is required for the efficient subcellular localization of a Lipid-Anchored Protein, and of a ciliary Protein.
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The BEACH Protein LRBA Promotes the Localization of the Heterotrimeric G-Protein Golf to Olfactory Cilia
Scientific Reports, 2017Co-Authors: Stefan Kurtenbach, Andreas Gießl, Siv Strömberg, Jan Kremers, Jenny Atorf, Sebastian Rasche, Eva M. Neuhaus, Denis Hervé, Johann Helmut Brandstätter, Esther AsanAbstract:BEACH domain Proteins are involved in membrane Protein traffic and human diseases, but their molecular mechanisms are not understood. The BEACH Protein LRBA has been implicated in immune response and cell proliferation, and human LRBA mutations cause severe immune deficiency. Here, we report a first functional and molecular phenotype outside the immune system of LRBA-knockout mice: compromised olfaction, manifesting in reduced electro-olfactogram response amplitude, impaired food-finding efficiency, and smaller olfactory bulbs. LRBA is prominently expressed in olfactory and vomeronasal chemosensory neurons of wild-type mice. Olfactory impairment in the LRBA-KO is explained by markedly reduced concentrations (20–40% of wild-type levels) of all three subunits αolf, β1 and γ13 of the olfactory heterotrimeric G-Protein, Golf, in the sensory cilia of olfactory neurons. In contrast, cilia morphology and the concentrations of many other Proteins of olfactory cilia are not or only slightly affected. LRBA is also highly expressed in photoreceptor cells, another cell type with a specialized sensory cilium and heterotrimeric G-Protein-based signalling; however, visual function appeared unimpaired by the LRBA-KO. To our knowledge, this is the first observation that a BEACH Protein is required for the efficient subcellular localization of a Lipid-Anchored Protein, and of a ciliary Protein.
Denis Hervé - One of the best experts on this subject based on the ideXlab platform.
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The BEACH Protein LRBA Promotes the Localization of the Heterotrimeric G-Protein G_olf to Olfactory Cilia
Scientific Reports, 2017Co-Authors: Stefan Kurtenbach, Andreas Gießl, Siv Strömberg, Jan Kremers, Jenny Atorf, Sebastian Rasche, Eva M. Neuhaus, Denis Hervé, Johann Helmut Brandstätter, Esther AsanAbstract:BEACH domain Proteins are involved in membrane Protein traffic and human diseases, but their molecular mechanisms are not understood. The BEACH Protein LRBA has been implicated in immune response and cell proliferation, and human LRBA mutations cause severe immune deficiency. Here, we report a first functional and molecular phenotype outside the immune system of LRBA-knockout mice: compromised olfaction, manifesting in reduced electro-olfactogram response amplitude, impaired food-finding efficiency, and smaller olfactory bulbs. LRBA is prominently expressed in olfactory and vomeronasal chemosensory neurons of wild-type mice. Olfactory impairment in the LRBA-KO is explained by markedly reduced concentrations (20–40% of wild-type levels) of all three subunits α_olf, β_1 and γ_13 of the olfactory heterotrimeric G-Protein, G_olf, in the sensory cilia of olfactory neurons. In contrast, cilia morphology and the concentrations of many other Proteins of olfactory cilia are not or only slightly affected. LRBA is also highly expressed in photoreceptor cells, another cell type with a specialized sensory cilium and heterotrimeric G-Protein-based signalling; however, visual function appeared unimpaired by the LRBA-KO. To our knowledge, this is the first observation that a BEACH Protein is required for the efficient subcellular localization of a Lipid-Anchored Protein, and of a ciliary Protein.
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The BEACH Protein LRBA Promotes the Localization of the Heterotrimeric G-Protein Golf to Olfactory Cilia
Scientific Reports, 2017Co-Authors: Stefan Kurtenbach, Andreas Gießl, Siv Strömberg, Jan Kremers, Jenny Atorf, Sebastian Rasche, Eva M. Neuhaus, Denis Hervé, Johann Helmut Brandstätter, Esther AsanAbstract:BEACH domain Proteins are involved in membrane Protein traffic and human diseases, but their molecular mechanisms are not understood. The BEACH Protein LRBA has been implicated in immune response and cell proliferation, and human LRBA mutations cause severe immune deficiency. Here, we report a first functional and molecular phenotype outside the immune system of LRBA-knockout mice: compromised olfaction, manifesting in reduced electro-olfactogram response amplitude, impaired food-finding efficiency, and smaller olfactory bulbs. LRBA is prominently expressed in olfactory and vomeronasal chemosensory neurons of wild-type mice. Olfactory impairment in the LRBA-KO is explained by markedly reduced concentrations (20–40% of wild-type levels) of all three subunits αolf, β1 and γ13 of the olfactory heterotrimeric G-Protein, Golf, in the sensory cilia of olfactory neurons. In contrast, cilia morphology and the concentrations of many other Proteins of olfactory cilia are not or only slightly affected. LRBA is also highly expressed in photoreceptor cells, another cell type with a specialized sensory cilium and heterotrimeric G-Protein-based signalling; however, visual function appeared unimpaired by the LRBA-KO. To our knowledge, this is the first observation that a BEACH Protein is required for the efficient subcellular localization of a Lipid-Anchored Protein, and of a ciliary Protein.