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Victor Faundez - One of the best experts on this subject based on the ideXlab platform.
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The WASH complex, an endosomal Arp2/3 activator, interacts with the Hermansky-Pudlak syndrome complex BLOC-1 and its cargo phosphatidylinositol-4-kinase type IIα.
2018Co-Authors: Pearl V Ryder, Rachel Vistein, Avanti Gokhale, Matthew N J Seaman, Manojkumar A Puthenveedu, Victor FaundezAbstract:Vesicle biogenesis machinery components such as coat proteins can interact with the actin cytoskeleton for cargo sorting into multiple pathways. It is unknown, however, whether these interactions are a general requirement for the diverse endosome traffic routes. In this study, we identify actin cytoskeleton regulators as previously unrecognized interactors of complexes associated with the Hermansky-Pudlak syndrome. Two complexes mutated in the Hermansky-Pudlak syndrome, adaptor protein complex-3 and biogenesis of lysosome-related organelles complex-1 (BLOC-1), interact with and are regulated by the lipid kinase phosphatidylinositol-4-kinase type IIα (PI4KIIα). We therefore hypothesized that PI4KIIα interacts with novel regulators of these complexes. To test this hypothesis, we immunoaffinity purified PI4KIIα from isotope-Labeled Cell lysates to quantitatively identify interactors. Strikingly, PI4KIIα isolation preferentially coenriched proteins that regulate the actin cytoskeleton, including guanine exchange factors for Rho family GTPases such as RhoGEF1 and several subunits of the WASH complex. We biochemically confirmed several of these PI4KIIα interactions. Of importance, BLOC-1 complex, WASH complex, RhoGEF1, or PI4KIIα depletions altered the content and/or subCellular distribution of the BLOC-1-sensitive cargoes PI4KIIα, ATP7A, and VAMP7. We conclude that the Hermansky-Pudlak syndrome complex BLOC-1 and its cargo PI4KIIα interact with regulators of the actin cytoskeleton.
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the wash complex an endosomal arp2 3 activator interacts with the hermansky pudlak syndrome complex bloc 1 and its cargo phosphatidylinositol 4 kinase type iiα
Molecular Biology of the Cell, 2013Co-Authors: Pearl V Ryder, Rachel Vistein, Avanti Gokhale, Matthew N J Seaman, Manojkumar A Puthenveedu, Victor FaundezAbstract:Vesicle biogenesis machinery components such as coat proteins can interact with the actin cytoskeleton for cargo sorting into multiple pathways. It is unknown, however, whether these interactions are a general requirement for the diverse endosome traffic routes. In this study, we identify actin cytoskeleton regulators as previously unrecognized interactors of complexes associated with the Hermansky–Pudlak syndrome. Two complexes mutated in the Hermansky–Pudlak syndrome, adaptor protein complex-3 and biogenesis of lysosome-related organelles complex-1 (BLOC-1), interact with and are regulated by the lipid kinase phosphatidylinositol-4-kinase type IIα (PI4KIIα). We therefore hypothesized that PI4KIIα interacts with novel regulators of these complexes. To test this hypothesis, we immunoaffinity purified PI4KIIα from isotope-Labeled Cell lysates to quantitatively identify interactors. Strikingly, PI4KIIα isolation preferentially coenriched proteins that regulate the actin cytoskeleton, including guanine exchange factors for Rho family GTPases such as RhoGEF1 and several subunits of the WASH complex. We biochemically confirmed several of these PI4KIIα interactions. Of importance, BLOC-1 complex, WASH complex, RhoGEF1, or PI4KIIα depletions altered the content and/or subCellular distribution of the BLOC-1–sensitive cargoes PI4KIIα, ATP7A, and VAMP7. We conclude that the Hermansky–Pudlak syndrome complex BLOC-1 and its cargo PI4KIIα interact with regulators of the actin cytoskeleton.
Pearl V Ryder - One of the best experts on this subject based on the ideXlab platform.
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The WASH complex, an endosomal Arp2/3 activator, interacts with the Hermansky-Pudlak syndrome complex BLOC-1 and its cargo phosphatidylinositol-4-kinase type IIα.
2018Co-Authors: Pearl V Ryder, Rachel Vistein, Avanti Gokhale, Matthew N J Seaman, Manojkumar A Puthenveedu, Victor FaundezAbstract:Vesicle biogenesis machinery components such as coat proteins can interact with the actin cytoskeleton for cargo sorting into multiple pathways. It is unknown, however, whether these interactions are a general requirement for the diverse endosome traffic routes. In this study, we identify actin cytoskeleton regulators as previously unrecognized interactors of complexes associated with the Hermansky-Pudlak syndrome. Two complexes mutated in the Hermansky-Pudlak syndrome, adaptor protein complex-3 and biogenesis of lysosome-related organelles complex-1 (BLOC-1), interact with and are regulated by the lipid kinase phosphatidylinositol-4-kinase type IIα (PI4KIIα). We therefore hypothesized that PI4KIIα interacts with novel regulators of these complexes. To test this hypothesis, we immunoaffinity purified PI4KIIα from isotope-Labeled Cell lysates to quantitatively identify interactors. Strikingly, PI4KIIα isolation preferentially coenriched proteins that regulate the actin cytoskeleton, including guanine exchange factors for Rho family GTPases such as RhoGEF1 and several subunits of the WASH complex. We biochemically confirmed several of these PI4KIIα interactions. Of importance, BLOC-1 complex, WASH complex, RhoGEF1, or PI4KIIα depletions altered the content and/or subCellular distribution of the BLOC-1-sensitive cargoes PI4KIIα, ATP7A, and VAMP7. We conclude that the Hermansky-Pudlak syndrome complex BLOC-1 and its cargo PI4KIIα interact with regulators of the actin cytoskeleton.
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the wash complex an endosomal arp2 3 activator interacts with the hermansky pudlak syndrome complex bloc 1 and its cargo phosphatidylinositol 4 kinase type iiα
Molecular Biology of the Cell, 2013Co-Authors: Pearl V Ryder, Rachel Vistein, Avanti Gokhale, Matthew N J Seaman, Manojkumar A Puthenveedu, Victor FaundezAbstract:Vesicle biogenesis machinery components such as coat proteins can interact with the actin cytoskeleton for cargo sorting into multiple pathways. It is unknown, however, whether these interactions are a general requirement for the diverse endosome traffic routes. In this study, we identify actin cytoskeleton regulators as previously unrecognized interactors of complexes associated with the Hermansky–Pudlak syndrome. Two complexes mutated in the Hermansky–Pudlak syndrome, adaptor protein complex-3 and biogenesis of lysosome-related organelles complex-1 (BLOC-1), interact with and are regulated by the lipid kinase phosphatidylinositol-4-kinase type IIα (PI4KIIα). We therefore hypothesized that PI4KIIα interacts with novel regulators of these complexes. To test this hypothesis, we immunoaffinity purified PI4KIIα from isotope-Labeled Cell lysates to quantitatively identify interactors. Strikingly, PI4KIIα isolation preferentially coenriched proteins that regulate the actin cytoskeleton, including guanine exchange factors for Rho family GTPases such as RhoGEF1 and several subunits of the WASH complex. We biochemically confirmed several of these PI4KIIα interactions. Of importance, BLOC-1 complex, WASH complex, RhoGEF1, or PI4KIIα depletions altered the content and/or subCellular distribution of the BLOC-1–sensitive cargoes PI4KIIα, ATP7A, and VAMP7. We conclude that the Hermansky–Pudlak syndrome complex BLOC-1 and its cargo PI4KIIα interact with regulators of the actin cytoskeleton.
Monique R. Bernsen - One of the best experts on this subject based on the ideXlab platform.
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Cell quantification evolution of compartmentalization and distribution of iron oxide particles and Labeled Cells
Contrast Media & Molecular Imaging, 2012Co-Authors: Gyula Kotek, S T Van Tiel, Gabriel P. Krestin, Piotr A Wielopolski, Gavin C Houston, Monique R. BernsenAbstract:The purpose of the study was to show the feasibility of quantification in the case of Cell death, Cell migration and Cell division by parametric MRI. We identify limitations for quantitative Cell tracking owing to mixed parallel processes. Various intravoxel SPIO-Labeled Cell, super paramagnetic iron oxide particles (SPIO) and micron-sized paramagnetic iron oxide (MPIO) particle distributions were prepared by methods mimicking biologically relevant processes (compartmentalization, migration, division and Cell death). R2* and R2 relaxometry measurements were performed at 3.0 T; iron concentration was measured by optical emission spectrometry. The effects of spatial distribution and compartmentalization of paramagnetic iron-oxide particles on relaxivity were analyzed. Assessment of R2′ (R2*-R2) allowed differentiation between intraCellular and extraCellular SPIO only if no high-iron-content extraCellular particles were present. Relaxivity was sensitive to variations in Cell labeling. Samples of the same Cell types embedded in the same suspension media at the same Cell density produced different relaxivity values, depending on the preparation of the Labeled Cells. In the case of Cell division, a unique relationship between relaxation rate and iron concentration was found, where the relaxivity proved to be independent of initial Cell labeling. In case of Cell mixing, the Cell density could be derived from relaxation values, even if iron concentration was undetermined. We demonstrated that relaxometry does not allow Labeled Cell quantification when multiple physiological processes such as Cell division and Cell migration coexist. The measured transversal relaxation rates were sensitive to the labeling technique. However, under special circumstances, despite the numerous limiting factors, quantification of the number of Labeled Cells by relaxometry was feasible. Copyright © 2012 John Wiley & Sons, Ltd.
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Ferumoxides-protamine sulfate is more effective than ferucarbotran for Cell labeling: implications for clinically applicable Cell tracking using MRI.
Contrast media & molecular imaging, 2009Co-Authors: G.m. Van Buul, Eric Farrell, Nicole Kops, S T Van Tiel, Pieter K. Bos, Harrie Weinans, Gabriel P. Krestin, G.j.v.m. Van Osch, Monique R. BernsenAbstract:The use of superparamagnetic iron oxide (SPIO) for labeling Cells holds great promise for clinically applicable Cell tracking using magnetic resonance imaging. For clinical application, an effectively and specifically Labeled Cell preparation is highly desired (i.e. a large amount of intraCellular iron and a negligible amount of extraCellular iron). In this study we performed a direct comparison of two SPIO labeling strategies that have both been reported as efficient and clinically translatable approaches. These approaches are Cell labeling using ferumoxides-protamine complexes or ferucarabotran particles. Cell labeling was performed on primary human bone marrow stromal Cells (hBMSCs) and chondrocytes. For both Cell types ferumoxides-protamine resulted in a higher percentage of Labeled Cells, a higher total iron load, a larger amount of intraCellular iron and a lower amount of extraCellular iron aggregates, compared with ferucarbotran. Consequently, hBMSC and chondrocyte labeling with ferumoxides-protamine is more effective and results in more specific Cell labeling than ferucarbotran.
Matthias Mann - One of the best experts on this subject based on the ideXlab platform.
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super silac mix for quantitative proteomics of human tumor tissue
Nature Methods, 2010Co-Authors: Tamar Geiger, Pawel Ostasiewicz, Jacek R Wisniewski, Matthias MannAbstract:Robust and accurate quantification of human tumor tissue proteomes is made possible by combining the tissue sample with an 'internal standard' mixture of five relevant, stable isotope–Labeled Cell lines, followed by mass spectrometry analysis. We describe a method to accurately quantify human tumor proteomes by combining a mixture of five stable-isotope labeling by amino acids in Cell culture (SILAC)-Labeled Cell lines with human carcinoma tissue. This generated hundreds of thousands of isotopically Labeled peptides in appropriate amounts to serve as internal standards for mass spectrometry–based analysis. By decoupling the labeling from the measurement, this super-SILAC method broadens the scope of SILAC-based proteomics.
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super silac mix for quantitative proteomics of human tumor tissue
Nature Methods, 2010Co-Authors: Tamar Geiger, Pawel Ostasiewicz, Jacek R Wisniewski, Juergen Cox, Matthias MannAbstract:We describe a method to accurately quantify human tumor proteomes by combining a mixture of five stable-isotope labeling by amino acids in Cell culture (SILAC)-Labeled Cell lines with human carcinoma tissue. This generated hundreds of thousands of isotopically Labeled peptides in appropriate amounts to serve as internal standards for mass spectrometry-based analysis. By decoupling the labeling from the measurement, this super-SILAC method broadens the scope of SILAC-based proteomics.
Rachel Vistein - One of the best experts on this subject based on the ideXlab platform.
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The WASH complex, an endosomal Arp2/3 activator, interacts with the Hermansky-Pudlak syndrome complex BLOC-1 and its cargo phosphatidylinositol-4-kinase type IIα.
2018Co-Authors: Pearl V Ryder, Rachel Vistein, Avanti Gokhale, Matthew N J Seaman, Manojkumar A Puthenveedu, Victor FaundezAbstract:Vesicle biogenesis machinery components such as coat proteins can interact with the actin cytoskeleton for cargo sorting into multiple pathways. It is unknown, however, whether these interactions are a general requirement for the diverse endosome traffic routes. In this study, we identify actin cytoskeleton regulators as previously unrecognized interactors of complexes associated with the Hermansky-Pudlak syndrome. Two complexes mutated in the Hermansky-Pudlak syndrome, adaptor protein complex-3 and biogenesis of lysosome-related organelles complex-1 (BLOC-1), interact with and are regulated by the lipid kinase phosphatidylinositol-4-kinase type IIα (PI4KIIα). We therefore hypothesized that PI4KIIα interacts with novel regulators of these complexes. To test this hypothesis, we immunoaffinity purified PI4KIIα from isotope-Labeled Cell lysates to quantitatively identify interactors. Strikingly, PI4KIIα isolation preferentially coenriched proteins that regulate the actin cytoskeleton, including guanine exchange factors for Rho family GTPases such as RhoGEF1 and several subunits of the WASH complex. We biochemically confirmed several of these PI4KIIα interactions. Of importance, BLOC-1 complex, WASH complex, RhoGEF1, or PI4KIIα depletions altered the content and/or subCellular distribution of the BLOC-1-sensitive cargoes PI4KIIα, ATP7A, and VAMP7. We conclude that the Hermansky-Pudlak syndrome complex BLOC-1 and its cargo PI4KIIα interact with regulators of the actin cytoskeleton.
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the wash complex an endosomal arp2 3 activator interacts with the hermansky pudlak syndrome complex bloc 1 and its cargo phosphatidylinositol 4 kinase type iiα
Molecular Biology of the Cell, 2013Co-Authors: Pearl V Ryder, Rachel Vistein, Avanti Gokhale, Matthew N J Seaman, Manojkumar A Puthenveedu, Victor FaundezAbstract:Vesicle biogenesis machinery components such as coat proteins can interact with the actin cytoskeleton for cargo sorting into multiple pathways. It is unknown, however, whether these interactions are a general requirement for the diverse endosome traffic routes. In this study, we identify actin cytoskeleton regulators as previously unrecognized interactors of complexes associated with the Hermansky–Pudlak syndrome. Two complexes mutated in the Hermansky–Pudlak syndrome, adaptor protein complex-3 and biogenesis of lysosome-related organelles complex-1 (BLOC-1), interact with and are regulated by the lipid kinase phosphatidylinositol-4-kinase type IIα (PI4KIIα). We therefore hypothesized that PI4KIIα interacts with novel regulators of these complexes. To test this hypothesis, we immunoaffinity purified PI4KIIα from isotope-Labeled Cell lysates to quantitatively identify interactors. Strikingly, PI4KIIα isolation preferentially coenriched proteins that regulate the actin cytoskeleton, including guanine exchange factors for Rho family GTPases such as RhoGEF1 and several subunits of the WASH complex. We biochemically confirmed several of these PI4KIIα interactions. Of importance, BLOC-1 complex, WASH complex, RhoGEF1, or PI4KIIα depletions altered the content and/or subCellular distribution of the BLOC-1–sensitive cargoes PI4KIIα, ATP7A, and VAMP7. We conclude that the Hermansky–Pudlak syndrome complex BLOC-1 and its cargo PI4KIIα interact with regulators of the actin cytoskeleton.
