The Experts below are selected from a list of 55152 Experts worldwide ranked by ideXlab platform
Sylvie Friant - One of the best experts on this subject based on the ideXlab platform.
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Evolutionary analysis of the ENTH/ANTH/VHS Protein Superfamily reveals a coevolution between membrane trafficking and metabolism.
BMC genomics, 2012Co-Authors: Johan-owen De Craene, Raymond Ripp, Odile Lecompte, Julie D. Thompson, Olivier Poch, Sylvie FriantAbstract:Background Membrane trafficking involves the complex regulation of Proteins and lipids intracellular localization and is required for metabolic uptake, cell growth and development. Different trafficking pathways passing through the endosomes are coordinated by the ENTH/ANTH/VHS adaptor Protein Superfamily. The endosomes are crucial for eukaryotes since the acquisition of the endomembrane system was a central process in eukaryogenesis.
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Evolutionary analysis of the ENTH/ANTH/VHS Protein Superfamily reveals a coevolution between membrane trafficking and metabolism.
BMC Genomics, 2012Co-Authors: Johan-owen De Craene, Raymond Ripp, Odile Lecompte, Olivier Poch, Julie Thompson, Sylvie FriantAbstract:ABSTRACT: BACKGROUND: Membrane trafficking involves the complex regulation of Proteins and lipids intracellular localization and is required for metabolic uptake, cell growth and development. Different trafficking pathways passing through the endosomes are coordinated by the ENTH/ANTH/VHS adaptor Protein Superfamily. The endosomes are crucial for eukaryotes since the acquisition of the endomembrane system was a central process in eukaryogenesis. RESULTS: Our in silico analysis of this ENTH/ANTH/VHS Superfamily, consisting of Proteins gathered from 84 complete genomes representative of the different eukaryotic taxa, revealed that genomic distribution of this Superfamily allows to discriminate Fungi and Metazoa from Plantae and Protists. Next, in a four way genome wide comparison, we showed that this discriminative feature is observed not only for other membrane trafficking effectors, but also for Proteins involved in metabolism and in cytokinesis, suggesting that metabolism, cytokinesis and intracellular trafficking pathways co-evolved. Moreover, some of the Proteins identified were implicated in multiple functions, in either trafficking and metabolism or trafficking and cytokinesis, suggesting that membrane trafficking is central to this co-evolution process. CONCLUSION: Our study suggests that membrane trafficking and compartmentalization were not only key features for the emergence of eukaryotic cells but also drove the separation of the eukaryotes in the different taxa.
A. Osuna - One of the best experts on this subject based on the ideXlab platform.
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Characterization and functionality of two members of the SPFH Protein Superfamily, prohibitin 1 and 2 in Leishmania major
Parasites & vectors, 2018Co-Authors: Teresa Cruz-bustos, Ana Karina Ibarrola-vannucci, Isabel Díaz-lozano, José Luis Ramírez, A. OsunaAbstract:Leishmaniasis, a disease caused by parasites of the genus Leishmania, infects roughly 12 million people worldwide, with about two million new cases per year. Prohibitins (PHBs) are highly conserved Proteins belonging to the stomatin-prohibitin flotillin-HflC/K (SPFH) Protein Superfamily. In this study, we examine the potential functions of two Proteins of Leishmania major, PHB1 and PHB2, as well as how they might help protect the protozoan against oxidative stress. By immunolocalization in the parasite cells, PHB1 appeared in the mitochondria and plasma membrane, whereas PHB2 was grouped in the nucleus. When Leishmania cells were under oxidative stress, PHB1 migrates towards the plasma membrane and the paraxial rod, while PHB2 remained in the nucleus and near the kinetoplast. PHB1 presented higher mRNA levels than PHB2 in the amastigotes and the infective metacyclic forms. The mRNA expression of both prohibitins was affected by the presence of the Fe3+ ion. PHBs inhibited the Fenton reaction, where reactive oxygen species could nick DNA, implying that they play a crucial role in controlling oxidative stress. Here, we propose that PHBs may help to protect membranes and DNA against superoxide ions, thus enhancing the survival capacity of the protozoan by controlling the ROS within the phagosome of the macrophages where the parasite multiplies.
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Characterization and functionality of two members of the SPFH Protein Superfamily, prohibitin 1 and 2 in Leishmania major
BMC, 2018Co-Authors: Teresa Cruz-bustos, Ana Karina Ibarrola-vannucci, Isabel Díaz-lozano, José Luis Ramírez, A. OsunaAbstract:Abstract Background Leishmaniasis, a disease caused by parasites of the genus Leishmania, infects roughly 12 million people worldwide, with about two million new cases per year. Prohibitins (PHBs) are highly conserved Proteins belonging to the stomatin-prohibitin flotillin-HflC/K (SPFH) Protein Superfamily. In this study, we examine the potential functions of two Proteins of Leishmania major, PHB1 and PHB2, as well as how they might help protect the protozoan against oxidative stress. Results By immunolocalization in the parasite cells, PHB1 appeared in the mitochondria and plasma membrane, whereas PHB2 was grouped in the nucleus. When Leishmania cells were under oxidative stress, PHB1 migrates towards the plasma membrane and the paraxial rod, while PHB2 remained in the nucleus and near the kinetoplast. PHB1 presented higher mRNA levels than PHB2 in the amastigotes and the infective metacyclic forms. The mRNA expression of both prohibitins was affected by the presence of the Fe3+ ion. PHBs inhibited the Fenton reaction, where reactive oxygen species could nick DNA, implying that they play a crucial role in controlling oxidative stress. Conclusions Here, we propose that PHBs may help to protect membranes and DNA against superoxide ions, thus enhancing the survival capacity of the protozoan by controlling the ROS within the phagosome of the macrophages where the parasite multiplies
Trevor Lithgow - One of the best experts on this subject based on the ideXlab platform.
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A comprehensive analysis of the Omp85/TpsB Protein Superfamily structural diversity, taxonomic occurrence, and evolution
Frontiers in microbiology, 2014Co-Authors: Eva Heinz, Trevor LithgowAbstract:Members of the Omp85/TpsB Protein Superfamily are ubiquitously distributed in Gram-negative bacteria, and function in Protein translocation (e.g., FhaC) or the assembly of outer membrane Proteins (e.g., BamA). Several recent findings are suggestive of a further level of variation in the Superfamily, including the identification of the novel membrane Protein assembly factor TamA and Protein translocase PlpD. To investigate the diversity and the causal evolutionary events, we undertook a comprehensive comparative sequence analysis of the Omp85/TpsB Proteins. A total of 10 Protein subfamilies were apparent, distinguished in their domain structure and sequence signatures. In addition to the Proteins FhaC, BamA, and TamA, for which structural and functional information is available, are families of Proteins with so far undescribed domain architectures linked to the Omp85 β-barrel domain. This study brings a classification structure to a dynamic Protein Superfamily of high interest given its essential function for Gram-negative bacteria as well as its diverse domain architecture, and we discuss several scenarios of putative functions of these so far undescribed Proteins.
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a comprehensive analysis of the omp85 tpsb Protein Superfamily structural diversity taxonomic occurrence and evolution
Frontiers in Microbiology, 2014Co-Authors: Eva Heinz, Trevor LithgowAbstract:Members of the Omp85/TpsB Protein Superfamily are ubiquitously distributed in Gram-negative bacteria, and function in Protein translocation (e.g., FhaC) or the assembly of outer membrane Proteins (e.g., BamA). Several recent findings are suggestive of a further level of variation in the Superfamily, including the identification of the novel membrane Protein assembly factor TamA and Protein translocase PlpD. To investigate the diversity and the causal evolutionary events, we undertook a comprehensive comparative sequence analysis of the Omp85/TpsB Proteins. A total of 10 Protein subfamilies were apparent, distinguished in their domain structure and sequence signatures. In addition to the Proteins FhaC, BamA, and TamA, for which structural and functional information is available, are families of Proteins with so far undescribed domain architectures linked to the Omp85 β-barrel domain. This study brings a classification structure to a dynamic Protein Superfamily of high interest given its essential function for Gram-negative bacteria as well as its diverse domain architecture, and we discuss several scenarios of putative functions of these so far undescribed Proteins.
Johan-owen De Craene - One of the best experts on this subject based on the ideXlab platform.
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Evolutionary analysis of the ENTH/ANTH/VHS Protein Superfamily reveals a coevolution between membrane trafficking and metabolism.
BMC genomics, 2012Co-Authors: Johan-owen De Craene, Raymond Ripp, Odile Lecompte, Julie D. Thompson, Olivier Poch, Sylvie FriantAbstract:Background Membrane trafficking involves the complex regulation of Proteins and lipids intracellular localization and is required for metabolic uptake, cell growth and development. Different trafficking pathways passing through the endosomes are coordinated by the ENTH/ANTH/VHS adaptor Protein Superfamily. The endosomes are crucial for eukaryotes since the acquisition of the endomembrane system was a central process in eukaryogenesis.
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Evolutionary analysis of the ENTH/ANTH/VHS Protein Superfamily reveals a coevolution between membrane trafficking and metabolism.
BMC Genomics, 2012Co-Authors: Johan-owen De Craene, Raymond Ripp, Odile Lecompte, Olivier Poch, Julie Thompson, Sylvie FriantAbstract:ABSTRACT: BACKGROUND: Membrane trafficking involves the complex regulation of Proteins and lipids intracellular localization and is required for metabolic uptake, cell growth and development. Different trafficking pathways passing through the endosomes are coordinated by the ENTH/ANTH/VHS adaptor Protein Superfamily. The endosomes are crucial for eukaryotes since the acquisition of the endomembrane system was a central process in eukaryogenesis. RESULTS: Our in silico analysis of this ENTH/ANTH/VHS Superfamily, consisting of Proteins gathered from 84 complete genomes representative of the different eukaryotic taxa, revealed that genomic distribution of this Superfamily allows to discriminate Fungi and Metazoa from Plantae and Protists. Next, in a four way genome wide comparison, we showed that this discriminative feature is observed not only for other membrane trafficking effectors, but also for Proteins involved in metabolism and in cytokinesis, suggesting that metabolism, cytokinesis and intracellular trafficking pathways co-evolved. Moreover, some of the Proteins identified were implicated in multiple functions, in either trafficking and metabolism or trafficking and cytokinesis, suggesting that membrane trafficking is central to this co-evolution process. CONCLUSION: Our study suggests that membrane trafficking and compartmentalization were not only key features for the emergence of eukaryotic cells but also drove the separation of the eukaryotes in the different taxa.
Alfonso Valencia - One of the best experts on this subject based on the ideXlab platform.
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the ras Protein Superfamily evolutionary tree and role of conserved amino acids
Journal of Cell Biology, 2012Co-Authors: Ana M. Rojas, Gloria Fuentes, Antonio Rausell, Alfonso ValenciaAbstract:The Ras Superfamily is a fascinating example of functional diversification in the context of a preserved structural framework and a prototypic GTP binding site. Thanks to the availability of complete genome sequences of species representing important evolutionary branch points, we have analyzed the composition and organization of this Superfamily at a greater level than was previously possible. Phylogenetic analysis of gene families at the organism and sequence level revealed complex relationships between the evolution of this Protein Superfamily sequence and the acquisition of distinct cellular functions. Together with advances in computational methods and structural studies, the sequence information has helped to identify features important for the recognition of molecular partners and the functional specialization of different members of the Ras Superfamily.
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Evolution: The Ras Protein Superfamily: Evolutionary tree and role of conserved amino acids
The Journal of cell biology, 2012Co-Authors: Ana M. Rojas, Gloria Fuentes, Antonio Rausell, Alfonso ValenciaAbstract:The Ras Superfamily is a fascinating example of functional diversification in the context of a preserved structural framework and a prototypic GTP binding site. Thanks to the availability of complete genome sequences of species representing important evolutionary branch points, we have analyzed the composition and organization of this Superfamily at a greater level than was previously possible. Phylogenetic analysis of gene families at the organism and sequence level revealed complex relationships between the evolution of this Protein Superfamily sequence and the acquisition of distinct cellular functions. Together with advances in computational methods and structural studies, the sequence information has helped to identify features important for the recognition of molecular partners and the functional specialization of different members of the Ras Superfamily.
