Evolution of the Rab family of small GTP-binding proteins.
@article{PereiraLeal2001EvolutionOT, title={Evolution of the Rab family of small GTP-binding proteins.}, author={Jos{\'e} B. Pereira-Leal and Miguel C. Seabra}, journal={Journal of molecular biology}, year={2001}, volume={313 4}, pages={ 889-901 } }
Rab proteins are small GTP-binding proteins that form the largest family within the Ras superfamily. Rab proteins regulate vesicular trafficking pathways, behaving as membrane-associated molecular switches. Here, we have identified the complete Rab families in the Caenorhabditis elegans (29 members), Drosophila melanogaster (29), Homo sapiens (60) and Arabidopsis thaliana (57), and we defined criteria for annotation of this protein family in each organism. We studied sequence conservation…
785 Citations
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A bioinformatics approach was taken to identify and classify the complete C. elegans Rab family placing individual Rabs into specific subfamilies based on molecular phylogenetics, and a molecular toolset was created to facilitate research on biological processes that involve Rab proteins.
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Analysis supports a scenario where Rabs differentiated into an independent family in Archaea, interacting with proteins involved in membrane biogenesis and provides a new insight into the intermediate stages and the evolutionary path toward the complex membrane-associated signaling circuits that characterize the Ras superfamily of small GTPases, and specifically Rab proteins.
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Comparative analysis of the amino acid sequences and the three-dimensional electrostatic and hydrophobic molecular interaction fields of 62 human Rab proteins revealed a wide range of binding properties with large differences between some Rab proteins.
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The presence of many Rab7 and Rab9 isoforms suggests their functional specialization and complexity of subcellular trafficking even in unicellular eukaryotes, as well as finding a phylogenetic signal and inferred evolutionary relationships between them.
Chapter 5: rab proteins and their interaction partners.
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- 2002
Data suggest that RABRP1 is involved in the lysosomal vesicle transport pathway, including the biogenesis or degradation of pigment granules in photoreceptor and pigment cells in the retina.
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Phylogenetic analyses of amino acid sequence of Rab GTPases suggest their segregation into subfamilies on the basis of their localization and/or function in membrane trafficking.
Methods to Study the Unique SOCS Box Domain of the Rab40 Small GTPase Subfamily.
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An unbiased approach to identify potential Rab40b/Cullin5 substrates is described and it is anticipated that this method will be useful for studying the function of other Rab40 family members as well as other SOCS box containing proteins.
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This work proposes a model whereby an effector binds to RabF (switch) regions to discriminate between nucleotide-bound states and simultaneously to other regions that confer specificity to the interaction, possibly Rab subfamily (RabSF) specific regions that are defined here.
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The present studies indicate that Rab24 possesses several unusual characteristics that distinguish it from other Rab proteins, indicating that, if Rab24 functions in vesicular transport processes, it may operate through a novel mechanism that does not depend on GTP hydrolysis or GDP dissociation inhibitor-mediated recycling.
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It is suggested that in the absence of Rab binding, REP interaction with RabGG transferase is maintained through Rab-independent binding sites, providing a molecular explanation for the kinetic properties of Rab prenylation in vitro.
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Rab proteins, members of the Ras superfamily of small GTPases, play regulatory roles in intercompartmental vesicular transport, and binding sites for multiple transcription factors are found in the TATA-less promoter region.
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The isolation of this gene will aid in the dissection of the machinery involved in soluble protein sorting at the trans-Golgi network of plants and was able to complement the temperature-sensitive phenotype of the YPT6 null mutant in yeast.
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The Rab family is part of the Ras superfamily of small GTPases, which regulate vesicle formation, actin- and tubulin-dependent vesicles movement, and membrane fusion in yeast and humans.
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This work purified a GEP from rat brain with lipid-modified Rab3A as a substrate and found that Rab3 GEP was expressed in all the rat tissues examined with the highest expression in brain, and showed a minimum molecular mass on SDS-polyacrylamide gel electrophoresis.
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It is suggested that at least three members of the rab family use GTP hydrolysis to regulate components of the transport machinery involved in vesicle traffic between early compartments of the secretory pathway.