Results 141 to 150 of about 14,125 (185)
Altered Intracellular Trafficking as a Mechanism for Prolonged Duration of G Protein-Coupled Receptor Activation. [PDF]
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Dimerization of small GTPase Rab5
International Journal of Molecular Medicine, 2001Rab proteins are small GTPases, localized to distinct cellular compartments, regulating specific steps of intracellular membrane trafficking. One member of the Rab family, Rab5, consists of three isoforms, Rab5a, Rab5b, and Rab5c, which have been shown to play an important role in early events of endocytosis.
H, Daitoku +4 more
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Dynamics of rab5 activation in endocytosis and phagocytosis
Journal of Leukocyte Biology, 2000Abstract Fluid-phase endocytosis is stimulated by H-ras-linked growth factor receptors and this stimulation requires activation of rab5. We utilized a GFP-rab5a:wt fusion protein to monitor GFP-rab5a:wt activation in living fibroblasts and in J774 macrophages.
R L, Roberts +3 more
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Rab5 in the Regulation of Cell Motility and Invasion
Current Protein & Peptide Science, 2011Cellular invasion requires careful regulation of the cell migration and apoptotic signaling cascades, allowing cell movement and survival of the emigrating populations. Components of the endosomal machinery are involved in these processes, and in particular the role of small GTPases of the Rab family has become appreciated.
Vicente A, Torres, Dwayne G, Stupack
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Trends in Cell Biology, 2000
The Rab proteins (Ypt in budding yeast) comprise the largest branch of the Ras family of GTPases and are involved in the trafficking of membranous compartments within a cell. Like Ras, they possess a molecular on/off switch. The activated protein is GTP bound, whereas the inactive one is GDP bound.
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The Rab proteins (Ypt in budding yeast) comprise the largest branch of the Ras family of GTPases and are involved in the trafficking of membranous compartments within a cell. Like Ras, they possess a molecular on/off switch. The activated protein is GTP bound, whereas the inactive one is GDP bound.
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Characterization of a RAB5 homologue in Trypanosoma cruzi
Biochemical and Biophysical Research Communications, 2005RAB proteins are small GTPases involved in exocytic and endocytic pathways of eukaryotic cells, controlling vesicle docking and fusion. RABs show a remarkable specificity in subcellular localization, so they can be used as molecular markers for studying protein trafficking in Trypanosoma cruzi, the causal agent of Chagas' disease.
Júlia Rolão, Araripe +7 more
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1994
Abstract Rab5 has been identified by screening cDNA libraries with degenerate oligonucleotides corresponding to the sequence WDTAGQE shared by members of the Ypt1/Sec4/rab subfamily45. The DNA sequence of canine rab5 (GenBank accession number M35520) predicts a pro tein with a molecular mass of 23,658 Daltons.
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Abstract Rab5 has been identified by screening cDNA libraries with degenerate oligonucleotides corresponding to the sequence WDTAGQE shared by members of the Ypt1/Sec4/rab subfamily45. The DNA sequence of canine rab5 (GenBank accession number M35520) predicts a pro tein with a molecular mass of 23,658 Daltons.
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Control of Rab5 and Rab7 Expression by the Isoprenoid Pathway
Biochemical and Biophysical Research Communications, 1998Rab proteins are small molecular mass GTP-ases involved in the regulation of vescicular transport. The ability of rab proteins to carry out their role in intracellular membrane traffic requires the post-translational attachment to their C-terminus of a geranylgeranyl group, an isoprenoid lipid moiety derived from mevalonate.
LAEZZA, CHIARA +4 more
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Nature Cell Biology, 2005
It has long been known that the mammalian small GTPase Rab5 is involved in clathrin-mediated endocytosis. However, most Rab5-interacting proteins are localized to endosomes rather than to the plasma membrane. A newly discovered nucleotide-exchange factor for Rab5 in Caenorhabditis elegans now provides the missing link for activating Rab5 at the plasma ...
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It has long been known that the mammalian small GTPase Rab5 is involved in clathrin-mediated endocytosis. However, most Rab5-interacting proteins are localized to endosomes rather than to the plasma membrane. A newly discovered nucleotide-exchange factor for Rab5 in Caenorhabditis elegans now provides the missing link for activating Rab5 at the plasma ...
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