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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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rab5 controls early endosome fusion in vitro
Cell, 1991The small GTP-binding protein rab5 was previously localized on early endosomes and on the cytoplasmic face of the plasma membrane. Using a cell-free assay, we have now tested whether rab5 is involved in controlling an early endocytic fusion event. Fusion could be inhibited by cytosol containing the overexpressed mutant rab5lle133, which does not bind ...
J P, Gorvel +3 more
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Characterization of Rab5:Q79L-Stimulated Endosome Fusion
Archives of Biochemistry and Biophysics, 1996Fusion of intracellular membrane-bound compartments is a common step in the transport of macromolecules along the endocytic and secretory pathways. Previous work has shown that GTP gamma S stimulates endosome fusion in the presence of low concentrations of cytosol.
M A, Barbieri +3 more
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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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The SAC, EEA1, Rab5 and endosome fusion
Trends in Cell Biology, 1999The information that might help distinguish how the sub-apical compartment relates to apical recycling endosomes includes whether it carries other endosomal markers. One such marker, normally associated with early endosomes, is EEA1. This is a Ptdins(3)P-binding protein involved in regulating endosomal traffic (for a review, see Ref. 1xCorvera, S.
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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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Myristoylation Cannot Functionally Replace the Isoprenylation of Rab5
Archives of Biochemistry and Biophysics, 1995C-terminal isoprenylation is necessary for the small GTPase Rab5 to associate with early endosomes and to exert its regulatory function in endocytosis. In this study, we tested whether Rab5 could retain its membrane association and biological function if the isoprenylation were replaced by another type of lipid modification (myristoylation).
G, Li, M A, Barbieri, P D, Stahl
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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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