Results 191 to 200 of about 25,169 (206)
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Myristoylation Cannot Functionally Replace the Isoprenylation of Rab5

Archives of Biochemistry and Biophysics, 1995
C-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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A sixth sense for Rab5

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 ...
openaire   +1 more source

Rab5 regulates motility of early endosomes on microtubules

Nature Cell Biology, 1999
The small GTPase Rab5 regulates membrane docking and fusion in the early endocytic pathway. Here we reveal a new role for Rab5 in the regulation of endosome interactions with the microtubule network. Using Rab5 fused to green fluorescent protein we show that Rab5-positive endosomes move on microtubules in vivo.
E, Nielsen   +4 more
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Characterization of a RAB5 homologue in Trypanosoma cruzi

Biochemical and Biophysical Research Communications, 2005
RAB 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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Dynamics of rab5 activation in endocytosis and phagocytosis

Journal of Leukocyte Biology, 2000
Abstract 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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Structural basis of Rab5-Rabaptin5 interaction in endocytosis

Nature Structural & Molecular Biology, 2004
Rab5 is a small GTPase that regulates early endosome fusion. We present here the crystal structure of the Rab5 GTPase domain in complex with a GTP analog and the C-terminal domain of effector Rabaptin5. The proteins form a dyad-symmetric Rab5-Rabaptin5(2)-Rab5 ternary complex with a parallel coiled-coil Rabaptin5 homodimer in the middle.
Guangyu, Zhu   +5 more
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Endosome fusion in living cells overexpressing GFP-rab5

Journal of Cell Science, 1999
ABSTRACT CHO and BHK cells which overexpress either wild-type rab5 or rab5:Q79L, a constitutively active rab5 mutant, develop enlarged cytoplasmic vesicles that exhibit many characteristics of early endosomes including immunoreactivity for rab5 and transferrin receptor.
R L, Roberts   +5 more
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Ruffling with Rab5 and RN-tre

Science's STKE, 2004
Lanzetti et al. investigated receptor tyrosine kinase (RTK)-mediated regulation of the actin cytoskeleton and discovered that Rab5, a small guanosine triphosphatase (GTPase) previously implicated in intracellular trafficking, is critical to circular ruffling (an RTK-dependent process that involves cytoskeletal ...
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Ubiquitin Regulation of the Rab5 Family GEF Vps9p

2005
To maintain cellular homeostasis, the levels of transmembrane receptors found on the plasma membrane must be tightly regulated. Endocytosis of activated receptors and the eventual degradation of these transmembrane proteins in the lysosome serve a vital role in maintaining the plasma membrane receptor levels as well as attenuating the downstream ...
Brian A, Davies   +2 more
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Molecular cloning and expression of an avian rab5 homolog

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1998
A chicken rab5 cDNA was isolated that contains the complete open reading frame for a protein of 216 amino acids, which, by comparison with available rab5 sequences from other species, is most closely related to the rab5c isoform. Two rab5 transcripts of 1.3 and 1.8 kb were detectable in various chicken tissues; they are abundant in tissues with high ...
C D, Bojer, F, Wohlrab, N E, Ivessa
openaire   +2 more sources

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