Results 151 to 160 of about 14,125 (185)

The SAC, EEA1, Rab5 and endosome fusion

Trends in Cell Biology, 1999
The 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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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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Characterization of Rab5:Q79L-Stimulated Endosome Fusion

Archives of Biochemistry and Biophysics, 1996
Fusion 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, G, Li, L S, Mayorga, P D, Stahl   +3 more
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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, F, Severin, J M, Backer, A A, Hyman, M, Zerial   +4 more
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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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Regulation of endocytosis by the small GTP-ase Rab5

Cytotechnology, 1993
Rab5 is a small GTPase associated with the plasma membrane and the early endosomes. Expression of wild type rab5 and a mutant protein defective in GTP-binding in BHK cells led to alterations in the rate of endocytosis and in the morphology of endocytic organelles.
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A Window into the Dynamics of Rab5 Activity

Science Signaling, 2008
The small guanosine triphosphatase (GTPase) Rab5, known for its role in early endocytosis, has also been implicated in the engulfment of apoptotic cells, a process important in limiting the inflammatory response. Kitano et al .
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rab5 controls early endosome fusion in vitro

Cell, 1991
The 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, P, Chavrier, M, Zerial, J, Gruenberg   +3 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
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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, Peng, Zhai, Jian, Liu, Simon, Terzyan, Guangpu, Li, Xuejun C, Zhang   +5 more
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