[Study of the mechanism of Ras-dva small GTPase intracellular localization].
An analysis of amino acid sequences of small GTPases of the Ras-dva family allowed us to determine the C-terminal prenylation motif, which could be responsible for the membrane localization of these proteins. We demonstrated using in vivo EGFP tracing that the Ras-dva small GTPases from Xenopus laevis embryo cells and NIH-3T3 fibroblasts are localized on both plasma membranes and endomembranes (the endoplasmic reticulum, the Golgi apparatus, and vesicles). At the same time, the replacement of the Cys residue, the SH group of which must be theoretically farnesylated, in the C-terminal prenylation motif of the Ras-dva small GTPase by the Ser residue prevented the membrane localization of the protein. These results indicate that the C-terminal prenylation site is critical for the membrane localization of small Ras-dva GTPases.
M B
MB
Tereshina
V V
VV
Belousov
A G
AG
Zaraĭskiĭ
D000595:Amino Acid Sequence; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology*; D049452:Green Fluorescent Proteins / Q000032:analysis / Q000235:genetics; D007425:Intracellular Membranes / Q000201:enzymology*; D051379:Mice; D008969:Molecular Sequence Data; D020559:Monomeric GTP-Binding Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D041681:NIH 3T3 Cells; D017368:Protein Prenylation; D029867:Xenopus Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism*
D029867:Xenopus Proteins; C485184:enhanced green fluorescent protein; D049452:Green Fluorescent Proteins; D020559:Monomeric GTP-Binding Proteins; C509608:ras-dva1 protein, Xenopus