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Science 27 March 1992:
Vol. 255. no. 5052, pp. 1695 - 1697
DOI: 10.1126/science.1348148
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Articles
Science, Vol 255, Issue 5052, 1695-1697
Copyright © 1992 by American Association for the Advancement of Science
Evidence of a role for heterotrimeric GTP-binding proteins in endosome fusion
MI Colombo,
LS Mayorga,
PJ Casey,
and
PD Stahl
Department of Cell Biology and Physiology, Washington University, School of Medicine, St. Louis, MO 63110.
Guanosine triphosphate (GTP)-binding proteins are required for intracellular vesicular transport. Mastoparan is a peptide component of wasp venom that increases nucleotide exchange in some classes of G alpha subunits of regulatory heterotrimeric GTP-binding proteins (G proteins). Mastoparan and other compounds that increase nucleotide exchange by G proteins inhibited endosome fusion in vitro and reversed the effects of guanosine 5'-O-(3-thiotriphosphate) (GTP-gamma-S), a nonhydrolyzable GTP analog. Addition of beta gamma subunits of G proteins to the fusion assay antagonized the stimulatory effect of GTP-gamma-S, confirming the participation of G proteins. These results indicate that GTP-binding proteins are required for endosome fusion and in particular that a G protein is involved. Given the function of G proteins in signal transduction, these findings may provide insight into the mechanism by which endosomal vesicles become competent for fusion after their formation at the cell surface.
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