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PMID: 2519610 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

GTP gamma S stimulation of endosome fusion suggests a role for a GTP-binding protein in the priming of vesicles before fusion.

Cell regulation ·Vol. 1 ·No. 1 ·1989-11-00 ·Pages 113-24

Mayorga LS, Diaz R, Colombo MI, Stahl PD

Abstract

Guanosine 5'-(3-O-thio)triphosphate (GTP gamma S), a non-hydrolyzable analogue of GTP, inhibits in vitro fusion among early endocytic vesicles in the presence of high concentrations of cytosol. In this report we show that fusion is remarkably stimulated by GTP gamma S under conditions where cytosolic components are the limiting factors for the process. The amount of cytosolic factors required for maximal fusion activity is several-fold decreased by the presence of GTP gamma S. Moreover, preincubation of vesicles in the presence of cytosol and GTP gamma S allows fusion to proceed even in the absence of cytosol. Our results indicate that a GTP-binding protein facilitates the binding of cytosolic factor(s) required for endosome fusion to the endosomal membrane and stabilizes a dilution-resistant intermediate of the fusion process.

MeSH Terms
Animals Clone Cells Cytosol/metabolism Endocytosis/drug effects,physiology GTP-Binding Proteins/metabolism Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology Kinetics Membrane Fusion/drug effects,physiology Microscopy, Electron
Chemicals
Guanosine 5'-O-(3-Thiotriphosphate) GTP-Binding Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Mayorga L S
Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110.
Diaz R
Colombo M I
Stahl P D
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Article Info
Journal
Cell regulation
Abbr.
Cell Regul
ISSN
1044-2030
Published
1989-11-00
Pages
113-24
Language
English
Region
United States
NLM ID
9005331
PMCID
PMC361430
Subset
IM
Grants
NIAID NIH HHS · AI 20015 · United States
NCI NIH HHS · CA 12858 · United States
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