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Papers In Press, published online ahead of print September 7, 2000
J. Biol. Chem, 10.1074/jbc.M006710200
Submitted on July 27, 2000
Accepted on September 6, 2000

A syntaxin 7 homologue is present in Dictyostelium discoideum endosomes and controls their homotypic fusion

Aleksandra Bogdanovic, Franz Bruckert, Takahiro Morio, and Michel Satre

Département de Biologie Moléculaire et Structurale, CEA-Grenoble, Grenoble 38054

Corresponding Author: fbruckert{at}cea.fr

Endo-phagocytic activity is prominent in Dictyostelium discoideum and makes it a good model organism to study the molecular organization of membrane traffic in this pathway. We have identified a syntaxin 7 homologue (26% identity and 54% similarity to human syntaxin 7) in Dictyostelium cDNA and genomic databanks. In addition to the Habc and H3 helices and the C-terminal transmembrane domain characteristic of syntaxins, this protein contains a repetitive N-terminal extension of 68 amino acids. We first showed that Dictyostelium syntaxin 7 was able to form a complex with NSF, a- and g-SNAP. Its intracellular localization was then studied by cell fractionation techniques and magnetic purification of the endocytic compartments. Most of D. discoideum syntaxin 7 is contained in endosomes. Finally, an in vitro endosome homotypic fusion assay (Laurent et al. 1998, J. Biol. Chem. 273: 793-799) was used to study a possible role for syntaxin 7 in this process. Purified anti-syntaxin 7 antibodies and a recombinant soluble fragment of syntaxin 7 both strongly inhibited fusion activity, indicating that this protein was necessary for endosome-endosome fusion. These results demonstrate the importance of this syntaxin 7 homologue in the early phases of Dictyostelium endo-phagocytic pathway.


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