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J. Biol. Chem., Vol. 275, Issue 47, 36691-36697, November 24, 2000

This Article Full Text Full Text (PDF) All Versions of this Article: 275/47/36691    most recent M006710200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Bogdanovic, A. Articles by Satre, M. Search for Related Content PubMed PubMed Citation Articles by Bogdanovic, A. Articles by Satre, M. Social Bookmarking                      What's this?

A Syntaxin 7 Homologue Is Present in Dictyostelium discoideum Endosomes and Controls Their Homotypic Fusion^*

Aleksandra Bogdanovic^§, Franz Bruckert, Takahiro Morio^¶, and Michel Satre

From the From the  Laboratoire de Biochimie et Biophysique des Systèmes Intégrés, Département de Biologie Moléculaire et Structurale, 38054 Grenoble Cedex 9, France and the ^¶ Institute of Biological Sciences, University of Tsukuba, Ibaraki 305-0006, Japan

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 data banks. 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 N-ethylmaleimide-sensitive fusion protein and - and -soluble N-ethylmaleimide-sensitive fusion protein attachment protein. 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, O., Bruckert, F., Adessi, C., and Satre, M. (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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