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Preferential association of syntaxin 8 with the early endosome
V.N. Subramaniam, E. Loh, H. Horstmann, A. Habermann, Y. Xu, J. Coe, G. Griffiths, W. Hong
J Cell Sci 2000 113: 997-1008;
V.N. Subramaniam
Membrane Biology Laboratory, Institute of Molecular and Cell Biology, Singapore 117609, Singapore.
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E. Loh
Membrane Biology Laboratory, Institute of Molecular and Cell Biology, Singapore 117609, Singapore.
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H. Horstmann
Membrane Biology Laboratory, Institute of Molecular and Cell Biology, Singapore 117609, Singapore.
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A. Habermann
Membrane Biology Laboratory, Institute of Molecular and Cell Biology, Singapore 117609, Singapore.
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Y. Xu
Membrane Biology Laboratory, Institute of Molecular and Cell Biology, Singapore 117609, Singapore.
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J. Coe
Membrane Biology Laboratory, Institute of Molecular and Cell Biology, Singapore 117609, Singapore.
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G. Griffiths
Membrane Biology Laboratory, Institute of Molecular and Cell Biology, Singapore 117609, Singapore.
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W. Hong
Membrane Biology Laboratory, Institute of Molecular and Cell Biology, Singapore 117609, Singapore.
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Summary

Members of the syntaxin family play a fundamental role in vesicle docking and fusion of diverse transport events. We have molecularly characterized syntaxin 8, a novel member of the syntaxin family. The nucleotide sequence of cloned rat cDNA predicts a polypeptide of 236 residues with a carboxyl-terminal 18-residue hydrophobic domain that may function as a membrane anchor. Characteristic of syntaxins, syntaxin 8 also contain regions that have the potential to form coiled-coil structures. Among the known syntaxins, syntaxin 8 is most homologous to syntaxin 6 which is predominantly associated with the trans-Golgi network (TGN). The syntaxin 8 transcript is detected in all rat tissues examined by northern blot. Antibodies against recombinant syntaxin 8 recognize a 27 kDa protein that is enriched in membrane fractions containing the Golgi apparatus and the endosomal/lysosomal compartments. Syntaxin 8 in membrane extract could be incorporated into a 20S protein complex in a way that is dependent on the soluble N-ethylmaleimide-sensitive factor (NSF) and soluble NSF attachment protein ((alpha)-SNAP), suggesting that syntaxin 8 is indeed a SNAP receptor (SNARE). Indirect immunofluorescence microscopy reveals that the majority of syntaxin 8 is localized to the early endosome marked by Rab5. This is corroborated by immunogold labeling experiments showing enrichment of syntaxin 8 in the early endosome and its co-labeling with Rab5.

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Preferential association of syntaxin 8 with the early endosome
V.N. Subramaniam, E. Loh, H. Horstmann, A. Habermann, Y. Xu, J. Coe, G. Griffiths, W. Hong
J Cell Sci 2000 113: 997-1008;
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Preferential association of syntaxin 8 with the early endosome
V.N. Subramaniam, E. Loh, H. Horstmann, A. Habermann, Y. Xu, J. Coe, G. Griffiths, W. Hong
J Cell Sci 2000 113: 997-1008;

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