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Vol. 10, Issue 11, 3891-3908, November 1999
and
*Howard Hughes Medical Institute, Department of Molecular and
Cellular Physiology, Stanford University School of Medicine, Stanford,
California 94305-5428; and To understand molecular mechanisms that regulate the intricate and
dynamic organization of the endosomal compartment, it is important to
establish the morphology, molecular composition, and functions of the
different organelles involved in endosomal trafficking. Syntaxins and
vesicle-associated membrane protein (VAMP) families, also known as
soluble N-ethylmaleimide-sensitive factor (NSF)
attachment protein receptors (SNAREs), have been implicated in
mediating membrane fusion and may play a role in determining the
specificity of vesicular trafficking. Although several SNAREs,
including VAMP3/cellubrevin, VAMP8/endobrevin, syntaxin 13, and
syntaxin 7, have been localized to the endosomal membranes, their
precise localization, biochemical interactions, and function remain
unclear. Furthermore, little is known about SNAREs involved in
lysosomal trafficking. So far, only one SNARE, VAMP7, has been
localized to late endosomes (LEs), where it is proposed to mediate
trafficking of epidermal growth factor receptor to LEs and lysosomes.
Here we characterize the localization and function of two additional
endosomal syntaxins, syntaxins 7 and 8, and propose that they mediate
distinct steps of endosomal protein trafficking. Both syntaxins are
found in SNARE complexes that are dissociated by Medical School, University of
Utrecht, Institute for Biomembranes, 3584CX Utrecht, The Netherlands
-soluble NSF
attachment protein and NSF. Syntaxin 7 is mainly localized to
vacuolar early endosomes (EEs) and may be involved in protein
trafficking from the plasma membrane to the EE as well as in homotypic
fusion of endocytic organelles. In contrast, syntaxin 8 is likely to
function in clathrin-independent vesicular transport and membrane
fusion events necessary for protein transport from EEs to LEs.
These authors contributed equally to this work.
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