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Vol. 11, Issue 9, 3137-3153, September 2000
¶
*Wellcome Trust Centre for Molecular Mechanisms in Disease,
University of Cambridge, Addenbrooke's Hospital, Cambridge CB2 2XY,
United Kingdom; Protein traffic from the cell surface or the
trans-Golgi network reaches the lysosome via a series of
endosomal compartments. One of the last steps in the endocytic pathway
is the fusion of late endosomes with lysosomes. This process has been
reconstituted in vitro and has been shown to require NSF, Department of Physiology and Biophysics,
University of Iowa, Iowa City, Iowa 52242; Department of
Physiology, University of Queensland, Brisbane, Queensland 4068, Australia; §Lysosomal Diseases Research Unit, Department
of Chemical Pathology, Women's and Children's Hospital, North
Adelaide, South Australia 5006, Australia; and Institute
of Molecular and Cellular Biology, University of Queensland, Brisbane,
Queensland 4068, Australia
and 
SNAP, and a Rab GTPase based on inhibition by Rab GDI. In
Saccharomyces cerevisiae, fusion events to the
lysosome-like vacuole are mediated by the syntaxin protein Vam3p, which
is localized to the vacuolar membrane. In an effort to identify the
molecular machinery that controls fusion events to the lysosome, we
searched for mammalian homologues of Vam3p. One such candidate is
syntaxin 7. Here we show that syntaxin 7 is concentrated in late
endosomes and lysosomes. Coimmunoprecipitation experiments show that
syntaxin 7 is associated with the endosomal v-SNARE Vamp 8, which
partially colocalizes with syntaxin 7. Importantly, we show that
syntaxin 7 is specifically required for the fusion of late endosomes
with lysosomes in vitro, resulting in a hybrid organelle. Together,
these data identify a SNARE complex that functions in the late
endocytic system of animal cells.
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