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Vol. 12, Issue 6, 1699-1709, June 2001
Secretory Pathway Laboratory, Imperial Cancer Research Fund, London
WC2A 3PX, UK
Homotypic fusion of immature secretory granules (ISGs) gives rise
to mature secretory granules (MSGs), the storage compartment in
endocrine and neuroendocrine cells for hormones and neuropeptides. With
the use of a cell-free fusion assay, we investigated which soluble
N-ethylmaleimide-sensitive fusion protein attachment receptor (SNARE)
molecules are involved in the homotypic fusion of ISGs. Interestingly,
the SNARE molecules mediating the exocytosis of MSGs in neuroendocrine
cells, syntaxin 1, SNAP-25, and VAMP2, were not involved in homotypic
ISG fusion. Instead, we have identified syntaxin 6 as a component of
the core machinery responsible for homotypic ISG fusion. Subcellular
fractionation studies and indirect immunofluorescence microscopy show
that syntaxin 6 is sorted away during the maturation of ISGs to MSGs.
Although, syntaxin 6 on ISG membranes is associated with SNAP-25 and
SNAP-29/GS32, we could not find evidence that these target (t)-SNARE
molecules are involved in homotypic ISG fusion. Nor could we find any
involvement for the vesicle (v)-SNARE VAMP4, which is known to be
associated with syntaxin 6. Importantly, we have shown that homotypic
fusion requires the function of syntaxin 6 on both donor as well as
acceptor membranes, which suggests that t-t-SNARE interactions, either direct or indirect, may be required during fusion of ISG membranes.
Corresponding author: Secretory Pathway Laboratory,
Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, London WC2A
3PX, UK. E-mail: tooze{at}icrf.icnet.uk.
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