Abstract
In yeast, the assembly of the target (t)-SNAREs [Tlg2p/Tlg1p,Vti1p] and [Pep12p/Tlg1p,Vti1p] with the vesicular (v)-SNARE Snc2p promotes endocytic fusion. Here, selected mutations and truncations of SNARE proteins were tested in an in vitro fusion assay to identify potential regulatory regions in these proteins, and two distinct regions were found. The first is represented by the combined effect of the three t-SNARE N-terminal regions and the second is located within the Tlg1p SNARE motif. These internal controls provide a potential mechanism to enable SNARE-dependent fusion to be regulated.
Highlights
The core mechanism of SNARE1 (soluble N-ethylmaleimidesensitive factor (NSF) attachment protein (SNAP) receptor)mediated fusion is strikingly simple: a target-SNARE generates fusion only with its cognate vesicularSNARE (v-SNARE) [1,2,3,4,5]
The first is represented by the combined effect of the three t-SNARE N-terminal regions and the second is located within the Tlg1p SNARE motif
It has been demonstrated that such peptides are able to bind and restructure t-SNARE complexes [23]
Summary
The core mechanism of SNARE1 (soluble N-ethylmaleimidesensitive factor (NSF) attachment protein (SNAP) receptor)mediated fusion is strikingly simple: a target-SNARE (tSNARE) generates fusion only with its cognate vesicularSNARE (v-SNARE) [1,2,3,4,5]. The N-terminal Domains of the t-SNARE Constitute a Potential Regulatory Switch—Both yeast endocytic t-SNAREs, [Tlg2p/Tlg1p,Vti1p] and [Pep12p/Tlg1p,Vti1p], must be activated to promote fusion of liposomes [4, 5]. These Nterminal extensions are neither homologous to each other nor to other SNAREs. To study their influence on fusion, we generated t-SNARE constructs in which one or more of these N-terminal domains could be removed by thrombin cleavage.
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