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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Motifs
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Amino Acid Sequence
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Animals
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Endocytosis
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Endosomes / metabolism*
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Gene Expression Regulation, Fungal*
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Golgi Apparatus / metabolism
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Humans
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Kinetics
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Liposomes / chemistry
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Membrane Proteins / chemistry
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Membrane Proteins / metabolism
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Molecular Sequence Data
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Mutation
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Peptides / chemistry
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Plasmids / metabolism
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Protein Structure, Tertiary
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Qa-SNARE Proteins
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R-SNARE Proteins
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Recombinant Fusion Proteins / chemistry
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SNARE Proteins
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Time Factors
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Vesicular Transport Proteins / chemistry*
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Yeasts / metabolism
Substances
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Liposomes
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Membrane Proteins
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Peptides
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Qa-SNARE Proteins
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R-SNARE Proteins
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Recombinant Fusion Proteins
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SNARE Proteins
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VAMP8 protein, human
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Vesicular Transport Proteins