t-SNARE activation through transient interaction with a rab-like guanosine triphosphatase.
Intracellular vesicle targeting involves the interaction of vesicle proteins, termed v-SNAREs, with target membrane proteins, termed t-SNAREs. Assembly of v-SNARE-t-SNARE targeting complexes is modulated by members of the Sec1-Sly1 protein family, and by small guanosine triphosphatases termed Rabs. The interactions of these proteins during assembly of the endoplasmic reticulum-to-Golgi targeting ... complex in Saccharomyces cerevisiae were studied. The data suggest that the Rab protein Ypt1p transiently interacts with the t-SNARE Sed5p and results in displacement of the negative regulator Sly1p, allowing subsequent formation of the v-SNARE-t-SNARE targeting complex.
Mesh Terms:
Biological Transport, Carrier Proteins, Endoplasmic Reticulum, Fungal Proteins, GTP Phosphohydrolases, GTP-Binding Proteins, Golgi Apparatus, Membrane Proteins, Models, Biological, Munc18 Proteins, Plant Proteins, Precipitin Tests, Protein Binding, Qa-SNARE Proteins, SNARE Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Vesicular Transport Proteins, rab GTP-Binding Proteins
Biological Transport, Carrier Proteins, Endoplasmic Reticulum, Fungal Proteins, GTP Phosphohydrolases, GTP-Binding Proteins, Golgi Apparatus, Membrane Proteins, Models, Biological, Munc18 Proteins, Plant Proteins, Precipitin Tests, Protein Binding, Qa-SNARE Proteins, SNARE Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Vesicular Transport Proteins, rab GTP-Binding Proteins
Science
Date: May. 23, 1997
PubMed ID: 9157884
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