Drosophila SNAP-29 is an essential SNARE that binds multiple proteins involved in membrane traffic.
Each membrane fusion event along the secretory and endocytic pathways requires a specific set of SNAREs to assemble into a 4-helical coiled-coil, the so-called trans-SNARE complex. Although most SNAREs contribute one helix to the trans-SNARE complex, members of the SNAP-25 family contribute two helixes. We report the characterization of the ... Drosophila homologue of SNAP-29 (dSNAP-29), which is expressed throughout development. Unlike the other SNAP-25 like proteins in fruit fly (i.e., dSNAP-25 and dSNAP-24), which form SDS-resistant SNARE complexes with their cognate SNAREs, dSNAP-29 does not participate in any SDS-resistant complexes, despite its interaction with dsyntaxin1 and dsyntaxin16 in vitro. Immunofluorescence studies indicated that dSNAP-29 is distributed in various tissues, locating in small intracellular puncta and on the plasma membrane, where it associates with EH domain-containing proteins implicated in the endocytic pathway. Overexpression and RNAi studies suggested that dSNAP-29 mediates an essential process in Drosophila development.
Mesh Terms:
Animals, Cell Membrane, Crosses, Genetic, Drosophila Proteins, Drosophila melanogaster, Microscopy, Fluorescence, Phenotype, Protein Binding, Protein Structure, Tertiary, RNA Interference, SNARE Proteins, Syntaxin 1, Syntaxin 16
Animals, Cell Membrane, Crosses, Genetic, Drosophila Proteins, Drosophila melanogaster, Microscopy, Fluorescence, Phenotype, Protein Binding, Protein Structure, Tertiary, RNA Interference, SNARE Proteins, Syntaxin 1, Syntaxin 16
PLoS ONE
Date: Mar. 15, 2014
PubMed ID: 24626111
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