title: Drosophila SNAP-29 is an essential SNARE that binds multiple proteins involved in membrane traffic.
abstract: 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.
authors.affiliation: Department of Biological Sciences, University of Southern Mississippi, Hattiesburg, Mississippi, United States of America.
authors.forename: Hao
authors.initials: H
authors.lastname: Xu
authors.affiliation: Department of Immunology, Sunnybrook Research Institute, Toronto, Ontario, Canada.
authors.forename: Mahmood
authors.initials: M
authors.lastname: Mohtashami
authors.affiliation: Department of Biology, University of Toronto Mississauga, Mississauga, Ontario, Canada.
authors.forename: Bryan
authors.initials: B
authors.lastname: Stewart
authors.affiliation: Developmental and Stem Cell Biology Program, Hospital for Sick Children, and Department of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada.
authors.forename: Gabrielle
authors.initials: G
authors.lastname: Boulianne
authors.affiliation: Cell Biology Program, Hospital for Sick Children, and Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada.
authors.forename: William S
authors.initials: WS
authors.lastname: Trimble
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D003433:Crosses, Genetic; D029721:Drosophila Proteins / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D010641:Phenotype; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D034622:RNA Interference; D050600:SNARE Proteins / Q000378:metabolism*; D050827:Syntaxin 1 / Q000378:metabolism; D051438:Syntaxin 16 / Q000378:metabolism
chemical_list: D029721:Drosophila Proteins; D050600:SNARE Proteins; C582206:Snap29 protein, Drosophila; D050827:Syntaxin 1; D051438:Syntaxin 16