ArticlePloS one2014
Drosophila SNAP-29 is an essential SNARE that binds multiple proteins involved in membrane traffic.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- A look beyond the QR code of SNARE proteins.Protein science : a publication of the Protein Society · 2024Article
- Getting Sugar Coating Right! The Role of the Golgi Trafficking Machinery in Glycosylation.Cells · 2021Review
- Activity of the SNARE Protein SNAP29 at the Endoplasmic Reticulum and Golgi Apparatus.Frontiers in cell and developmental biology · 2021Article
- Review
- VAMP3/Syb and YKT6 are required for the fusion of constitutive secretory carriers with the plasma membrane.PLoS genetics · 2017Article
- Dedicated SNAREs and specialized TRIM cargo receptors mediate secretory autophagy.The EMBO journal · 2017Article
- TSSC1 is novel component of the endosomal retrieval machinery.Molecular biology of the cell · 2016Article
Corrections and comments
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Authors and funding
5 authors.
Funding
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.
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Registered trials
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