ArticleProceedings of the National Academy of Sciences of the United States of America2011
Epsin N-terminal homology domains bind on opposite sides of two SNAREs.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Structure of a membrane tethering complex incorporating multiple SNAREs.Nature structural & molecular biology · 2024Article
- Structural basis for the binding of SNAREs to the multisubunit tethering complex Dsl1.The Journal of biological chemistry · 2020Article
- Intracellular Trafficking Mechanisms of Synaptic Dysfunction in Alzheimer's Disease.Frontiers in cellular neuroscience · 2020Article
- A mechanism for differential sorting of the planar cell polarity proteins Frizzled6 and Vangl2 at theThe Journal of biological chemistry · 2018Article
- Endomembrane-associated RSD-3 is important for RNAi induced by extracellular silencing RNA in both somatic and germ cells of Caenorhabditis elegans.Scientific reports · 2016Article
- The lipid composition and physical properties of the yeast vacuole affect the hemifusion-fusion transition.Traffic (Copenhagen, Denmark) · 2013Article
- Importance of the N-terminal domain of the Qb-SNARE Vti1p for different membrane transport steps in the yeast endosomal system.PloS one · 2013Article
- Article
- Phosphoinositide-mediated clathrin adaptor progression at the trans-Golgi network.Nature cell biology · 2012Article
- Structural basis for type VI secretion effector recognition by a cognate immunity protein.PLoS pathogens · 2012Article
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Authors and funding
8 authors.
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No grant is acknowledged in the PubMed record.
Abstract
SNARE proteins are crucial for membrane fusion in vesicular transport. To ensure efficient and accurate fusion, SNAREs need to be sorted into different budding vesicles. This process is usually regulated by specific recognition between SNAREs and their adaptor proteins. How different pairs of SNAREs and adaptors achieve their recognition is unclear. Here, we report the recognition between yeast SNARE Vti1p and its adaptor Ent3p derived from three crystal structures. Surprisingly, this yeast pair Vti1p/Ent3p interacts through a distinct binding site compared to their homologues vti1b/epsinR in mammals. An opposite surface on Vti1p_Habc domain binds to a conserved area on the epsin N-terminal homology (ENTH) domain of Ent3p. Two-hybrid, in vitro pull-down and in vivo experiments indicate this binding interface is important for correct localization of Vti1p in the cell. This previously undescribed discovery that a cargo and adaptor pair uses different binding sites across species suggests the diversity of SNARE-adaptor recognition in vesicular transport.
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