ArticleStructure (London, England : 1993)2013
Structural basis for the interaction of the Golgi-Associated Retrograde Protein Complex with the t-SNARE Syntaxin 6.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 32 citations in OpenAlex.
- Deconvolution of the On-Target Activity of Plasmepsin V Peptidomimetics inACS infectious diseases · 2025Article
- A proximity map of RAB GTPases delineates roles for RAB14 in EARP complex and UHRF1BP1 endosomal recruitments.Communications biology · 2025Article
- Acute GARP depletion disrupts vesicle transport, leading to severe defects in sorting, secretion, and O-glycosylation.bioRxiv : the preprint server for biology · 2024Article
- Structure of a membrane tethering complex incorporating multiple SNAREs.Nature structural & molecular biology · 2024Article
- Role of GARP Vesicle Tethering Complex in Golgi Physiology.International journal of molecular sciences · 2023Review
- LRRK2 recruitment, activity, and function in organelles.The FEBS journal · 2022Review
- Neuronal SNARE complex assembly guided by Munc18-1 and Munc13-1.FEBS open bio · 2022Review
- SHIP164 is a chorein motif lipid transfer protein that controls endosome-Golgi membrane traffic.The Journal of cell biology · 2022Article
- SNARE proteins: zip codes in vesicle targeting?The Biochemical journal · 2022Review
- Structural basis for the binding of SNAREs to the multisubunit tethering complex Dsl1.The Journal of biological chemistry · 2020Article
- The inner workings of intracellular heterotypic and homotypic membrane fusion mechanisms.Journal of biosciences · 2019Article
- SNAREs define targeting specificity of trafficking vesicles by combinatorial interaction with tethering factors.Nature communications · 2019Article
- EARP is a multisubunit tethering complex involved in endocytic recycling.Nature cell biology · 2015Article
- Analysis on the interaction domain of VirG and apyrase by pull-down assay.Molecules (Basel, Switzerland) · 2014Article
- Vacuolar protein sorting mechanisms in apicomplexan parasites.Molecular and biochemical parasitologyArticle
- Acute GARP Depletion Disrupts Vesicle Transport, Leading to Severe Defects in Sorting, Secretion and O-Glycosylation.Traffic (Copenhagen, Denmark)Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
The Golgi-Associated Retrograde Protein (GARP) complex is a tethering factor involved in the fusion of endosome-derived transport vesicles to the trans-Golgi network through interaction with components of the Syntaxin 6/Syntaxin 16/Vti1a/VAMP4 SNARE complex. The mechanisms by which GARP and other tethering factors engage the SNARE fusion machinery are poorly understood. Herein, we report the structural basis for the interaction of the human Ang2 subunit of GARP with the Syntaxin 6 and the closely related Syntaxin 10. The crystal structure of the Syntaxin 6 Habc domain in complex with a peptide from the N terminus of Ang2 shows a binding mode in which a dityrosine motif of Ang2 interacts with a highly conserved groove in Syntaxin 6. Structure-based mutational analyses validate the crystal structure and support the phylogenetic conservation of this interaction.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.