ArticleProceedings of the National Academy of Sciences of the United States of America2010
Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of Golgi-associated retrograde protein (GARP) complex to a family of tethering complexes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- COG Complex in Golgi Trafficking and Glycosylation.Sub-cellular biochemistry · 2026Review
- GARP Complex in Golgi Physiology.Sub-cellular biochemistry · 2026Review
- 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
- Getting Sugar Coating Right! The Role of the Golgi Trafficking Machinery in Glycosylation.Cells · 2021Review
- Homology and Modular Evolution of CATCHR at the Origin of the Eukaryotic Endomembrane System.Genome biology and evolution · 2021Article
- VPS53 Suppresses Malignant Properties in Colorectal Cancer by Inducing the Autophagy Signaling Pathway.OncoTargets and therapy · 2020Article
- VPS53 gene is associated with a new phenotype of complicated hereditary spastic paraparesis.Neurogenetics · 2019Article
- A systematic approach to identify recycling endocytic cargo depending on the GARP complex.eLife · 2019Article
- Evolution of late steps in exocytosis: conservation and specialization of the exocyst complex.Wellcome open research · 2019Article
- Two subunits of the exocyst, Sec3p and Exo70p, can function exclusively on the plasma membrane.Molecular biology of the cell · 2018Article
- AFM/TIRF force clamp measurements of neurosecretory vesicle tethers reveal characteristic unfolding steps.PloS one · 2017Article
- The Trypanosome Exocyst: A Conserved Structure Revealing a New Role in Endocytosis.PLoS pathogens · 2017Article
- Distinct Roles for the N- and C-terminal Regions of M-Sec in Plasma Membrane Deformation during Tunneling Nanotube Formation.Scientific reports · 2016Article
- CATCHR, HOPS and CORVET tethering complexes share a similar architecture.Nature structural & molecular biology · 2016Article
- Molecular architecture of the complete COG tethering complex.Nature structural & molecular biology · 2016Article
- Cog5-Cog7 crystal structure reveals interactions essential for the function of a multisubunit tethering complex.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Structural basis for the interaction of the Golgi-Associated Retrograde Protein Complex with the t-SNARE Syntaxin 6.Structure (London, England : 1993) · 2013Article
- A new role for RINT-1 in SNARE complex assembly at the trans-Golgi network in coordination with the COG complex.Molecular biology of the cell · 2013Article
- Structures and mechanisms of vesicle coat components and multisubunit tethering complexes.Current opinion in cell biology · 2012Review
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4 authors.
Funding
Abstract
The Golgi-associated retrograde protein (GARP) complex is a membrane-tethering complex that functions in traffic from endosomes to the trans-Golgi network. Here we present the structure of a C-terminal fragment of the Vps53 subunit, important for binding endosome-derived vesicles, at a resolution of 2.9 A. We show that the C terminus consists of two alpha-helical bundles arranged in tandem, and we identify a highly conserved surface patch, which may play a role in vesicle recognition. Mutations of the surface result in defects in membrane traffic. The fold of the Vps53 C terminus is strongly reminiscent of proteins that belong to three other tethering complexes--Dsl1, conserved oligomeric Golgi, and the exocyst--thought to share a common evolutionary origin. Thus, the structure of the Vps53 C terminus suggests that GARP belongs to this family of complexes.
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