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 |
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Authors: | Neil Vasan Alex Hutagalung Peter Novick Karin M. Reinisch |
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Affiliation: | aDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT 06520; and;bDepartment of Cellular and Molecular Medicine, University of California, La Jolla, CA 92093 |
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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 Å. We show that the C terminus consists of two α-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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Keywords: | endocytosis membrane traffic |
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