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Structural and Functional Analysis of the Globular Head Domain of p115 Provides Insight into Membrane Tethering |
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| Authors: | Yu An Christine Y Chen Piotr Rotkiewicz Adam Godzik William E Balch |
| Institution: | 1 Department of Cell Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla CA 92037, USA 2 Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla CA 92037, USA 3 Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla CA 92037, USA 4 Program in Bioinformatics and Systems Biology, Burnham Institute for Medical Research, 10901 N. Torrey Pines Road, La Jolla, CA 92037, USA 5 Skaggs Institute for Chemical Biology The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla CA 92037, USA 6 The Institute for Childhood and Neglected Disease, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla CA 92037, USA |
| Abstract: | Molecular tethers have a central role in the organization of the complex membrane architecture of eukaryotic cells. p115 is a ubiquitous, essential tether involved in vesicle transport and the structural organization of the exocytic pathway. We describe two crystal structures of the N-terminal domain of p115 at 2.0 Å resolution. The p115 structures show a novel α-solenoid architecture constructed of 12 armadillo-like, tether-repeat, α-helical tripod motifs. We find that the H1 TR binds the Rab1 GTPase involved in endoplasmic reticulum to Golgi transport. Mutation of the H1 motif results in the dominant negative inhibition of endoplasmic reticulum to Golgi trafficking. We propose that the H1 helical tripod contributes to the assembly of Rab-dependent complexes responsible for the tether and SNARE-dependent fusion of membranes. |
| Keywords: | ER endoplasmic reticulum TRAPP transport protein particle COG conserved oligomeric Golgi SNARE soluble N-ethylmaleimide-sensitive factor attachment protein receptors MAD multiwavelength anomalous diffraction TR tether repeat VSV-G vesicular stomatitis virus glycoprotein TC tethering complex |
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