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MBC in Press, published online ahead of print April 23, 2008
Mol. Biol. Cell 10.1091/mbc.E07-12-1236

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Submitted on December 12, 2007
Revised on April 3, 2008
Accepted on April 14, 2008

Coat-Tether Interaction in Golgi Organization

Yusong Guo, Vasu Punj, Debrup Sengupta, and Adam D. Linstedt

Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA 15213

Monitoring Editor: Patrick Brennwald

Biogenesis of the Golgi apparatus is likely mediated by the COPI vesicle coat complex but the mechanism is poorly understood. Modeling of the COPI subunit {beta}COP based on the clathrin adaptor AP2 suggested that the {beta}COP C-terminus forms an appendage domain with a conserved FW binding pocket motif. On gene replacement after knockdown, versions of {beta}COP with a mutated FW motif or flanking basic residues yielded a defect in Golgi organization reminiscent of that occurring in the absence of the vesicle tether p115. Indeed, {beta}COP bound p115 and this depended on the {beta}COP FW motif. Further, the interaction depended on E19E21 in the p115 head domain and inverse charge substitution blocked Golgi biogenesis in intact cells. Finally, Golgi assembly in permeabilized cells was significantly reduced by inhibitors containing intact, but not mutated, {beta}COP FW or p115 EE motifs. Thus, Golgi organization depends on mutually interacting domains in {beta}COP and p115 suggesting that vesicle tethering at the Golgi involves p115 binding to the COPI coat.

Address correspondence to: Adam D. Linstedt (linstedt{at}andrew.cmu.edu)






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