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Originally published as MBC in Press, 10.1091/mbc.E07-12-1236 on April 23, 2008

Vol. 19, Issue 7, 2830-2843, July 2008

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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

Submitted December 12, 2007; Revised April 3, 2008; Accepted April 14, 2008
Monitoring Editor: Patrick Brennwald

InCytes from MBC

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 βCOP based on the clathrin adaptor AP2 suggested that the βCOP C terminus forms an appendage domain with a conserved FW binding pocket motif. On gene replacement after knockdown, versions of βCOP 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, βCOP bound p115, and this depended on the βCOP FW motif. Furthermore, 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, βCOP FW or p115 EE motifs. Thus, Golgi organization depends on mutually interacting domains in βCOP and p115, suggesting that vesicle tethering at the Golgi involves p115 binding to the COPI coat.

This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E07-12-1236) on April 23, 2008.

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


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InCytes from MBC, July 2008

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