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Vol. 18, Issue 1, 94-105, January 2007

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A Role for Clathrin in Reassembly of the Golgi Apparatus

Andreea E. Radulescu^*, Anirban Siddhanta^*,, and Dennis Shields^*,

*Departments of Developmental and Molecular Biology and Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, NY 10461

Submitted June 19, 2006; Revised October 10, 2006; Accepted October 13, 2006
Monitoring Editor: Adam Linstedt

The Golgi apparatus is a highly dynamic organelle whose organization is maintained by a proteinaceous matrix, cytoskeletal components, and inositol phospholipids. In mammalian cells, disassembly of the organelle occurs reversibly at the onset of mitosis and irreversibly during apoptosis. Several pharmacological agents including nocodazole, brefeldin A (BFA), and primary alcohols (1-butanol) induce reversible fragmentation of the Golgi apparatus. To dissect the mechanism of Golgi reassembly, rat NRK and GH3 cells were treated with 1-butanol, BFA, or nocodazole. During washout of 1-butanol, clathrin, a ubiquitous coat protein implicated in vesicle traffic at the trans-Golgi network and plasma membrane, and abundant clathrin coated vesicles were recruited to the region of nascent Golgi cisternae. Knockdown of endogenous clathrin heavy chain showed that the Golgi apparatus failed to reform efficiently after BFA or 1-butanol removal. Instead, upon 1-butanol washout, it maintained a compact, tight morphology. Our results suggest that clathrin is required to reassemble fragmented Golgi elements. In addition, we show that after butanol treatment the Golgi apparatus reforms via an initial compact intermediate structure that is subsequently remodeled into the characteristic interphase lace-like morphology and that reassembly requires clathrin.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E06-06-0532) on October 25, 2006.

Present address: Department of Biochemistry, University of Calcutta, Kolkata 700 019, India.

Address correspondence to: Dennis Shields (shields{at}aecom.yu.edu)

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