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MBC in Press, published online ahead of print July 12, 2006
Mol. Biol. Cell 10.1091/mbc.E05-12-1112

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Submitted on December 7, 2005
Revised on June 19, 2006
Accepted on July 5, 2006

Capacity of the Golgi Apparatus for Cargo Transport Prior to Complete Assembly

Shu Jiang,* Sung Wu Rhee,* Paul A. Gleeson,{dagger} and Brian Storrie*

*Department of Physiology and Biophysics, University of Arkansas for Medical Sciences, Little Rock, AR 72205; {dagger}Department of Biochemistry and Molecular Biology and Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Melbourne, Victoria 3010, Australia

Monitoring Editor: Vivek Malhotra

In yeast, particular emphasis has been given to ER-derived, cisternal maturation models of Golgi assembly while in mammalian cells more emphasis has been given to golgins as a potentially stable assembly framework. In the case of de novo Golgi formation from the ER following brefeldin A/H89 washout in HeLa cells, we found that scattered, golgin-enriched, structures formed early and contained golgins including giantin, ranging across the entire cis to trans spectrum of the Golgi apparatus. These structures were incompetent in VSV-G cargo transport. Second, we compared Golgi competence in cargo transport to the kinetics of addition of various glycosyltransferases and glycosidases into nascent, golgin-enriched structures following drug washout. Enzyme accumulation was sequential with trans then medial glycosyltransferases/glycosidases found in the scattered, nascent Golgi. Involvement in cargo transport preceded full accumulation of enzymes or GPP130 into nascent Golgi. Third, during mitosis, we found that the formation of a golgin-positive acceptor compartment in early telophase preceded the accumulation of a Golgi glycosyltransferase in nascent Golgi structures. We conclude that during mammalian Golgi assembly components fit into a dynamic, first-formed, multi-golgin-enriched framework that is initially cargo transport incompetent. Resumption of cargo transport precedes full Golgi assembly.


Address correspondence to: Brian Storrie (StorrieBrian{at}uams.edu)




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