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MBC in Press, published online ahead of print October 18, 2006
Mol. Biol. Cell 10.1091/mbc.E06-06-0531

A more recent version of this article appeared on December 1, 2006
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Submitted on June 19, 2006
Revised on September 28, 2006
Accepted on October 5, 2006

The Monomeric Clathrin Assembly Protein, AP180, Regulates Contractile Vacuole Size in Dictyostelium discoideum

Irene Stavrou and Theresa J. O’Halloran

Department of Molecular Cell and Developmental Biology, Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712

Monitoring Editor: Carole Parent

AP180, one of many assembly proteins and adaptors for clathrin, stimulates the assembly of clathrin lattices on membranes, but its unique contribution to clathrin function remains elusive. In this study we identified the Dictyostelium discoideum ortholog of the adaptor protein AP180 and characterized a mutant strain carrying a deletion in this gene. Imaging GFP-labeled AP180 showed that it localized to punctae at the plasma membrane, the contractile vacuole and cytoplasm and associated with clathrin. AP180 null cells did not display defects characteristic of clathrin mutants, and continued to localize clathrin punctae on their plasma membrane and within the cytoplasm. However, like clathrin mutants, AP180 mutants, were osmosensitive. When immersed in water, AP180 null cells formed abnormally large contractile vacuoles. Furthermore, the cycle of expansion and contraction for contractile vacuoles in AP80 null cells was twice as long as that of wild type cells. Taken together, our results suggest that AP180 plays a unique role as a regulator of contractile vacuole morphology and activity in Dictyostelium.

Address correspondence to: Theresa J. O’Halloran (t.ohalloran{at}mail.utexas.edu)




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[Abstract] [Full Text] [PDF]


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