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Originally published as MBC in Press, 10.1091/mbc.E07-08-0805 on January 16, 2008

Vol. 19, Issue 4, 1295-1303, April 2008

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Cation Diffusion Facilitator Cis4 Is Implicated in Golgi Membrane Trafficking via Regulating Zinc Homeostasis in Fission Yeast

Yue Fang*, Reiko Sugiura*,{dagger}, Yan Ma*, Tomoko Yada-Matsushima*,{ddagger}, Hirotatsu Umeno*,§, and Takayoshi Kuno*

*Division of Molecular Pharmacology and Pharmacogenomics, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan; and {dagger}Laboratory of Molecular Pharmacogenomics, School of Pharmaceutical Sciences, Kinki University, Higashi-Osaka, 577-8502, Japan

Submitted August 19, 2007; Revised December 26, 2007; Accepted January 8, 2008
Monitoring Editor: Benjamin Glick

We screened for mutations that confer sensitivities to the calcineurin inhibitor FK506 and to a high concentration of MgCl2 and isolated the cis4-1 mutant, an allele of the gene encoding a cation diffusion facilitator (CDF) protein that is structurally related to zinc transporters. Consistently, the addition of extracellular Zn2+ suppressed the phenotypes of the cis4 mutant cells. The cis4 mutants and the mutant cells of another CDF-encoding gene SPBC16E9.14c (we named zrg17+) shared common and nonadditive zinc-suppressible phenotypes, and Cis4 and Zrg17 physically interacted. Cis4 localized at the cis-Golgi, suggesting that Cis4 is responsible for Zn2+ uptake to the cis-Golgi. The cis4 mutant cells showed phenotypes such as weak cell wall and decreased acid phosphatase secretion that are thought to be resulting from impaired membrane trafficking. In addition, the cis4 deletion cells showed synthetic growth defects with all the four membrane-trafficking mutants tested, namely ypt3-i5, ryh1-i6, gdi1-i11, and apm1-1. Interestingly, the addition of extracellular Zn2+ significantly suppressed the phenotypes of the ypt3-i5 and apm1-1 mutant cells. These results suggest that Cis4 forms a heteromeric functional complex with Zrg17 and that Cis4 is implicated in Golgi membrane trafficking through the regulation of zinc homeostasis in fission yeast.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E07-08-0805) on January 16, 2008.

Present addresses: {ddagger} Sysmex Corporation, Kobe 651-0073, Japan;

§ Chugai Pharmaceutical Co., Tokyo 103-8324, Japan.

Address correspondence to: Takayoshi Kuno (tkuno{at}med.kobe-u.ac.jp)




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