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A more recent version of this article appeared on June 1, 2004 Originally published as MBC in Press, 10.1091/mbc.E03-09-0659 on March 26, 2004
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Submitted on September 11, 2003
Revised on March 12, 2004
Accepted on March 12, 2004
1 Division of Molecular Pharmacology and Pharmacogenomics, Department of Genome Sciences, Kobe University Graduate School of Medicine, Kusunoki-cho, Chuo-ku, Kobe 650-0017, Japan; Laboratory of Molecular Pharmacogenomics, School of Pharmaceutical Sciences, Kinki University, Kowakae 3-4-1, Higashi-Osaka, 577-8502, Japan
2 Division of Molecular Pharmacology and Pharmacogenomics, Department of Genome Sciences, Kobe University Graduate School of Medicine, Kusunoki-cho, Chuo-ku, Kobe 650-0017, Japan; Laboratory of Molecular Pharmacogenomics, School of Pharmaceutical Sciences, Kinki University, Kowakae 3-4-1, Higashi-Osaka, 577-8502, Japan;
3 Division of Molecular Pharmacology and Pharmacogenomics, Department of Genome Sciences, Kobe University Graduate School of Medicine, Kusunoki-cho, Chuo-ku, Kobe 650-0017, Japan
4 Division of Molecular Pharmacology and Pharmacogenomics, Department of Genome Sciences, Kobe University Graduate School of Medicine, Kusunoki-cho, Chuo-ku, Kobe 650-0017, Japan; Department of Pharmacology, College of Medicine, University of the Philippines Manila, Manila 1000, Philippines
5 Department of Life Sciences, Faculty of Agriculture, Kagawa University, Miki-cho, Kagawa, 761-0795, Japan
6 Schools of Humanities for Environmental Policy and Technology. Himeji Institute of Technology. 1-1-12 Shinzaike Honmachi, Himeji 670-0092, Japan
7 Faculty of Health Science, Kobe University School of Medicine, 7-10-2 Tomogaoka, Suma-ku, Kobe 654-0142, Japan
* Corresponding author. E-mail address: sugiurar{at}med.kobe-u.ac.jp.
Calcineurin is a highly conserved regulator of Ca2+ signaling in eukaryotes. In fission yeast, calcineurin is not essential for viability but is required for cytokinesis and Cl- homeostasis. In a genetic screen for mutations that are synthetically lethal with calcineurin deletion, we isolated a mutant, cis1-1/apm1-1, an allele of the apm1+ gene that encodes a homolog of the mammalian µ1A subunit of the clathrin-associated adaptor protein-1 (AP-1) complex. The cis1-1/apm1-1 mutant as well as the apm1-deleted (
apm1) cells showed distinct phenotypes: temperature sensitivity; FK506 sensitivity; and pleiotropic defects in cytokinesis, cell integrity and vacuole fusion. Electron micrographs revealed that apm1 cells showed large vesicular structures associated with Golgi stacks, and accumulated postGolgi secretory vesicles. apm1 cells also showed the massive accumulation of the exocytic v-SNARE Syb1 in the Golgi/endosomes and a reduced secretion of acid phosphatase. These phenotypes observed in apm1 mutations were accentuated upon temperature up-shift and FK506-treatment. Notably, Apm1-GFP localized to the Golgi/endosomes, the spindle pole bodies, and the medial region. These findings suggest a role for Apm1 associated with the Golgi/endosome function thereby affecting various cellular processes including secretion, cytokinesis, vacuole fusion, and cell integrity, and that calcineurin is also involved in these events.
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