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Originally published as MBC in Press, 10.1091/mbc.E03-09-0659 on April 2, 2004 Originally published as MBC in Press, 10.1091/mbc.E03-09-0659 on March 26, 2004

Vol. 15, Issue 6, 2920-2931, June 2004

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Loss of Apm1, the µ1 Subunit of the Clathrin-Associated Adaptor-Protein-1 Complex, Causes Distinct Phenotypes and Synthetic Lethality with Calcineurin Deletion in Fission Yeast

Ayako Kita * {dagger} {ddagger}, Reiko Sugiura * {dagger} {ddagger} §, Hiromi Shoji *, Yi He *, Lu Deng *, Yabin Lu *, Susie O. Sio * ||, Kaoru Takegawa ¶, Motoyoshi Sakaue #, Hisato Shuntoh @, and Takayoshi Kuno *

* Division of Molecular Pharmacology and Pharmacogenomics, Department of Genome Sciences, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan; {dagger} Laboratory of Molecular Pharmacogenomics, School of Pharmaceutical Sciences, Kinki University, Higashi-Osaka 577-8502, Japan; || Department of Pharmacology, College of Medicine, University of the Philippines Manila, Manila 1000, Philippines; Department of Life Sciences, Faculty of Agriculture, Kagawa University, Kagawa 761-0795, Japan; # Schools of Humanities for Environmental Policy and Technology. Himeji Institute of Technology, Himeji 670-0092, Japan.; and @ Faculty of Health Science, Kobe University School of Medicine, Kobe 654-0142, Japan

Submitted September 11, 2003; Revised March 12, 2004; Accepted March 12, 2004
Monitoring Editor: Juan S. Bonifacino

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 ({Delta}apm1) cells showed distinct phenotypes: temperature sensitivity; tacrolimus (FK506) sensitivity; and pleiotropic defects in cytokinesis, cell integrity, and vacuole fusion. Electron micrographs revealed that {Delta}apm1 cells showed large vesicular structures associated with Golgi stacks and accumulated post-Golgi secretory vesicles. {Delta}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 also suggest that calcineurin is involved in these events.

Article published online ahead of print. Mol. Biol. Cell 10.1091/mbc.E03-09-0659. Article and publication date are available at www.molbiolcell.org/cgi/doi/10.1091/mbc.E03-09-0659.

{ddagger} Both authors contributed equally to this work.

§ Corresponding author. E-mail address: sugiurar{at}med.kobe-u.ac.jp.




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