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¹ Division of Molecular Pharmacology and Pharmacogenomics, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, Kusunoki-cho, Chuo-ku, Kobe 650-0017, Japan
² Laboratory of Molecular Pharmacogenomics, School of Pharmaceutical Sciences, Kinki University, Kowakae 3-4-1, Higashi-Osaka 577-8502, Japan
³ University of the Philippines Manila, Manila 1000, Philippines

Adaptins are subunits of the heterotetrameric (β/µ//) adaptor protein (AP) complexes that are involved in clathrin-mediated membrane trafficking. Here, we show that in Schizosaccharomyces pombe the deletion strains of each individual subunit of the AP-1 complex [Apl2 (β), Apl4 (), Apm1 (µ) and Aps1 ()] caused distinct phenotypes on growth sensitivity to temperature or drugs. We also show that the apm1 and apl2 mutants displayed similar but more severe phenotypes than those of aps1 or apl4 mutants. Furthermore, the apl2aps1 and apl2apl4 double mutants displayed synthetic growth defects, whereas the aps1apl4 and apl2apm1 double mutants did not. In pull-down assay, Apm1 binds Apl2 even in the absence of Aps1 and Apl4, and Apl4 binds Aps1 even in the absence of Apm1 and Apl2. Consistently, the deletion of any subunit generally caused the disassociation of the heterotetrameric complex from endosomes, although some subunits weakly localized to endosomes. In addition, the deletion of individual subunits caused similar endosomal accumulation of v-SNARE synaptobrevin Syb1. Altogether, results suggest that the four subunits are all essential for the heterotetrameric complex formation and for the AP-1 function in exit transport from endosomes.

^* mayan{at}med.kobe-u.ac.jp