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Vol. 13, Issue 8, 2963-2976, August 2002
*Division of Molecular Pharmacology and Pharmacogenomics,
Department of Genome Sciences, Kobe University Graduate School of
Medicine, Kobe 650-0017, Japan. A genetic screen for mutations synthetically lethal with fission
yeast calcineurin deletion led to the identification of Ypt3, a homolog
of mammalian Rab11 GTP-binding protein. A mutant with the
temperature-sensitive ypt3-i5 allele showed pleiotropic
phenotypes such as defects in cytokinesis, cell wall integrity, and
vacuole fusion, and these were exacerbated by FK506-treatment, a
specific inhibitor of calcineurin. Green fluorescent protein
(GFP)-tagged Ypt3 showed cytoplasmic staining that was concentrated at
growth sites, and this polarized localization required the actin
cytoskeleton. It was also detected as a punctate staining in an
actin-independent manner. Electron microscopy revealed that
ypt3-i5 mutants accumulated aberrant Golgi-like structures
and putative post-Golgi vesicles, which increased remarkably at the
restrictive temperature. Consistently, the secretion of GFP fused with
the pho1+ leader peptide (SPL-GFP) was abolished
at the restrictive temperature in ypt3-i5 mutants.
FK506-treatment accentuated the accumulation of aberrant Golgi-like
structures and caused a significant decrease of SPL-GFP secretion at a
permissive temperature. These results suggest that Ypt3 is required at
multiple steps of the exocytic pathway and its mutation affects diverse
cellular processes and that calcineurin is functionally connected to
these cellular processes.
National Institute of
Bioscience and Human-Technology, Agency of Industrial Science and
Technology, Ibaraki 305-8566, Japan; §Department of Life
Sciences, Faculty of Agriculture, Kagawa University, Kagawa, 761-0795, Japan; and ¶Faculty of Health Science, Kobe University
School of Medicine, Kobe 650-0142, Japan.
Both authors contributed equally to this work.
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