Role of the Rab GTP-Binding Protein Ypt3 in the Fission Yeast Exocytic Pathway and Its Connection to Calcineurin Function

• Hong Cheng

  Division of Molecular Pharmacology and Pharmacogenomics, Department of Genome Sciences, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan.

• Reiko Sugiura

  Division of Molecular Pharmacology and Pharmacogenomics, Department of Genome Sciences, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan.

• Wenlian Wu

  Division of Molecular Pharmacology and Pharmacogenomics, Department of Genome Sciences, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan.

• Masaaki Fujita

  Division of Molecular Pharmacology and Pharmacogenomics, Department of Genome Sciences, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan.

• Yabin Lu

  Division of Molecular Pharmacology and Pharmacogenomics, Department of Genome Sciences, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan.

• Susie O. Sio

  Division of Molecular Pharmacology and Pharmacogenomics, Department of Genome Sciences, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan.

• Rena Kawai

  National Institute of Bioscience and Human-Technology, Agency of Industrial Science and Technology, Ibaraki 305-8566, Japan;

• Kaoru Takegawa

  Department of Life Sciences, Faculty of Agriculture, Kagawa University, Kagawa, 761-0795, Japan; and

• Hisato Shuntoh

  Faculty of Health Science, Kobe University School of Medicine, Kobe 650-0142, Japan.

• Takayoshi Kuno

  Division of Molecular Pharmacology and Pharmacogenomics, Department of Genome Sciences, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan.

• Mitsuhiro Yanagida

  editor

抄録

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 thatypt3-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.

収録刊行物

• Molecular Biology of the Cell

  Molecular Biology of the Cell 13 (8), 2963-2976, 2002-08

  American Society for Cell Biology (ASCB)

キーワード

• Cell Biology
• Molecular Biology

詳細情報

• CRID: 1361981469504261888
• NII論文ID: 30018378297
• DOI: 10.1091/mbc.01-09-0463
• ISSN: 19394586
• ISSN: 10591524
• ISSN: http://id.crossref.org/issn/10591524
• データソース種別:
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  • CiNii Articles