Distinct roles for plasma membrane PtdIns(4)P and PtdIns(4,5)P2 during yeast receptor-mediated endocytosis
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- Wataru Yamamoto
- Department of Biological Science and Technology, Tokyo University of Science, 6-3-1 Niijyuku, Katsushika-ku, Tokyo 125-8585, Japan
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- Suguru Wada
- Department of Biological Science and Technology, Tokyo University of Science, 6-3-1 Niijyuku, Katsushika-ku, Tokyo 125-8585, Japan
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- Makoto Nagano
- Department of Biological Science and Technology, Tokyo University of Science, 6-3-1 Niijyuku, Katsushika-ku, Tokyo 125-8585, Japan
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- Kaito Aoshima
- Department of Biological Science and Technology, Tokyo University of Science, 6-3-1 Niijyuku, Katsushika-ku, Tokyo 125-8585, Japan
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- Daria Elisabeth Siekhaus
- Institute of Science and Technology Austria, Am Campus 1, A-3400 Klosterneuburg, Austria
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- Junko Y. Toshima
- School of Health Science, Tokyo University of Technology, 5-23-22 Nishikamada, Ota-ku, Tokyo 144-8535, Japan
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- Jiro Toshima
- Department of Biological Science and Technology, Tokyo University of Science, 6-3-1 Niijyuku, Katsushika-ku, Tokyo 125-8585, Japan
抄録
<jats:p>Clathrin-mediated endocytosis requires the coordinated assembly of various endocytic proteins and lipids at the plasma membrane. Accumulating evidence demonstrates a crucial role for phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2) in endocytosis, but specific roles for PtdIns(4)P other than as the biosynthetic precursor of PtdIns(4,5)P2 have not been clarified. In this study we investigated the role of PtdIns(4)P or PtdIns(4,5)P2 in receptor-mediated endocytosis through the construction of temperature-sensitive (ts) mutants for the PI 4-kinases Stt4p and Pik1p and the PtdIns(4) 5-kinase Mss4p. Quantitative analyses of endocytosis revealed that both the stt4ts pik1ts and mss4ts mutants have a severe defect in endocytic internalization. Live-cell imaging of endocytic protein dynamics in stt4ts pik1ts and mss4ts mutants revealed that PtdIns(4)P is required for the recruitment of the α-factor receptor Ste2p to clathrin-coated pits whereas PtdIns(4,5)P2 is required for membrane internalization. We also found that the localization to endocytic sites of the ENTH/ANTH domain-bearing clathrin adaptors, Ent1p/Ent2p and Yap1801p/Yap1802p, is significantly impaired in the stt4ts pik1ts mutant, but not in the mss4ts mutant. These results suggest distinct roles in successive steps for PtdIns(4)P and PtdIns(4,5)P2 during receptor-mediated endocytosis.</jats:p>
収録刊行物
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- Journal of Cell Science
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Journal of Cell Science 2017-01-01
The Company of Biologists
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キーワード
詳細情報 詳細情報について
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- CRID
- 1360285711956512768
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- ISSN
- 14779137
- 00219533
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- データソース種別
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- Crossref
- KAKEN