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• W2023223627 abstract "Protein phosphorylation plays important roles in a variety of stress responses. Although plasmodium ofPhysarum polycephalumrapidly grows and shows an active cytoplasmic streaming under nutrient and wet conditions, dry stress transforms plasmodium into a dormant state called sclerotium. Sclerotium can change into plasmodium within several hours after addition of water. We herein report that more than half of actin in sclerotium was in a phosphorylated state. Thein vivophosphorylation site was identified to be Thr-203 which is in contact with another actin molecule upon polymerization. The phosphorylated form of actin showed no polymerizing activity, while the unphosphorylated form possessed the ability to polymerize into F-actin. These results suggest that phosphorylation ofPhysarumactin is involved in reorganization and/or preservation of the actin molecules in the process of sclerotium formation." @default.
• W2023223627 created "2016-06-24" @default.
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• W2023223627 date "1998-01-01" @default.
• W2023223627 modified "2023-09-29" @default.
• W2023223627 title "Dry Stress-Induced Phosphorylation ofPhysarumActin" @default.
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• W2023223627 doi "https://doi.org/10.1006/bbrc.1997.8044" @default.
• W2023223627 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9464272" @default.
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