ArticleThe Journal of cell biology1990
Control of actin filament length by phosphorylation of fragmin-actin complex.
Article in The Journal of cell biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 39 citations in OpenAlex.
- Structural Biology of Actin: Interplay Between Molecular Assembly, Conformational Polymorphism and ATPase.Sub-cellular biochemistry · 2026Review
- Age-Onset Phosphorylation of a Minor Actin Variant Promotes Intestinal Barrier Dysfunction.Developmental cell · 2019Article
- STK16 regulates actin dynamics to control Golgi organization and cell cycle.Scientific reports · 2017Article
- Review
- There is more than one way to model an elephant. Experiment-driven modeling of the actin cytoskeleton.Biophysical journal · 2013Review
- The MEK kinase Ssk2p promotes actin cytoskeleton recovery after osmotic stress.Molecular biology of the cell · 2002Article
- A novel type of protein kinase phosphorylates actin in the actin-fragmin complex.The EMBO journal · 1996Article
- Zonula occludens toxin modulates tight junctions through protein kinase C-dependent actin reorganization, in vitro.The Journal of clinical investigation · 1995Article
- Neurofilament expression in human T lymphocytes.Immunology · 1993Article
- Physarum actin is phosphorylated as the actin-fragmin complex at residues Thr203 and Thr202 by a specific 80 kDa kinase.The EMBO journal · 1992Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fragmin is a Ca2(+)-sensitive F-actin-severing protein purified from a slime mold, Physarum polycephalum (Hasegawa, T., S. Takahashi, H. Hayashi, and S. Hatano. 1980. Biochemistry. 19:2677-2683). It binds to G-actin to form a 1:1 fragmin/actin complex in the presence of micromolar free Ca2+. The complex nucleates actin polymerization and caps the barbed end of the short F-actin (Sugino, H., and S. Hatano. 1982. Cell Motil. 2:457-470). Subsequent removal of Ca2+, however, hardly dissociates the complex. This complex nucleates actin polymerization and caps the F-actin regardless of Ca2+ concentration. Here we report that this activity of fragmin-actin complex can be abolished by phosphorylation of actin of the complex. When crude extract from Physarum plasmodium was incubated with 5 mM ATP and 1 mM EGTA, the activities of the complex decreased to a great extent. The inactivation of the complex in the crude extract was not observed in the presence of Ca2+. In addition, the activities of the complex inactivated in the crude extract were restored under conditions suitable for phosphatase reactions. We purified factors that inactivated fragmin-actin complex from the crude extract. These factors phosphorylated actin of the complex, and the activities of the complex decreased with an increased level of phosphorylation of the complex. These factors, termed actin kinase, also inactivated the complex that capped the barbed end of short F-actin, leading to elongation of the short F-actin to long F-actin. Thus the length of F-actin can be controlled by phosphorylation of fragmin-actin complex by actin kinase.
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