ArticleThe Journal of cell biology1983
An actin-depolymerizing protein (depactin) from starfish oocytes: properties and interaction with actin.
Article in The Journal of cell biology, 1983. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 130 citations in OpenAlex.
- Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023Review
- Dithiothreitol Affects the Fertilization Response in Immature and Maturing Starfish Oocytes.Biomolecules · 2023Article
- Comparative Transcriptome Analysis of Deep-Rooting and Shallow-Rooting Potato (Plants (Basel, Switzerland) · 2022Article
- Cofilin-induced structural changes in actin filaments stay local.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Functions of actin-interacting protein 1 (AIP1)/WD repeat protein 1 (WDR1) in actin filament dynamics and cytoskeletal regulation.Biochemical and biophysical research communications · 2018Review
- Combinatorial genetic analysis of a network of actin disassembly-promoting factors.Cytoskeleton (Hoboken, N.J.) · 2015Article
- Structure and mechanism of mouse cyclase-associated protein (CAP1) in regulating actin dynamics.The Journal of biological chemistry · 2014Article
- Toxoplasma gondii actin depolymerizing factor acts primarily to sequester G-actin.The Journal of biological chemistry · 2010Article
- Three cotton genes preferentially expressed in flower tissues encode actin-depolymerizing factors which are involved in F-actin dynamics in cells.Journal of experimental botany · 2010Article
- Actin-depolymerizing factor2-mediated actin dynamics are essential for root-knot nematode infection of Arabidopsis.The Plant cell · 2009Article
- Reconstitution and dissection of the 600-kDa Srv2/CAP complex: roles for oligomerization and cofilin-actin binding in driving actin turnover.The Journal of biological chemistry · 2009Article
- Three-dimensional arrangement of F-actin in the contractile ring of fission yeast.The Journal of cell biology · 2007Article
- Actin-depolymerizing protein Adf1 is required for formation and maintenance of the contractile ring during cytokinesis in fission yeast.Molecular biology of the cell · 2006Article
- Regulation of the pollen-specific actin-depolymerizing factor LlADF1.The Plant cell · 2002Article
- The ADF/cofilin family: actin-remodeling proteins.Genome biology · 2002Review
- ADF proteins are involved in the control of flowering and regulate F-actin organization, cell expansion, and organ growth in Arabidopsis.The Plant cell · 2001Article
- Molecular identification and characterization of the Arabidopsis AtADF1, AtADFS and AtADF6 genes.Plant molecular biology · 2001Article
- The ADF/cofilin proteins: stimulus-responsive modulators of actin dynamics.Molecular biology of the cell · 1995Review
- Focusing on unpolymerized actin.The Journal of cell biology · 1993Review
- Colocalization of ADF and cofilin in intranuclear actin rods of cultured muscle cells.Journal of muscle research and cell motility · 1993Article
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Authors and funding
1 author.
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Abstract
Physico-chemical properties and interaction with actin of an actin-depolymerizing protein from mature starfish oocytes were studied. This protein, which is called depactin, exists in a monomeric form under physiological conditions. Its molecular weight is approximately 20,000 for the native protein and approximately 17,000 for denatured protein. The Glu + Asp/Lys + Arg molar ratio of this protein is 1.55. The apparent pl of the denatured depactin is approximately 6. The extent of actin polymerization is reduced by the presence of depactin; however, the rate of polymerization seems to be accelerated as measured spectrophotometrically at 238nm. This effect is interpreted to indicate that depactin cut the newly formed filaments into small fragments, thereby increasing the number of the filament ends to which monomers are added. The apparent critical concentration of actin for polymerization, as determined by viscometry or flow birefringence measurement, is increased by the presence of depactin in a concentration-dependent manner. Raising the pH of the solution does not reverse the action of depactin. The molar ratio of actin and depactin, which interact with each other, is estimated to be 1:1 by means of a cross-linking experiment using a water-soluble carbodiimide. Depactin binds to a DNase I-Sepharose column via actin and is selectively eluted with 0.6 M KCl or 0.6 M Kl. The association constant between actin and depactin is estimated, using the column, to be 2-3 X 10(6) M-1. The content of depactin in the high-speed supernatant of the oocyte extract is determined to be 1%; this can act upon approximately 63% of the actin in the supernatant.
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