ArticleThe EMBO journal1987
The F-actin capping proteins of Physarum polycephalum: cap42(a) is very similar, if not identical, to fragmin and is structurally and functionally very homologous to gelsolin; cap42(b) is Physarum actin.
Article in The EMBO journal, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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39 citing papers in PubMed, 117 citations in OpenAlex.
- Structural Biology of Actin: Interplay Between Molecular Assembly, Conformational Polymorphism and ATPase.Sub-cellular biochemistry · 2026Review
- Structural and biochemical evidence for the emergence of a calcium-regulated actin cytoskeleton prior to eukaryogenesis.Communications biology · 2022Article
- Insights into the evolution of regulated actin dynamics via characterization of primitive gelsolin/cofilin proteins from Asgard archaea.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Regulatory role of the second gelsolin-like domain of Caenorhabditis elegans gelsolin-like protein 1 (GSNL-1) in its calcium-dependent conformation and actin-regulatory activities.Cytoskeleton (Hoboken, N.J.) · 2013Article
- Identification and characterization of the actin-binding motif of phostensin.International journal of molecular sciences · 2012Article
- Structural analysis of an Echinococcus granulosus actin-fragmenting protein by small-angle x-ray scattering studies and molecular modeling.Biophysical journal · 2006Article
- Villin-like actin-binding proteins are expressed ubiquitously in Arabidopsis.Plant physiology · 2000Article
- In vivo, villin is required for Ca(2+)-dependent F-actin disruption in intestinal brush borders.The Journal of cell biology · 1999Article
- Phototactic migration of Dictyostelium cells is linked to a new type of gelsolin-related protein.Molecular biology of the cell · 1999Article
- Murine adseverin (D5), a novel member of the gelsolin family, and murine adseverin are induced by interleukin-9 in T-helper lymphocytes.Molecular and cellular biology · 1998Article
- Xenopus actin depolymerizing factor/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails.The Journal of cell biology · 1997Article
- A novel type of protein kinase phosphorylates actin in the actin-fragmin complex.The EMBO journal · 1996Article
- A gelsolin-related protein from lobster muscle: cloning, sequence analysis and expression.The Biochemical journal · 1995Article
- Molecular cloning and functional expression of chromaffin cell scinderin indicates that it belongs to the family of Ca(2+)-dependent F-actin severing proteins.Molecular and cellular biochemistry · 1994Article
- X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Identification of secreted and cytosolic gelsolin in Drosophila.The Journal of cell biology · 1994Article
- A novel protein accumulated during maturation of the pods of the plant Impatiens balsamina.Molecular and cellular biochemistry · 1994Article
- Three-dimensional solution structure of Acanthamoeba profilin-I.The Journal of cell biology · 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
- Are the conserved sequences in segment 1 of gelsolin important for binding actin?The Journal of cell biology · 1992Article
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Abstract
We have carried out a primary structure analysis of the F-actin capping proteins of Physarum polycephalum. Cap42(b) was completely sequenced and was found to be identical with Physarum actin. Approximately 88% of the sequence of cap42(a) was determined. Cap42(a) and fragmin were found to be identical by amino acid composition, isoelectric point, mol. wt, elution time on reversed-phase chromatography and amino acid sequence of their tryptic peptides. The available sequence of cap42(a) is greater than 36% homologous with the NH2-terminal 42-kd domain of human gelsolin. A highly homologous region of 16 amino acids is also shared between cap42(a), gelsolin and the Acanthamoeba profilins. Cap42(a) binds two actin molecules in a similar way to gelsolin suggesting a mechanism of F-actin modulation that has been conserved during evolution.
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