ArticleThe Journal of cell biology1989
The Dictyostelium gelation factor shares a putative actin binding site with alpha-actinins and dystrophin and also has a rod domain containing six 100-residue motifs that appear to have a cross-beta conformation.
Article in The Journal of cell biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 130 citations in OpenAlex.
- Conservation of Energetic Pathways for Electroautotrophy in the Uncultivated Candidate OrdermSphere · 2022Article
- TaWRKY68 responses to biotic stresses are revealed by the orthologous genes from major cereals.Genetics and molecular biology · 2014Article
- Filamins in mechanosensing and signaling.Annual review of biophysics · 2012Review
- Cell type-specific filamin complex regulation by a novel class of HECT ubiquitin ligase is required for normal cell motility and patterning.Development (Cambridge, England) · 2011Article
- CP250, a novel acidic coiled-coil protein of the Dictyostelium centrosome, affects growth, chemotaxis, and the nuclear envelope.Molecular biology of the cell · 2009Article
- Filamin repeat segments required for photosensory signalling in Dictyostelium discoideum.BMC cell biology · 2007Article
- The sarcomeric Z-disc: a nodal point in signalling and disease.Journal of molecular medicine (Berlin, Germany) · 2006Review
- A cell number-counting factor regulates the cytoskeleton and cell motility in Dictyostelium.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Expression patterns of cell-type-specific genes in Dictyostelium.Molecular biology of the cell · 2001Article
- Myozenin: an alpha-actinin- and gamma-filamin-binding protein of skeletal muscle Z lines.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Interaptin, an actin-binding protein of the alpha-actinin superfamily in Dictyostelium discoideum, is developmentally and cAMP-regulated and associates with intracellular membrane compartments.The Journal of cell biology · 1998Article
- Interaction of a Dictyostelium member of the plastin/fimbrin family with actin filaments and actin-myosin complexes.Molecular biology of the cell · 1997Article
- Dictyostelium discoideum cells lacking the 34,000-dalton actin-binding protein can grow, locomote, and develop, but exhibit defects in regulation of cell structure and movement: a case of partial redundancy.The Journal of cell biology · 1996Article
- Mechanical perturbation elicits a phenotypic difference between Dictyostelium wild-type cells and cytoskeletal mutants.Biophysical journal · 1996Article
- The Dictyostelium cytoskeleton.Experientia · 1995Review
- Genetic analysis of the fimbrin-actin binding interaction in Saccharomyces cerevisiae.Genetics · 1995Article
- Cell-substrate interactions and locomotion of Dictyostelium wild-type and mutants defective in three cytoskeletal proteins: a study using quantitative reflection interference contrast microscopy.Biophysical journal · 1995Article
- Genetic deletion of ABP-120 alters the three-dimensional organization of actin filaments in Dictyostelium pseudopods.The Journal of cell biology · 1995Article
- The dystrophin superfamily: variability and complexity.Journal of muscle research and cell motility · 1994Review
- The murine mutation jaundiced is caused by replacement of an arginine with a stop codon in the mRNA encoding the ninth repeat of beta-spectrin.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
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5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 120-kD gelation factor and alpha-actinin are among the most abundant F-actin cross-linking proteins in Dictyostelium discoideum. Both molecules are homodimers and have extended rod-like configurations that are respectively approximately 35 and 40 nm long. Here we report the complete cDNA sequence of the 120-kD gelation factor which codes for a protein of 857 amino acids. Its calculated molecular mass is 92.2 kD which is considerably smaller than suggested by its mobility in SDS-PAGE. Analysis of the sequence shows a region that is highly homologous to D. discoideum alpha-actinin, chicken fibroblast alpha-actinin, and human dystrophin. This conserved domain probably represents an actin binding site that is connected to the rod-forming part of the molecule via a highly charged stretch of amino acids. Whereas the sequence of alpha-actinin (Noegel, A., W. Witke, and M. Schleicher. 1987. FEBS [Fed. Eur. Biochem. Soc.] Lett. 221:391-396) suggests that the extended rod domain of the molecule is based on four spectrin-like repeats with high alpha-helix potential, the rod domain of the 120-kD gelation factor is constructed from six 100-residue repeats that have a high content of glycine and proline residues and which, in contrast to alpha-actinin, do not appear to have a high alpha-helical content. These repeats show a distinctive pattern of regions that have high beta-sheet potential alternating with short zones rich in residues with a high potential for turns. This observation suggests that each 100-residue motif has a cross-beta conformation with approximately nine sheets arranged perpendicular to the long axis of the molecule. In the high beta-potential zones every second residue is often hydrophobic. In a cross-beta structure, this pattern would result in one side of the domain having a surface rich in hydrophobic side chains which could account for the dimerization of the 120-kD gelation factor subunits.
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