The N-Terminus ofDictyosteliumScar Interacts with Abi and HSPC300 and Is Essential for Proper Regulation and Function
| Autor: | Mark M. Compton, Charles L. Saxe, Cheryl Jones, Diana Caracino |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Recombinant Fusion Proteins
Green Fluorescent Proteins Protozoan Proteins macromolecular substances Plasma protein binding In Vitro Techniques Cell morphology Animals Dictyostelium Binding site Molecular Biology Actin Cytokinesis Binding Sites biology Chemotaxis Articles Cell Biology biology.organism_classification Molecular biology ABI1 Actins Peptide Fragments Cell biology Multiprotein Complexes Protein Binding |
| Zdroj: | Molecular Biology of the Cell. 18:1609-1620 |
| ISSN: | 1939-4586 1059-1524 |
| Popis: | Scar/WAVE proteins, members of the conserved Wiskott-Aldrich syndrome (WAS) family, promote actin polymerization by activating the Arp2/3 complex. A number of proteins, including a complex containing Nap1, PIR121, Abi1/2, and HSPC300, interact with Scar/WAVE, though the role of this complex in regulating Scar function remains unclear. Here we identify a short N-terminal region of Dictyostelium Scar that is necessary and sufficient for interaction with HSPC300 and Abi in vitro. Cells expressing Scar lacking this N-terminal region show abnormalities in F-actin distribution, cell morphology, movement, and cytokinesis. This is true even in the presence of wild-type Scar. The data suggest that the first 96 amino acids of Scar are necessary for participation in a large-molecular-weight protein complex, and that this Scar-containing complex is responsible for the proper localization and regulation of Scar. The presence of mis-regulated or unregulated Scar has significant deleterious effects on cells and may explain the need to keep Scar activity tightly controlled in vivo either by assembly in a complex or by rapid degradation. |
| Databáze: | OpenAIRE |
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