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The N-terminus of Dictyostelium Scar interacts with Abi and HSPC300 and is essential for proper regulation and function.

Abstract
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.
AuthorsDiana Caracino, Cheryl Jones, Mark Compton, Charles L Saxe 3rd
JournalMolecular biology of the cell (Mol Biol Cell) Vol. 18 Issue 5 Pg. 1609-20 (May 2007) ISSN: 1059-1524 [Print] United States
PMID17314411 (Publication Type: Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't)
Chemical References
  • Actins
  • Multiprotein Complexes
  • Peptide Fragments
  • Protozoan Proteins
  • Recombinant Fusion Proteins
  • SCAR protein, Dictyostelium
  • Green Fluorescent Proteins
Topics
  • Actins (metabolism)
  • Animals
  • Binding Sites
  • Chemotaxis
  • Cytokinesis
  • Dictyostelium (cytology, genetics, metabolism)
  • Green Fluorescent Proteins (genetics, metabolism)
  • In Vitro Techniques
  • Multiprotein Complexes
  • Peptide Fragments (chemistry, genetics, metabolism)
  • Protein Binding
  • Protozoan Proteins (chemistry, genetics, metabolism)
  • Recombinant Fusion Proteins (chemistry, genetics, metabolism)

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