N-WASP Regulation--the Sting in the Tail
- 27 October 2000
- journal article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 290 (5492) , 725-726
- https://doi.org/10.1126/science.290.5492.725
Abstract
Signaling proteins can be regulated by their interactions with other proteins and phospholipids. As Fawcett and Pawson discuss in their Perspective, activation of the N-WASP protein (which coordinates formation of actin filaments) is far more complex, depending on the interaction of N-WASP with both a protein and a phospholipid. The authors explain new results ( Prehoda et al.) demonstrating that cooperative binding of the phospholipid PIPand the small GTPase Cdc42 to N-WASP results in its activation. The Arp2/3 complex is then able to bind to N-WASP and to proceed with its job of initiating the assembly of actin monomers into actin filaments.Keywords
This publication has 7 references indexed in Scilit:
- Integration of Multiple Signals Through Cooperative Regulation of the N-WASP-Arp2/3 ComplexScience, 2000
- Mechanism of N-Wasp Activation by Cdc42 and Phosphatidylinositol 4,5-BisphosphateThe Journal of cell biology, 2000
- Activation by Cdc42 and Pip2 of Wiskott-Aldrich Syndrome Protein (Wasp) Stimulates Actin Nucleation by Arp2/3 ComplexThe Journal of cell biology, 2000
- Protein–protein interactions define specificity in signal transductionGenes & Development, 2000
- Autoinhibition and activation mechanisms of the Wiskott–Aldrich syndrome proteinNature, 2000
- The Interaction between N-WASP and the Arp2/3 Complex Links Cdc42-Dependent Signals to Actin AssemblyCell, 1999
- Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASPNature, 1998