Cortactin interacts with WIP in regulating Arp2/3 activation and membrane protrusion.

BACKGROUND: Modulation of actin cytoskeleton assembly is an integral step in many cellular events. A key regulator of actin polymerization is Arp2/3 complex. Cortactin, an F-actin binding protein that localizes to membrane ruffles, is an activator of Arp2/3 complex. RESULTS: A yeast two-hybrid screen revealed the interaction of the cortactin ...
Src homology 3 (SH3) domain with a peptide fragment derived from a cDNA encoding a region of WASp-Interacting Protein (WIP). GST-cortactin interacted with WIP in an SH3-dependent manner. The subcellular localization of cortactin and WIP coincided at the cell periphery. WIP increased the efficiency of cortactin-mediated Arp2/3 complex activation of actin polymerization in a concentration-dependent manner. Lastly, coexpression of cortactin and WIP stimulated membrane protrusions. CONCLUSIONS: WIP, a protein involved in filopodia formation, binds to both actin monomers and cortactin. Thus, recruitment of actin monomers to a cortactin-activated Arp2/3 complex likely leads to the observed increase in cortactin activation of Arp2/3 complex by WIP. These data suggest that a cortactin-WIP complex functions in regulating actin-based structures at the cell periphery.
Mesh Terms:
Actin-Related Protein 2, Actin-Related Protein 3, Actins, Animals, CHO Cells, Carrier Proteins, Cell Membrane, Cortactin, Cricetinae, Cytoskeletal Proteins, Humans, Intracellular Signaling Peptides and Proteins, Microfilament Proteins, Protein Structure, Tertiary
Curr. Biol.
Date: Mar. 04, 2003
Download Curated Data For This Publication
5738
Switch View:
  • Interactions 3