A conserved amphipathic helix in WASP/Scar proteins is essential for activation of Arp2/3 complex View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2003-08

AUTHORS

Sanjay C Panchal, Donald A Kaiser, Eduardo Torres, Thomas D Pollard, Michael K Rosen

ABSTRACT

Members of the Wiskott-Aldrich syndrome protein (WASP) family link Rho GTPase signaling pathways to the cytoskeleton through a multiprotein assembly called Arp2/3 complex. The C-terminal VCA regions (verprolin-homology, central hydrophobic, and acidic regions) of WASP and its relatives stimulate Arp2/3 complex to nucleate actin filament branches. Here we show by differential line broadening in NMR spectra that the C (central) and A (acidic) segments of VCA domains from WASP, N-WASP and Scar bind Arp2/3 complex. The C regions of these proteins have a conserved sequence motif consisting of hydrophobic residues and an arginine residue. Point mutations in this conserved sequence motif suggest that it forms an amphipathic helix that is required in biochemical assays for activation of Arp2/3 complex. Key residues in this motif are buried through contacts with the GTPase binding domain in the autoinhibited structure of WASP and N-WASP, indicating that sequestration of these residues is an important aspect of autoinhibition. More... »

PAGES

591-598

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsb952

DOI

http://dx.doi.org/10.1038/nsb952

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1020429132

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/12872157


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