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© The Rockefeller University Press, 0021-9525/2000//353 $5.00
The Journal of Cell Biology, Volume 148, Number 2, , 2000 353-362

Original Article

A Role for Myosin-I in Actin Assembly through Interactions with Vrp1p, Bee1p, and the Arp2/3 Complex



Marie Evangelistaa, Bert M. Kleblb, Amy H.Y. Tonga, Bradley A. Webba, Thomas Leeuwb, Ekkehard Lebererb, Malcolm Whitewayb, David Y. Thomasb, and Charles Boonea

a Department of Biology, Queen's University, Kingston, Ontario, K7L 3N6, Canada
b Genetics Division, Institut de Recherche en Biotechnologie, 6100, Avenue Royalmount, Montreal, Quebec, H4P 2R2, Canada
Department of Biology, Earl Hall, Queen's University, Kingston, Ontario, K7L 3N6, Canada.(613) 533-6617(613) 533-6124

boonec{at}biology.queensu.ca

Type I myosins are highly conserved actin-based molecular motors that localize to the actin-rich cortex and participate in motility functions such as endocytosis, polarized morphogenesis, and cell migration. The COOH-terminal tail of yeast myosin-I proteins, Myo3p and Myo5p, contains an Src homology domain 3 (SH3) followed by an acidic domain. The myosin-I SH3 domain interacted with both Bee1p and Vrp1p, yeast homologues of human WASP and WIP, adapter proteins that link actin assembly and signaling molecules. The myosin-I acidic domain interacted with Arp2/3 complex subunits, Arc40p and Arc19p, and showed both sequence similarity and genetic redundancy with the COOH-terminal acidic domain of Bee1p (Las17p), which controls Arp2/3-mediated actin nucleation. These findings suggest that myosin-I proteins may participate in a diverse set of motility functions through a role in actin assembly.

Key Words: yeast • myosin-I • Arp2/3 • actin assembly • WASP

© 2000 The Rockefeller University Press

Abbreviations used in this paper: AD, acidic domain; DIC, differential interference contrast; GFP, green fluorescent protein; GST, glutathione-S-transferase; HA, hemagglutinin; MBP, maltose binding protein; SH3, Src homology domain 3; WH2, WASP homology domain 2.


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