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

doi:10.1083/jcb.148.2.353

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© The Rockefeller University Press, 0021-9525/2000/1/353/ $5.00
The Journal of Cell Biology, Volume 148, Number 2, January 24, 2000 353-362

Original Article

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

Marie Evangelista^a, Bert M. Klebl^b, Amy H.Y. Tong^a, Bradley A. Webb^a, Thomas Leeuw^b, Ekkehard Leberer^b, Malcolm Whiteway^b, David Y. Thomas^b, and Charles Boone^a
^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

Correspondence to: Charles Boone, Department of Biology, Earl Hall, Queen's University, Kingston, Ontario, K7L 3N6, Canada. Tel:(613) 533-6124 Fax:(613) 533-6617 E-mail:boonec{at}biology.queensu.ca.

Type I myosins are highly conserved actin-based molecular motorsthat localize to the actin-rich cortex and participate in motilityfunctions such as endocytosis, polarized morphogenesis, andcell migration. The COOH-terminal tail of yeast myosin-I proteins,Myo3p and Myo5p, contains an Src homology domain 3 (SH3) followedby an acidic domain. The myosin-I SH3 domain interacted withboth 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 geneticredundancy with the COOH-terminal acidic domain of Bee1p (Las17p),which controls Arp2/3-mediated actin nucleation. These findingssuggest that myosin-I proteins may participate in a diverseset of motility functions through a role in actin assembly.

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

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