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Published online 13 November 2000. doi:10.1083/jcb.151.4.789
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© The Rockefeller University Press, 0021-9525/2000/11/789/ $5.00
The Journal of Cell Biology, Volume 151, Number 4, November 13, 2000 789-800

Original Article

Fission Yeast Myosin-I, Myo1p, Stimulates Actin Assembly by Arp2/3 Complex and Shares Functions with WASp

Wei-Lih Leea,b, Magdalena Bezanillab, and Thomas D. Pollardb
a Graduate Program in Biochemistry, Cellular and Molecular Biology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205
b Structural Biology Laboratory, The Salk Institute for Biological Studies, La Jolla, California 92037

Correspondence to: Thomas D. Pollard, The Salk Institute for Biological Studies, 10010 North Torrey Pines Rd., La Jolla, CA 92037. Tel:(858) 453-4100, ext

Fission yeast myo1+ encodes a myosin-I with all three tail homology domains (TH1, 2, 3) found in typical long-tailed myosin-Is. Myo1p tail also contains a COOH-terminal acidic region similar to the A-domain of WASp/Scar proteins and other fungal myosin-Is. Our analysis shows that Myo1p and Wsp1p, the fission yeast WASp-like protein, share functions and cooperate in controlling actin assembly. First, Myo1p localizes to cortical patches enriched at tips of growing cells and at sites of cell division. Myo1p patches partially colocalize with actin patches and are dependent on an intact actin cytoskeleton. Second, although deletion of myo1+ is not lethal, {Delta}myo1 cells have actin cytoskeletal defects, including loss of polarized cell growth, delocalized actin patches, and mating defects. Third, additional disruption of wsp1+ is synthetically lethal, suggesting that these genes may share functions. In mapping the domains of Myo1p tail that share function with Wsp1p, we discovered that a Myo1p construct with just the head and TH1 domains is sufficient for cortical localization and to rescue all {Delta}myo1 defects. However, it fails to rescue the {Delta}myo1 {Delta}wsp1 lethality. Additional tail domains, TH2 and TH3, are required to complement the double mutant. Fourth, we show that a recombinant Myo1p tail binds to Arp2/3 complex and activates its actin nucleation activity.

Key Words: fission yeast, myosin-I, WASp, Arp2/3 complex, actin assembly


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