Journal
JOURNAL OF CELL BIOLOGY
Volume 151, Issue 4, Pages 789-799Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.151.4.789
Keywords
fission yeast; myosin-I; WASp; Arp2/3 complex; actin assembly
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Funding
- NIGMS NIH HHS [R37 GM026132, R01 GM026132, GM-26132] Funding Source: Medline
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Fission yeast myol(+) 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 myol(+) 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.
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