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. 2018 Apr 2;217(4):1467–1483. doi: 10.1083/jcb.201708195

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© 2018 Merlini et al.

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Figure 4. — Gap1 is a GTPase Activating Protein for Ras1. (A) In vitro GAP assays: MBP-Gap1, but not catalytically inactive MBP-Gap1^R340A, increases the rate of GST-Ras1-GTP^γ32P hydrolysis; n = 3. (B) ^GSTRBD pulldown of extracts from h-cells of indicated genotypes. (C) GFP-Ras1 (left) and RasAct^GFP (right) in gap1Δ strains during vegetative growth (top) and mating (bottom). Arrowheads indicate shmoo tips. (D) Percentage of cell lysis of h90 WT and gap1 mutant (gap1^R340A, gap1^{R195A R340A}, and gap1Δ) cells treated with 1.2 M sorbitol or lacking fus1 after 14 h in MSL-N (n > 500 for three independent experiments); ***, 9.34 × 10⁻⁷ ≤ P ≤ 6.54 × 10⁻⁶. (E) Time course of cell lysis and cell pair formation in h90 gap1Δ cells placed in MSL-N (n > 200 for three independent experiments). (F) Type V myosins (Myo52-tdTomato and Myo51-3YFP), actin (GFP-CHD), formin Fus1-sfGFP, and cell wall glucanases (Eng2-sfGFP and Exg3-sfGFP) are focalized in unpaired gap1Δ cells (white arrowheads) but either not detectable or not focalized (red arrowheads) in WT cells not yet engaged in fusion (early paired cells shown). Bars, 2 µm. Plots show means and SDs.