"The last 247 amino acids of DGK-1 were sufficient for binding to constitutively active RHO-1(G14V) and, at a lower level, to wild-type RHO-1. This DGK-1 fragment contains the DGK accessory domain, which is C-terminal to the DGK catalytic domain in all DAG kinases."
We found that the dgk-1(ok1462) null mutation suppressed the defect caused by the rhgf-1(ok880) deletion mutation or overexpression of the RGA-5 GAP domain (Fig. 4d and Supplementary Table 2).
"In addition, double mutants of grk-2(gk268) with the constitutive egg laying mutants egl-30(ep271), goa-1(n1134), eat-16(ep273), and dgk-1(sy428) were partially rescued with exogenous 5-HT (Fig. 3C), whereas double mutants with grk-2(rt97) were completely rescued (Fig. 3D)."