The Cdc42 GAP Rga6 promotes monopolar outgrowth of spores

The molecular mechanisms underlying the establishment of the monopolar growth of fission yeast spores have been less characterized. Here, we report that the Cdc42 GTPase-activating protein (GAP) Rga6 is required for promoting monopolar growth during spore germination. The absence of Rga6 increases the number of spores that grow in a bipolar fashion. Rga6 decorates the non-growing cortical region, binds phosphatidylinositol 4,5-bisphosphate, and colocalizes with the phosphatidylinositol 4,5-bisphosphate-binding protein Opy1. Overexpression of Opy1 diminishes the cortical localization of Rga6. The characteristic localization of Rga6 on the cell cortex depends on the C-terminal PBR region of Rga6. Moreover, engineered chimera composed of the Rga6 C-terminal PBR region fused to the GAP domain of Rga3 or Rga4 are sufficient to rescue the spore growth phenotype caused by the absence of Rga6. Hence, our work establishes a paradigm in which the lipid composition of the plasma membrane directs polarized cell growth by specifying the cortical localization of a GAP protein.

Automated summary

This study reveals the crucial role of the Cdc42 GTPase-activating protein (GAP) Rga6 in the monopolar growth of fission yeast spores. The absence of Rga6 leads to an increase in bipolar growth of spores. Rga6 decorates the non-growing cortical region, binds phosphatidylinositol 4,5-bisphosphate, and co-localizes with the phosphatidylinositol 4,5-bisphosphate-binding protein Opy1.