In vivo and in vitro analyses reveal how a Cdc42 GTPase-activating protein (GAP) interacts with other negative polarity cues at old division sites in budding yeast. Mathematical modeling suggests that… Click to show full abstract
In vivo and in vitro analyses reveal how a Cdc42 GTPase-activating protein (GAP) interacts with other negative polarity cues at old division sites in budding yeast. Mathematical modeling suggests that spatial distribution of a Cdc42 GAP in coordination with G1 progression is critical for fine-tuning the orientation of the polarity axis.
               
Click one of the above tabs to view related content.