Model for Pom1-dependent regulation of Cdr2 node assembly to restrict Cdr2 nodes to the medial cortex. Cdr2 binding to the plasma membrane depends on Cdr2 C terminus containing a KA-1 domain and basic motif that establish electrostatic interaction with acidic phospholipids such as phosphatidylserine. Cdr2 clustering relies on a unique property of Cdr2 KA-1 domain involving the hydrophobic loop (FF) as well as on Cdr2 N-terminal region in a Mid1-dependent manner. Pom1 prevents node assembly at the cell tips by phosphorylating the basic motif, reducing its affinity for lipids, and by modulating the Cdr2 N-terminal interaction with Mid1 involved in clustering. This second regulation exerted by Pom1 could result indirectly from an inhibition of Cdr2 activity by Pom1 kinase. Cter, C terminus; P, phosphorylation.