When Schizosaccharomyces pombe cells are too short to divide, Wee1 kinase inhibits mitotic entry. Once the cells have elongated, however, Cdr2, a major organiser of medial cortical nodes, is activated and, in concert with the direct Wee1 inhibitor Cdr1, inhibits Wee1 to promote cell division. Cdr2 also recruits Mid1 and other non-essential factors of the contractile ring, thus regulating where the cell will divide. Here (p. 2842), Anne Paoletti and colleagues mapped the molecular interactions by which Cdr2 organised the medial cortical node components to regulate mitotic entry and division plane positioning. They found that the ubiquitin-associated domain (UBA) of Cdr2 is essential for the activation of its kinase domain and for the recruitment of both Wee1 and Mid1 to the nodes. Interestingly, removal of the UBA domain did not affect Cdr1 node recruitment, and further investigation revealed that Cdr2 interacts with Cdr1 through the C-terminal basic and KA-1...

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