Finnigan GC, Booth EA, Duvalyan A, Liao EN, Thorner J

Septins are a conserved family of GTP-binding proteins that form hetero-octameric complexes that assemble into higher-order structures. In yeast, septin superstructure at the bud neck serves as a barrier to separate a daughter cell from its mother and as a scaffold to recruit the proteins that execute cytokinesis. However, how ...

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septins recruit specific factors has not been well characterized. In the preceding paper, we demonstrated that the C-terminal extensions (CTEs) of the alternative terminal subunits of septin hetero-octamers, Cdc11 and Shs1, share a role required for optimal septin function in vivo. Here we describe our use of unbiased genetic approaches (both selection of dosage suppressors and analysis of synthetic interactions) that pinpointed Bni5 as a protein that interacts with the CTEs of Cdc11 and Shs1. Furthermore, we used three independent methods- construction of chimeric proteins, non-covalent tethering mediated by a GFP-targeted nanobody, and imaging by fluorescence microscopy -to confirm that a physiological important function of the CTEs of Cdc11 and Shs1 is optimizing recruitment of Bni5 and thereby ensuring efficient localization at the bud neck of Myo1, the type II myosin of the actomyosin contractile ring.

Date: May. 12, 2015

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