Journal
DEVELOPMENTAL CELL
Volume 20, Issue 4, Pages 540-549Publisher
CELL PRESS
DOI: 10.1016/j.devcel.2011.02.004
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Funding
- NIH [GM86603, GM21841]
- Jane Coffin Childs Post-doctoral Fellowship [61-1357]
- NSF
- Agouron Foundation
- DOE Office of Biological & Environmental Research
- Howard Hughes Medical Institute
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Septins are GTP-binding proteins that form ordered, rod-like multimeric complexes and polymerize into filaments, but how such supramolecular structure is related to septin function was unclear. In Saccharomyces cerevisiae, four septins form an apolar hetero-octamer (Cdc11-Cdc12-Cdc3-Cdc10-Cdc10-Cdc3-Cdc12-Cdc11) that associates end-to-end to form filaments. We show that septin filament assembly displays previously unanticipated plasticity. Cells lacking Cdc10 or Cdc11 are able to divide because the now-exposed subunits (Cdc3 or Cdc12, respectively) retain an ability to homodimerize via their so-called G interface, thereby allowing for filament assembly. In such cdc10 Delta and cdc11 Delta cells, the remaining septins, like wild-type complexes, localize to the cortex at the bud neck and compartmentalize nonseptin factors, consistent with a diffusion barrier composed of continuous filaments in intimate contact with the plasma membrane. Conversely, Cdc10 or Cdc11 mutants that cannot self-associate, but cap Cdc3 or Cdc12, respectively, prevent filament formation, block cortical localization, and kill cells.
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