Journal
CELL REPORTS
Volume 33, Issue 12, Pages -Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2020.108526
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Funding
- NIH [14PRE19740000, 15PRE21780003, 17PRE33410245, CA68485, DK20593, DK58404, DK59637, EY08126, S10 OD012324, R35GM119525, T32GM008554-21, R01GM101035, R35GM131799]
- American Heart Association [14PRE19740000, 15PRE21780003, 17PRE33410245]
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Many eukaryotes assemble an actin- and myosin-based cytokinetic ring (CR) on the plasma membrane (PM) for cell division, but how it is anchored there remains unclear. In Schizosaccharomyces pombe, the F-BAR protein Cdc15 links the PM via its F-BAR domain to proteins in the CR's interior via its SH3 domain. However, Cdc15's F-BAR domain also directly binds formin Cdc12, suggesting that Cdc15 may polymerize a protein network directly adjacent to the membrane. Here, we determine that the F-BAR domain binds Cdc1 2 using residues on the face opposite its membrane-binding surface. These residues also bind paxillin-like Px11, promoting its recruitment with calcineurin to the CR. Mutation of these F-BAR domain residues results in a shallower CR, with components localizing similar to 35% closer to the PM than in wild type, and aberrant CR constriction. Thus, F-BAR domains serve as oligomeric membrane-bound platforms that can modulate the architecture of an entire actin structure.
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