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Cdc42EP3-bound septin filaments promote actin filament assembly
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Septins are filament-forming proteins that are involved in numerous cellular processes. Septins co-localize with actin, microtubule and membrane structures. The Cdc42 effector protein Cdc42EP3 (also known as BORG2) regulates septin localization to cellular actin structures, but it is unknown how Cdc42EP3 controls septin-actin association. Using biochemical analysis with purified components, I show that Cdc42EP3 binds to both septins and actin in a Cdc42-regulated fashion. Importantly, septin-bound Cdc42EP3 accelerates actin filament polymerization. Septin filaments composed of SEPT2, SEPT6 and SEPT7 directly interact with actin filaments, although this occurs less efficiently in pre-formed filaments. Thus, Cdc42EP3 is not needed to recruit actin filaments to septin filaments at equilibrium. Instead, Cdc42EP3 recruits actin monomers to septin filaments, promoting localized actin filament formation and septin-actin structure assembly.
Title: Cdc42EP3-bound septin filaments promote actin filament assembly
Description:
Septins are filament-forming proteins that are involved in numerous cellular processes.
Septins co-localize with actin, microtubule and membrane structures.
The Cdc42 effector protein Cdc42EP3 (also known as BORG2) regulates septin localization to cellular actin structures, but it is unknown how Cdc42EP3 controls septin-actin association.
Using biochemical analysis with purified components, I show that Cdc42EP3 binds to both septins and actin in a Cdc42-regulated fashion.
Importantly, septin-bound Cdc42EP3 accelerates actin filament polymerization.
Septin filaments composed of SEPT2, SEPT6 and SEPT7 directly interact with actin filaments, although this occurs less efficiently in pre-formed filaments.
Thus, Cdc42EP3 is not needed to recruit actin filaments to septin filaments at equilibrium.
Instead, Cdc42EP3 recruits actin monomers to septin filaments, promoting localized actin filament formation and septin-actin structure assembly.
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