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2014 ; 71
(6
): 361-79
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Coordination of the filament stabilizing versus destabilizing activities of
cofilin through its secondary binding site on actin
#MMPMID24943913
Aggeli D
; Kish-Trier E
; Lin MC
; Haarer B
; Cingolani G
; Cooper JA
; Wilkens S
; Amberg DC
Cytoskeleton (Hoboken)
2014[Jun]; 71
(6
): 361-79
PMID24943913
show ga
Cofilin is a ubiquitous modulator of actin cytoskeleton dynamics that can both
stabilize and destabilize actin filaments depending on its concentration and/or
the presence of regulatory co-factors. Three charge-reversal mutants of yeast
cofilin, located in cofilin's filament-specific secondary binding site, were
characterized in order to understand why disruption of this site leads to
enhanced filament disassembly. Crystal structures of the mutants showed that the
mutations specifically affect the secondary actin-binding interface, leaving the
primary binding site unaltered. The mutant cofilins show enhanced activity
compared to wild-type cofilin in severing and disassembling actin filaments.
Electron microscopy and image analysis revealed long actin filaments in the
presence of wild-type cofilin, while the mutants induced many short filaments,
consistent with enhanced severing. Real-time fluorescence microscopy of labeled
actin filaments confirmed that the mutants, unlike wild-type cofilin, were
functioning as constitutively active severing proteins. In cells, the mutant
cofilins delayed endocytosis, which depends on rapid actin turnover. We conclude
that mutating cofilin's secondary actin-binding site increases cofilin's ability
to sever and de-polymerize actin filaments. We hypothesize that activators of
cofilin severing, like Aip1p, may act by disrupting the interface between
cofilin's secondary actin-binding site and the actin filament.