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2014 ; 71
(8
): 472-83
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Drebrin inhibits cofilin-induced severing of F-actin
#MMPMID25047716
Grintsevich EE
; Reisler E
Cytoskeleton (Hoboken)
2014[Aug]; 71
(8
): 472-83
PMID25047716
show ga
Molecular cross-talk between neuronal drebrin A and cofilin is believed to be a
part of the activity-dependent cytoskeleton-modulating pathway in dendritic
spines. Impairments in this pathway are implicated also in synaptic dysfunction
in Alzheimer's disease, Down syndrome, epilepsy, and normal aging. However, up to
now the molecular interplay between cofilin and drebrin has not been elucidated.
TIRF microscopy and solution experiments revealed that full length drebrin A or
its actin binding core (Drb1-300) inhibits, but do not abolish cofilin-induced
severing of actin filaments. Cosedimentation experiments showed that F-actin can
be fully occupied with combination of these two proteins. The dependence of
cofilin binding on fractional saturation of actin filaments with drebrin suggests
direct competition between these two proteins for F-actin binding. This implies
that cofilin and drebrin can either overcome or reverse the allosteric changes in
F-actin induced by the competitor's binding. The ability of cofilin to displace
drebrin from actin filaments is pH dependent and is facilitated at acidic pH
(6.8). Pre-steady state kinetic experiments reveal that both binding and
dissociation of drebrin to/from actin filaments is faster than that reported for
cooperative binding of cofilin. We found, that drebrin displacement by cofilin is
greatly inhibited when actin severing is abolished, which might be linked to the
cooperativity of drebrin binding to actin filaments. Our results contribute to
molecular understanding of the competitive interactions of drebrin and cofilin
with actin filaments.
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