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Phalloidin |
| Phalloidin
is a toxin from the toadstool "Death Cap" (Amanita
phalloides) that binds actin (Löw
& Wieland 1974).
Binding is specific for F-actin and this has provided a very convenient
tool to study this distribution of F-actin in permeabilised cells since
fluorescent analogs can be synthesized that retain actin binding (Wulf
et al, 1979).
Phalloidin binds to actin at the junction between subunits (Barden
et al, 1987;
Faulstich et
al, 1993;
Steinmetz et
al, 1998)
and because this is not a site at which many actin-binding proteins
bind, most of the F-actin in cells is available for phalloidin
labelling. There are two notable exceptions, these being nebulin
and ADF/cofilins. Nebulin is an
unusual actin binding protein in that each molecule binds about as 200
actin monomers within the thin filament of muscle. The actin
binding site seems to compete directly with the nebulin-binding repeat (Ao
& Lehrer, 1995).
The ADF/cofilin group alter the twist of the actin filament so that the
junction between the monomers is altered in such a manner as to be no
longer suitable for phalloidin binding. The ADF/Cofilins therefore
appear to compete indirectly with phalloidin for binding. Gelsolin
may act likewise as they share a similar fold to ADF/cofilins and also
seems to compete for phalloidin binding (Allen
& Janmey, 1994). |
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| References:-
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