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Vol. 13, Issue 1, 183-194, January 2002
and
*Programs in Cellular Biotechnology and Actin-depolymerizing factor (ADF)/cofilins are essential regulators
of actin filament turnover. Several ADF/cofilin isoforms are found in
multicellular organisms, but their biological differences have remained
unclear. Herein, we show that three ADF/cofilins exist in mouse and
most likely in all other mammalian species. Northern blot and in situ
hybridization analyses demonstrate that cofilin-1 is expressed in most
cell types of embryos and adult mice. Cofilin-2 is expressed in muscle
cells and ADF is restricted to epithelia and endothelia. Although the
three mouse ADF/cofilins do not show actin isoform specificity, they
all depolymerize platelet actin filaments more efficiently than muscle
actin. Furthermore, these ADF/cofilins are biochemically different. The
epithelial-specific ADF is the most efficient in turning over actin
filaments and promotes a stronger pH-dependent actin filament
disassembly than the two other isoforms. The muscle-specific cofilin-2
has a weaker actin filament depolymerization activity and displays a
5-10-fold higher affinity for ATP-actin monomers than cofilin-1 and
ADF. In steady-state assays, cofilin-2 also promotes filament assembly rather than disassembly. Taken together, these data suggest that the
three biochemically distinct mammalian ADF/cofilin isoforms evolved to
fulfill specific requirements for actin filament dynamics in different
cell types.
Developmental
Biology, Institute of Biotechnology, Viikki Biocenter, University of
Helsinki, Helsinki, 00014 Finland
Corresponding author. E-mail
address: pekka.lappalainen{at}helsinki.fi.
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