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A more recent version of this article appeared on January 1, 2002
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Submitted on July 6, 2001
Revised on October 2, 2001
Accepted on October 3, 2001
1 University of Helsinki, Institute of Biotechnology
* Corresponding author. E-mail address: pekka.lappalainen{at}helsinki.fi.
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. Here 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.
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