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J Biol Chem, Vol. 273, Issue 6, 3778-3783, February 6, 1998
From the Departments of Pathology and Cell Biology, Emory
University, Atlanta, Georgia 30322
The Caenorhabditis elegans unc-60
gene encodes two actin depolymerizing factor/cofilin proteins which are
implicated in the regulation of actin filament assembly in body wall
muscle. We examined the interaction of recombinant UNC-60A and B
proteins with actin and found that they differentially regulate actin
filament dynamics. Co-pelleting assays with F-actin showed that UNC-60A depolymerized but did not remain bound to F-actin, whereas UNC-60B bound to but did not depolymerize F-actin. In the pH range of 6.8-8.0, the apparent activities of UNC-60A and B did not change although UNC-60A showed greater actin-depolymerizing activity at higher
pH. These activities were further confirmed by a light scattering assay
and electron microscopy. The effects of these proteins on actin
polymerization were quite different. UNC-60A inhibited polymerization
in a concentration-dependent manner. On the other hand,
UNC-60B strongly inhibited the nucleation process but accelerated the
following elongation step. However, an excess amount of UNC-60B
increased the amount of unpolymerized actin. These results indicate
that UNC-60A depolymerizes actin filaments and inhibits actin
polymerization, whereas UNC-60B strongly binds to F-actin without
depolymerizing it and, through binding to G-actin, changes the rate of
actin polymerization depending on the UNC-60B:actin ratio. These data
suggest that the two UNC-60 isoforms play differential roles in
regulating actin filament dynamics in vivo.
Two Caenorhabditis elegans Actin Depolymerizing
Factor/Cofilin Proteins, Encoded by the unc-60 Gene,
Differentially Regulate Actin Filament Dynamics
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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