Key result
Adf1 proves essential for contractile ring formation and maintenance during cytokinesis in fission yeast.
Adf1 plays a critical role in the formation and maintenance of the contractile ring during cytokinesis in fission yeast through balanced collaboration with other cytoskeletal proteins.
No immediate clinical implications; extends cytoskeletal insights in fission yeast and leaves open conservation in mammalian cells.
The role of the actin-depolymerizing factor (ADF)/cofilin-family protein Adf1 in cytokinesis of fission yeast cells was studied. Adf1 was required for accumulation of actin at the division site by depolymerizing actin at the cell ends, assembly of the contractile ring through severing actin filaments, and maintenance of the contractile ring once formed. Genetic and cytological analyses suggested that it collaborates with profilin and capping protein in the mitotic reorganization of the actin cytoskeleton. Furthermore, it was unexpectedly found that Adf1 and myosin-II also collaborate in assembling the contractile ring. Tropomyosin was shown to antagonize the function of Adf1 in the contractile ring. We propose that formation and maintenance of the contractile ring are achieved by a balanced collaboration of these proteins.
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Nakano et al. (2006) studied Cytokinesis in fission yeast. Adf1 (actin-depolymerizing factor) was evaluated on Formation and maintenance of the contractile ring. Adf1 is required for the formation and maintenance of the contractile ring during cytokinesis in fission yeast, collaborating with profilin, capping protein, and myosin-II.
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