Cytokinesis defects of cofilin wildtype & mutant cells

Range Table - link
Organism Fission yeast Schizosaccharomyces pombe
Reference Chen Q, Pollard TD. Actin filament severing by cofilin is more important for assembly than constriction of the cytokinetic contractile ring. J Cell Biol. 2011 Oct 31 195(3):485-98. doi: 10.1083/jcb.201103067. p.490 table IIIPubMed ID22024167
Method "[Researchers] tested the hypothesis that the role of cofilin in cytokinesis is to sever actin filaments during assembly of contractile rings. [Their] initial observations of the temperature-sensitive cofilin adf1-1 strain by fluorescence microscopy of live cells showed that precursors called nodes failed to condense into a contractile ring at the restrictive temperature. The adf1-1 cofilin protein (L57S) was not sufficiently stable to purify, so [they] created seven new mutations based on temperature-sensitive mutations of budding yeast cofilin (Lappalainen et al., 1997)."
Comments "At 25°C the average rate of contractile ring constriction was the same in wild-type, adf1-M2, and adf1-M3 cells (Fig. 7 E and Table III), but the rates of constriction were much more variable in mutant cells (Fig. 7, A–C). Pauses did not account for the slower rates because each ring constricted at a constant rate (Fig. 7 D)."
Entered by Uri M
ID 111104