| 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.493 table IVPubMed 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 |
"[Researchers] tracked the movements of nodes marked with Rlc1p-
3GFP at 1-s intervals in a confocal section of the top of cells at
25°C to understand the defects in cofilin mutant cells. Nodes
moved at the same velocity in wild-type and adf1-M2 cells and
in adf1-M3 cells (Fig. 5 B and Table IV). However, nodes in cofilin mutant cells moved longer total distances over longer
times between pauses (Fig. 5, C and D, Table IV): 27% of nodes
in adf1-M2 cells moved for >30 s, compared with only 5% in
wild-type cells (Fig. 5 C and Table IV)." See notes beneath table |
| Entered by |
Uri M |
| ID |
111105 |