2I2Q

Fission Yeast cofilin

2I2Q の概要

• エントリーDOI: 10.2210/pdb2i2q/pdb
• 関連するPDBエントリー: 1COF
• 分子名称: Cofilin, SULFATE ION, LAURYL DIMETHYLAMINE-N-OXIDE, ... (5 entities in total)
• 機能のキーワード: n-terminal serine, actin-binding protein
• 由来する生物種: Schizosaccharomyces pombe (fission yeast)
• 細胞内の位置: Cytoplasm: P78929
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16310.66

構造登録者

Andrianantoandro, E.,Pollard, T.D. (登録日: 2006-08-16, 公開日: 2006-10-17, 最終更新日: 2023-08-30)

主引用文献

Andrianantoandro, E.,Pollard, T.D.
Mechanism of Actin Filament Turnover by Severing and Nucleation at Different Concentrations of ADF/Cofilin.
Mol.Cell, 24:13-23, 2006

PubMed Abstract: ADF/cofilins are key regulators of actin dynamics during cellular motility, yet their precise role and mechanism of action are shrouded in ambiguity. Direct observation of actin filaments by evanescent wave microscopy showed that cofilins from fission yeast and human do not increase the rate that pointed ends of actin filaments shorten beyond the rate for ADP-actin subunits, but both cofilins inhibit elongation and subunit dissociation at barbed ends. Direct observation also showed that cofilins from fission yeast, Acanthamoeba, and human sever actin filaments optimally at low-cofilin binding densities well below their K(d)s, but not at high binding densities. High concentrations of cofilin nucleate actin assembly. Thus, the action of cofilins in cells will depend on the local concentration of active cofilins: low concentrations favor severing, whereas high concentrations favor nucleation. These results establish a clear paradigm for actin turnover by cofilin in cells.

PubMed: 17018289
DOI: 10.1016/j.molcel.2006.08.006

実験手法

X-RAY DIFFRACTION (1.72 Å)