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在细胞分裂期间,丝状肌动蛋白结合蛋白cofilin在分裂沟处的浓度。

Concentration of cofilin, a small actin-binding protein, at the cleavage furrow during cytokinesis.

作者信息

Nagaoka R, Abe H, Kusano K, Obinata T

机构信息

Department of Biology, Faculty of Science, Chiba University, Japan.

出版信息

Cell Motil Cytoskeleton. 1995;30(1):1-7. doi: 10.1002/cm.970300102.

Abstract

Cofilin is a small actin-binding protein which regulates actin polymerization in a pH-dependent manner. Immunofluorescence microscopy with a monoclonal antibody for cofilin revealed that this protein is temporarily concentrated at the contractile ring during cytokinesis. Cofilin appeared to accumulate rapidly at the contractile ring during late stages of furrowing, and was finally enriched at the midbody. The concentration of cofilin at the contractile ring was observed in several kinds of cultured cells. Furthermore, cofilin introduced into living cells by a microinjection method was also concentrated at the contractile ring. These results suggest that cofilin is involved in actin reorganization during cytokinesis.

摘要

丝切蛋白是一种小的肌动蛋白结合蛋白,它以pH依赖的方式调节肌动蛋白聚合。用针对丝切蛋白的单克隆抗体进行免疫荧光显微镜观察发现,这种蛋白在胞质分裂期间暂时集中在收缩环处。在沟裂后期,丝切蛋白似乎在收缩环处迅速积累,最终在中体处富集。在几种培养细胞中都观察到了丝切蛋白在收缩环处的集中。此外,通过显微注射法导入活细胞的丝切蛋白也集中在收缩环处。这些结果表明,丝切蛋白参与了胞质分裂期间的肌动蛋白重组。

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