Cargando…
Cofilin-induced unidirectional cooperative conformational changes in actin filaments revealed by high-speed atomic force microscopy
High-speed atomic force microscopy was employed to observe structural changes in actin filaments induced by cofilin binding. Consistent with previous electron and fluorescence microscopic studies, cofilin formed clusters along actin filaments, where the filaments were 2-nm thicker and the helical pi...
Autores principales: | Ngo, Kien Xuan, Kodera, Noriyuki, Katayama, Eisaku, Ando, Toshio, Uyeda, Taro QP |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4337605/ https://www.ncbi.nlm.nih.gov/pubmed/25642645 http://dx.doi.org/10.7554/eLife.04806 |
Ejemplares similares
-
Allosteric regulation by cooperative conformational changes of actin filaments drives mutually exclusive binding with cofilin and myosin
por: Ngo, Kien Xuan, et al.
Publicado: (2016) -
Cofilin-induced cooperative conformational changes of actin subunits revealed using cofilin-actin fusion protein
por: Umeki, Nobuhisa, et al.
Publicado: (2016) -
Actin-binding domain of Rng2 sparsely bound on F-actin strongly inhibits actin movement on myosin II
por: Hayakawa, Yuuki, et al.
Publicado: (2022) -
Lamellipodin promotes actin assembly by clustering Ena/VASP proteins and tethering them to actin filaments
por: Hansen, Scott D, et al.
Publicado: (2015) -
Bacterial actin MreB forms antiparallel double filaments
por: van den Ent, Fusinita, et al.
Publicado: (2014)