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Structural basis of Arp2/3 complex inhibition by GMF, Coronin, and Arpinстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 11 марта 2017 г.
- Авторы: Sokolova Olga S., Chemeris Angelina, Guo Siyang, Alioto Salvatore L., Gandhi Meghal, Padrick Shae, Pechnikova Evgeniya, David Violaine, Gautreau Alexis, Goode Bruce L.
- Журнал: Journal of Molecular Biology
- Том: 429
- Номер: 2
- Год издания: 2017
- Издательство: Academic Press
- Местоположение издательства: United States
- Первая страница: 237
- Последняя страница: 248
- DOI: 10.1016/j.jmb.2016.11.030
- Аннотация: The evolutionarily conserved Arp2/3 complex plays a central role in nucleating the branched actin filament arrays that drive cell migration, endocytosis, and other processes. To better understand Arp2/3 complex regulation, we used single-particle electron microscopy to compare the structures of Arp2/3 complex bound to three different inhibitory ligands: glia maturation factor (GMF), Coronin, and Arpin. Although the three inhibitors have distinct binding sites on Arp2/3 complex, they each induced an "open" nucleation-inactive conformation. Coronin promoted a standard (previously described) open conformation of Arp2/3 complex, with the N-terminal β-propeller domain of Coronin positioned near the p35/ARPC2 subunit of Arp2/3 complex. GMF induced two distinct open conformations of Arp2/3 complex, which correlated with the two suggested binding sites for GMF. Furthermore, GMF synergized with Coronin in inhibiting actin nucleation by Arp2/3 complex. Arpin, which uses VCA-related acidic (A) motifs to interact with the Arp2/3 complex, induced the standard open conformation, and two new masses appeared at positions near Arp2 and Arp3. Furthermore, Arpin showed additive inhibitory effects on Arp2/3 complex with Coronin and GMF. Together, these data suggest that Arp2/3 complex conformation is highly polymorphic and that its activities can be controlled combinatorially by different inhibitory ligands.
- Добавил в систему: Соколова Ольга Сергеевна
Прикрепленные файлы
| № | Имя | Описание | Имя файла | Размер | Добавлен |
|---|---|---|---|---|---|
| 1. | Полный текст | 2017_Arp23.pdf | 2,4 МБ | 7 февраля 2017 [sokolova] |