Малые белки теплового шока способны защитить клетки млекопитающих от кофилинопатии
DOI:
https://doi.org/10.33910/2687-1270-2024-5-3-294-306Ключевые слова:
нейродегенеративные заболевания, цитоскелет клеток, ADF/кофилины, малый белок теплового шока, докинг белка в белок, шаперонная функцияАннотация
Регуляция динамики актинового цитоскелета играет фундаментальную роль в жизнедеятельности клетки. К группе актин-связывающих белков относится семейство актин-деполимеризующий фактор (ADF) / кофилины. Взаимодействие цитоскелета клеток нервной ткани с белками — представителями семейства ADF/кофилинов может приводить к развитию нейродегенеративных заболеваний. Для млекопитающих характерна экспрессия трех форм ADF/кофилинов: дестрин, кофилин-1 и кофилин-2. В то же время при стрессорных воздействиях в клетках млекопитающих экспрессируются малые белки теплового шока мБТШ27, для которых характерна широкая специфичность к белкам-мишеням. В предположении, что белок мБТШ27 способен связывать ряд ADF/кофилинов, с использованием программы ClusPro 2.0 был проведен докинг этих трех белков ADF/кофилинов в 24-мерный белковый комплекс мБТШ27. Показано, что сильнее всего с мБТШ27 связывается кофилин-1, затем дестрин и слабее всего — кофилин-2. При этом реконструкция F-актина — основного белка цитоскелета, ответственного за увеличение количества и размеров дендритных шипиков, а также синаптическую пластичность, модулируется именно кофилином-1. Таким образом, мБТШ27 способен осуществлять шаперонную функцию относительно ADF/кофилинов, защищая клетки от их высокой концентрации.
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