Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly

Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly

Low complexity (LC) domains can drive the formation of both amyloid fibrils and protein droplets. Here, the authors identify reversible amyloid cores from the LC of hnRNPA1, based on which they elucidate the structural basis of reversible fibrillation and its interplay with hnRNPA1 droplet formation...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Xinrui Gui, Feng Luo, Yichen Li, Heng Zhou, Zhenheng Qin, Zhenying Liu, Jinge Gu, Muyun Xie, Kun Zhao, Bin Dai, Woo Shik Shin, Jianhua He, Lin He, Lin Jiang, Minglei Zhao, Bo Sun, Xueming Li, Cong Liu, Dan Li
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
Materias:
Science
Q
Acceso en línea:https://doaj.org/article/a160475f7cbf47d1b2ddb73a38f8b907
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
Descripción
Sumario:Low complexity (LC) domains can drive the formation of both amyloid fibrils and protein droplets. Here, the authors identify reversible amyloid cores from the LC of hnRNPA1, based on which they elucidate the structural basis of reversible fibrillation and its interplay with hnRNPA1 droplet formation.

Ejemplares similares