凝聚
核糖核酸
丝氨酸
RNA剪接
核运输
SR蛋白
支架蛋白
核蛋白
高分子
化学
细胞生物学
生物物理学
细胞核
生物
生物化学
信号转导
基因
磷酸化
转录因子
作者
Mengjun Zhang,Zhuang Gu,Shuanghui Guo,Yu Sun,Suibin Ma,Shuo Yang,Jin Guo,Chunhua Fang,Shu Li,Yifan Ge,Zhongwen Chen,Bo Wang
出处
期刊:Cell Reports
[Elsevier]
日期:2024-03-01
卷期号:43 (3): 113827-113827
被引量:1
标识
DOI:10.1016/j.celrep.2024.113827
摘要
Summary
Nuclear speckles (NSs) are nuclear biomolecular condensates that are postulated to form by macromolecular phase separation, although the detailed underlying forces driving NS formation remain elusive. SRRM2 and SON are 2 non-redundant scaffold proteins for NSs. How each individual protein governs assembly of the NS protein network and the functional relationship between SRRM2 and SON are largely unknown. Here, we uncover immiscible multiphases of SRRM2 and SON within NSs. SRRM2 and SON are functionally independent, specifically regulating alternative splicing of subsets of mRNA targets, respectively. We further show that SRRM2 forms multicomponent liquid phases in cells to drive NS subcompartmentalization, which is reliant on homotypic interaction and heterotypic non-selective protein-RNA complex coacervation-driven phase separation. SRRM2 serine/arginine-rich (RS) domains form higher-order oligomers and can be replaced by oligomerizable synthetic modules. The serine residues within the RS domains, however, play an irreplaceable role in fine-tuning the liquidity of NSs.
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