美国约翰霍普金斯大学分子生物学和遗传学系GERALDINE SEYDOUX研究组发现界面蛋白簇对生物分子凝聚物的调控。2021年9月10日出版的《科学》发表了这项成果。

研究秀丽隐杆线虫的 P 颗粒时，他们发现其凝聚动力学受吸附到凝聚界面的蛋白质簇调节。 使用体外重组、现场观察和论证，他们证明 P 颗粒的局部组装受 MEG-3 控制，MEG-3 是一种内在无序的蛋白质，可在 P 颗粒上形成低动态组装。 遵循经典的 Pickering 乳液理论，MEG-3 簇可降低表面张力并减缓粗化。

在受精卵极化期间，MEG-3 招募 DYRK 家族激酶 MBK-2 以加速 P 颗粒乳液的空间调节生长。通过调节凝聚物 - 细胞质交换，界面簇调节生物分子凝聚物的结构完整性，让人想起脂质双层在膜结合细胞器中的作用。

据介绍，生物分子凝聚物是可以在没有限制膜的情况下通过相分离形成的细胞隔室。

附：英文原文

Title: Regulation of biomolecular condensates by interfacial protein clusters

Author: anonymous

Issue&Volume: 2021-09-10

Abstract: Biomolecular condensates are cellular compartments that can form by phase separation in the absence of limiting membranes. Studying the P granules of Caenorhabditis elegans, we find that condensate dynamics are regulated by protein clusters that adsorb to the condensate interface. Using in vitro reconstitution, live observations, and theory, we demonstrate that localized assembly of P granules is controlled by MEG-3, an intrinsically disordered protein that forms low dynamic assemblies on P granules. Following classic Pickering emulsion theory, MEG-3 clusters lower surface tension and slow down coarsening. During zygote polarization, MEG-3 recruits the DYRK family kinase MBK-2 to accelerate spatially regulated growth of the P granule emulsion. By tuning condensate-cytoplasm exchange, interfacial clusters regulate the structural integrity of biomolecular condensates, reminiscent of the role of lipid bilayers in membrane-bound organelles.

DOI: abg7071

Source: https://www.science.org/doi/10.1126/science.abg7071