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Phase separation modulates the assembly and dynamics of a polarity-related scaffold-signaling hub.

Authors :
Tan, Wei
Cheng, Sihua
Li, Yingying
Li, Xiao-Yang
Lu, Ning
Sun, Jingxian
Tang, Guiyue
Yang, Yujiao
Cai, Kezhu
Li, Xuefei
Ou, Xijun
Gao, Xiang
Zhao, Guo-Ping
Childers, W. Seth
Zhao, Wei
Source :
Nature Communications; 11/23/2022, Vol. 13 Issue 1, p1-14, 14p
Publication Year :
2022

Abstract

Asymmetric cell division (ACD) produces morphologically and behaviorally distinct cells and is the primary way to generate cell diversity. In the model bacterium Caulobacter crescentus, the polarization of distinct scaffold-signaling hubs at the swarmer and stalked cell poles constitutes the basis of ACD. However, mechanisms involved in the formation of these hubs remain elusive. Here, we show that a swarmer-cell-pole scaffold, PodJ, forms biomolecular condensates both in vitro and in living cells via phase separation. The coiled-coil 4–6 and the intrinsically disordered regions are the primary domains that contribute to biomolecular condensate generation and signaling protein recruitment in PodJ. Moreover, a negative regulation of PodJ phase separation by the stalked-cell-pole scaffold protein SpmX is revealed. SpmX impedes PodJ cell-pole accumulation and affects its recruitment ability. Together, by modulating the assembly and dynamics of scaffold-signaling hubs, phase separation may serve as a general biophysical mechanism that underlies the regulation of ACD in bacteria and other organisms. The polarization of distinct scaffold-signaling hubs at opposite cell poles constitutes the basis of asymmetric cell division. Here, the authors show that phase separation serves as a general mechanism to regulate the assembly and dynamics of a new-pole scaffold-signaling hub. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
20411723
Volume :
13
Issue :
1
Database :
Complementary Index
Journal :
Nature Communications
Publication Type :
Academic Journal
Accession number :
160371600
Full Text :
https://doi.org/10.1038/s41467-022-35000-2