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Studying Cell Cycle-regulated Gene Expression by Two Complementary Cell Synchronization Protocols

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Cell cycle-specific phase separation regulated by protein charge blockiness.

Hiroya Yamazaki^1,2, Masatoshi Takagi³, Hidetaka Kosako⁴

¹Graduate School of Biostudies, Kyoto University, Kyoto, Japan.

Nature Cell Biology

|May 5, 2022

Summary

This summary is machine-generated.

Protein phosphorylation controls cell structure changes by altering protein charge blocks, influencing liquid-liquid phase separation (LLPS) and organelle behavior during the cell cycle.

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Area of Science:

Cell Biology
Biochemistry
Molecular Biology

Background:

Protein phosphorylation regulates intracellular organelle dynamics.
The role of phosphorylation in controlling interactions of unstructured proteins and their macroscopic behaviors is not well understood.

Purpose of the Study:

To investigate the cell cycle-specific behavior of the Ki-67 protein.
To elucidate how phosphorylation influences the liquid-liquid phase separation (LLPS) of unstructured proteins.

Main Methods:

Analysis of Ki-67 localization during different cell cycle phases.
In vitro and in vivo experiments using phosphomimetic sequences and modified protein domains.
Assessment of liquid-liquid phase separation (LLPS) propensity.

Main Results:

Mitotic hyperphosphorylation of Ki-67 creates alternating charge blocks, promoting LLPS and relocation to the chromosome periphery.
Enhanced charge blockiness in protein sequences promotes LLPS in vitro and chromosome periphery formation in vivo.
Phosphorylation of NPM1 reduces charge blockiness, suppresses LLPS, and leads to nucleolar dissolution.

Conclusions:

Cell cycle-specific phase separation is modulated by phosphorylation through altering charge blockiness in disordered protein regions.
Phosphorylation's impact on LLPS is dependent on its effect on protein charge distribution, not just site-specific modification.