Popping at the poles

The polar organizing protein PopZ is an intrinsically disordered protein that regulates asymmetric cell division by forming microdomains at the cell poles of Caulobacter crescentus. To characterize how these microdomains form and their connection to cell-cycle function, Lasker et al. analyzed PopZ variants and revealed that microdomain formation is facilitated by PopZ phase separation. Specifically, the C-terminal oligomerization domain drives condensation and the intrinsically disordered region tunes the material properties through attractive forces and repulsive forces, respectively. Evaluation of solid and liquid PopZ condensates revealed that fluidity differentially influenced pole localization and client protein recruitment and required a tight balance to promote proper signaling and cell division. Leveraging these insights, the authors constructed a condensation platform in which PopZ was used in synthetic condensates to tune material properties, and studied their influence on condensate formation and function in eukaryotic cells. This ‘PopTag’ platform can potentially provide a means for helping to understand and interpret how specific condensate features contribute to normal physiology and pathogenesis.

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