Polo-like Kinase Couples Cytoplasmic Protein Gradients in the C. elegans Zygote

Intracellular protein gradients underlie essential cellular and developmental processes, but the mechanisms by which they are established are incompletely understood. During the asymmetric division of the C. elegans zygote, the RNA-binding protein MEX-5 forms an anterior-rich cytoplasmic gradient that causes the RNA-binding protein POS-1 to form an opposing, posterior-rich gradient. We demonstrate that the polo-like kinase PLK-1 mediates the repulsive coupling between MEX-5 and POS-1 by increasing the mobility of POS-1 in the anterior. PLK-1 is enriched in the anterior cytoplasm and phosphorylates POS-1, which is both necessary and sufficient to increase POS-1 mobility. Regulation of POS-1 mobility depends on both the interaction between PLK-1 and MEX-5 and between MEX-5 and RNA, suggesting that MEX-5 may recruit PLK-1 to RNA in the anterior. The low concentration of MEX-5/PLK-1 in the posterior cytoplasm provides a permissive environment for the retention of POS-1, which depends on POS-1 RNA binding. Our findings describe a novel reaction/diffusion mechanism in which the asymmetric distribution of cytoplasmic PLK-1 couples two RNA-binding protein gradients, thereby partitioning the cytoplasm. •POS-1 segregation requires the interaction of MEX-5 with RNA and PLK-1•PLK-1 phosphorylation increases POS-1 mobility in the anterior cytoplasm•RNA binding mediates the retention of POS-1 in the posterior The mechanisms that polarize the cytoplasm are not understood. Han et al. show that the polo-like kinase PLK-1 regulates cytoplasmic polarization in the C. elegans zygote. PLK-1 acts with the RNA-binding protein MEX-5 to locally control the mobility of POS-1, thereby driving the formation of a POS-1 concentration gradient.