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bioRxiv · 10.64898/2026.08.19.745790

MO25 binds CBL-interacting protein kinases associated with ribonucleoprotein condensates and regulates meiotic exit

Vargova, A.·Faturova, J.·Cairo, A.·Jankujova, K.·Pecinkova, J.·Mikulkova, P.·Capitao, C.·Riha, K.
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Abstract

Meiotic (M)-bodies are multiphasic ribonucleoprotein (RNP) condensates composed of a P-body core surrounded by a stress granule-like shell that promote meiotic exit through transient translational repression. This process depends on the phosphoserine-binding protein SMG7, which recruits the meiotic regulator TDM1 to M-bodies during meiosis II. Here, we identify the evolutionarily conserved scaffold protein MO25 as a regulator of SMG7 and TDM1 partitioning into M-bodies in Arabidopsis thaliana. Disruption of MO25A1 enhances the accumulation of SMG7 and TDM1 in M-bodies and increases the reduced fertility in the hypomorphic smg7-6 mutant, which exhibits impaired M-body association. In fungi and animals, MO25 proteins act as allosteric activators of STE20-family kinases. Interaction screening revealed that, whereas Arabidopsis MO25B proteins interact with STE20-family MAP4K kinases, MO25A paralogues have evolved specificity toward a subset of CBL-interacting protein kinases (CIPKs). Notably, the MO25A-interacting CIPKs localize to diverse nuclear and cytoplasmic RNP condensates. Among them, CIPK6 is required for fertility and pollen development, and disruption of its MO25-binding domain enhances SMG7 condensation. Together, our findings identify a previously unrecognized MO25A-CIPK interaction module that regulates M-body organization and may more broadly contribute to the regulation of RNP condensates.

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Vargova, A., Faturova, J., Cairo, A., Jankujova, K., Pecinkova, J., Mikulkova, P., Capitao, C., Riha, K.. 2026-08-20. MO25 binds CBL-interacting protein kinases associated with ribonucleoprotein condensates and regulates meiotic exit. https://doi.org/10.64898/2026.08.19.745790

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