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Explores the roles of FBXO42 and CCDC6 in regulating phosphatases, suggesting new pathways for cellular signaling.
The Ser/Thr phosphoprotein phosphatases (PPPs, PP1-PP7) are major regulators of phospho-dependent signaling and precise regulation of their activity is essential for cellular homeostasis (Nilsson, 2019). Within the PPP family, PP2A, PP4 and PP6 holoenzymes share a common architecture composed of a catalytic subunit, a scaffolding subunit and distinct regulatory subunits conferring substrate specificity. A complex biogenesis pathway involving several proteins ensures the integrity of the catalytic subunit and proper formation of holoenzymes. In addition, regulated methylation of the terminal leucine residue on the catalytic subunit controls holoenzyme assembly. Three new studies identify the ubiquitin ligase FBXO42 and the coiled coil protein CCDC6 as regulators of PP4 and PP2A.
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Jakob Nilsson (2026) studied this question.
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