C-terminal domain (CTD) small phosphatase-like 2 modulates the canonical bone morphogenetic protein (BMP) signaling and mesenchymal differentiation via smad dephosphorylation

Abstract

Background: Dephosphorylation of R-Smads in the nucleus shuts off TGF-β superfamily signaling. Results: SCP4 specifically dephosphorylates BMP-activated Smad1/5/8, but not TGF-β-activated Smad2/3, and ectopic expression of SCP4 inhibits BMP signaling, whereas SCP4 depletion enhances BMP signaling. Conclusion: SCP4 is a nuclear phosphatase terminating BMP signaling. Significance: Identification of SCP4 may suggest its physiological functions in BMP-induced cellular processes and relevant diseases.