Selective Dephosphorylation by SCP1 and PP2A in Phosphorylated Residues of SMAD2

Abstract

Protein phosphatase is important for cellular events, and a family of protein phosphatases, the so-called C-terminal domain (CTD) of RNA polymerase II (RNAPII) phosphatases, has recently attracted attention. The CTD is the largest subunit of RNAPII and consists of a tandem repeated heptapeptide (Y 1 S 2 P 3 T 4 S 5 P 6 S 7 ).1 Seven active CTD phosphatases in the human genome are known and share the same catalytic domain architecture and DXDX(T/V) active site motif.2 Small CTD phosphatase 1 (SCP1) dephosphorylates the fifth phosphorylated serine of Y 1 S 2 P 3 T 4 S 5 P 6 S 7 in the CTD 2 and has been renamed CTD small phosphatase 1 (CTDSP1). Small CTD phosphatase 2 (SCP2) and small CTD phosphatase 3 (SCP3) have a similar sequence, threedimensional structure, and biochemical function to SCP1.

Chloramphenicol inhibits eukaryotic Ser/Thr phosphatase and infection-specific cell differentiation in the rice blast fungus

“…S5). Dullard is involved in cell differentiation in higher organisms; for example, Dullard acts as a negative regulator of TGF-β signaling for endochondral ossification via phosphorylation of Smad2/3 in mice 24,25 . M. oryzae harbored two paralogues of MoDULLARD , namely MoNEM1 (nuclear envelope morphology protein 1) (MGG_06001) and MoFCP1 (RNA polymerase II subunit A domain phosphatase 1) (MGG_03485).…”