PPM1A Functions as a Smad Phosphatase to Terminate TGFβ Signaling

Abstract

(Cell 125, 915–928; June 2, 2006) We, the editors of Cell, published an Editorial Expression of Concern (http://dx.doi.org/10.1016/j.cell.2016.03.038) earlier this year regarding issues raised about Figures 2F, 2H, and 3G of the above article. Dr. Yao-Yun Liang, who performed the experiments in question, claimed to have manipulated his experiments to achieve pre-determined results. The corresponding author, Dr. Xin-Hua Feng, refuted the claims of falsification. In the intervening time, two independent labs have carried out experiments attempting to reproduce the data in question. This Editorial Note is to inform the community about the outcome of this process. Those two labs have now completed their experiments, and their data largely confirm the central conclusions drawn from the original figures. Although this does not resolve the conflicting claims, based on the information available to us at this time, we will take no further action. We would like to thank the independent labs who invested significant time and effort in ensuring the accuracy of the scientific record. PPM1A Functions as a Smad Phosphatase to Terminate TGFβ SignalingLin et al.CellApril 07, 2016In BriefCell 125, 915–928; June 2, 2006 Full-Text PDF Open ArchivePPM1A Functions as a Smad Phosphatase to Terminate TGFβ SignalingLin et al.CellJune 02, 2006In BriefTGFβ signaling controls diverse normal developmental processes and pathogenesis of diseases including cancer and autoimmune and fibrotic diseases. TGFβ responses are generally mediated through transcriptional functions of Smads. A key step in TGFβ signaling is ligand-induced phosphorylation of receptor-activated Smads (R-Smads) catalyzed by the TGFβ type I receptor kinase. However, the potential of Smad dephosphorylation as a regulatory mechanism of TGFβ signaling and the identity of Smad-specific phosphatases remain elusive. Full-Text PDF Open Archive