Anomalies and Possible Data Fabrication/Falsification in the Paper Entitled "Greatwall-phosphorylated Endosulfine is both an inhibitor and a substrate of PP2A-B55 heterotrimers." Authored by Williams, B.C., Filter, J.J., Blake-Hodek, K.A., Fuda, N.J., Shalloway, D. and Goldberg, M.L. and Published in the Journal eLife [eLife (2014) e01695, doi: 10.7554/elife.01695].

In the paper entitled “Greatwall-phosphorylated α-Endosulfine is both an inhibitor and a substrate of PP2A-B55 heterotrimers." Authored by Williams, B.C., Filter, J.J., Blake-Hodek, K.A., Fuda, N.J., Shalloway, D. and Goldberg, M.L. and Published in the Journal eLife [eLife (2014) e01695, doi: 10.7554/elife.01695], the authors claimed that when α-Endosulfine was phosphorylated on serine 67 by Greatwall kinase, it became a potent inhibitor of PP2A-B55α and that phospho serine 67 of α-Endosulfine was also a substrate of PP2A-B55 α. It is submitted that the authors failed to show that serine 67 of α-Endosulfine was dephosphorylated by the enzyme that it inhibited. The phosphorylation dependent inhibition of PP2A-B55 by α-Endosulfine has more to do with science fiction than science as the authors did not seem to know how to perform a protein phosphatase inhibition assay. Anomalies and possible Data Fabrication/Falsification are discussed