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. 2014 May 9;3(3):383–394. doi: 10.1002/mbo3.177

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© 2014 The Authors. MicrobiologyOpen published by John Wiley & Sons Ltd.

This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

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Dephosphorylation of FPtk1 by Ltp1. (A) Incubation of FPtk1 with Ltp1 results in dephosphorylation and reduced kinase activity in the tyrosine kinase assay. Substitution of Cys with Ser at amino acid 10 (Ltp1 C10S) in the catalytically active domain of Ltp1 restored kinase activity. ***P < 0.001 compared to negative control. (B) Western immunoblot of FPtk1 incubated with Ltp1 or Ltp1 C10S, and with ATP or phosphatase inhibitor as indicated. The phosphorylation level of FPtk1 was determined by Western blotting with phosphotyrosine antibodies. (C) Densiometric analysis of band intensity from the blot in (B) using ImageJ to quantitate band density. *P < 0.05; ***P < 0.001 compared to FPtk1 + Ltp1.