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Measuring In Vitro ATPase Activity for Enzymatic Characterization
Published on: August 23, 2016
The EphA8 receptor phosphorylates and activates low molecular weight phosphotyrosine protein phosphatase in vitro
1Department of Life Science, Sookmyung Women s University, 53-12 Chungpa-Dong 2-Ka, Yongsan-Ku, Seoul 140-742, Korea. scpark@sookmyung.ac.kr
Abstract:
Low molecular weight phosphotyrosine protein phosphatase (LMW-PTP) has been implicated in modulating the EphB1-mediated signaling pathway. In this study, we demonstrated that the EphA8 receptor phosphorylates LMW-PTP in vitro. In addition, we discovered that mixing these two proteins leads to EphA8 dephosphorylation in the absence of phosphatase inhibitors. Finally, we demonstrated that LMW-PTP, modified by the EphA8 autokinase activity, possesses enhanced catalytic activity in vitro. These results suggest that LMW-PTP may also participate in a feedback-control mechanism of the EphA8 receptor autokinase activity in vivo.
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