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The EphA8 receptor phosphorylates and activates low molecular weight phosphotyrosine protein phosphatase in vitro

Authors
Park, S
Issue Date
May-2003
Publisher
SPRINGER-VERLAG SINGAPORE PTE LTD
Keywords
Eph; EphA8; LMW-PTP; tyrosine kinase receptor
Citation
JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, v.36, no.3, pp.288 - 293
Journal Title
JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY
Volume
36
Number
3
Start Page
288
End Page
293
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/16188
DOI
10.5483/BMBRep.2003.36.3.288
ISSN
1225-8687
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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