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J Biol Chem, Vol. 273, Issue 15, 8691-8698, April 10, 1998
and p59fyn
From the Cell Regulation Laboratory, Institute of Molecular and
Cell Biology, National University of Singapore, 30 Medical Drive,
Singapore 117609, Republic of Singapore
We have examined the in vivo activity
of receptor-like protein-tyrosine phosphatase 
(PTP) toward
p59fyn, a widely expressed Src family kinase. In a coexpression
system, PTP effected a dose-dependent tyrosine
dephosphorylation and activation of p59fyn, where maximal
dephosphorylation correlated with a 5-fold increase in kinase activity.
PTP expression resulted in increased accessibility of the
p59fyn SH2 domain, consistent with a PTP-mediated
dephosphorylation of the regulatory C-terminal tyrosine residue of
p59fyn. No p59fyn dephosphorylation was observed with
an enzymatically inactive mutant form of PTP or with another
receptor-like PTP, CD45. Many enzyme-linked receptors are complexed
with their substrates, and we examined whether PTP and
p59fyn underwent association. Reciprocal immunoprecipitations
and assays detected p59fyn and an appropriate kinase activity
in PTP immunoprecipitates and PTP and PTP activity in
p59fyn immunoprecipitates. No association between CD45 and
p59fyn was detected in similar experiments. The PTP-mediated
activation of p59fyn is not prerequisite for association since
wild-type and inactive mutant PTP bound equally well to
p59fyn. Endogenous PTP and p59fyn were also found in
association in mouse brain. Together, these results demonstrate a
physical and functional interaction of PTP and p59fyn that
may be of importance in PTP-initiated signaling events.
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