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(Received for publication, May 15, 1995; and in revised form, November 16, 1995)
The COOH-terminal Src kinase (Csk) is responsible for the
phosphorylation of the conserved, negative regulatory,
carboxyl-terminal tyrosine of most of the Src family protein tyrosine
kinases. Up to now, no stable binding of Csk to Src kinases has been
detected. We therefore decided to analyze this interaction using two
systems which allow detection of transient interaction. We produced and
purified recombinant proteins in the glutathione S-transferase
prokaryotic expression system. First, using real-time biospecific
interaction analysis (BIAcore), we detected in vitro a specific interaction between Csk and one of its substrates Lck,
a lymphocyte-specific member of the Src family. This interaction
requires the autophosphorylation of Lck on tyrosine 394 (the
phosphorylation of which is correlated with an increase of the kinase
activity) and involves a functional Csk SH2 domain. Second, using the
yeast two-hybrid system, we confirmed in vivo the physical
interaction between Csk and Lck. Furthermore, in vitro we
showed that autophosphorylation of Lck on tyrosine 394 enhances the
phosphorylation of Lck by Csk on the negative regulatory site, tyrosine
505, suggesting that activated Lck serves preferentially as substrate
for Csk. These findings might explain the mechanism(s) by which Csk
interacts with most of Src kinases to down-regulate their kinase
activity.
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