Abstract
The C-terminal Src Kinase (CSK) is responsible for the phosphorylation of the negative regulatory carboxy terminal tyrosine of several members of the Src family. CSK is unique among the members of the protein tyrosine kinase family because it lacks the conserved tyrosine autophosphorylation site. Using the glutathione S-transferase (GST) bacterial expression system (Smith & Johnson, 1988), we have produced large amounts of a chimeric rat CSK protein. We have determined that the GST-CSK fusion protein isolated from bacteria is phosphorylated on tyrosine residue(s) and is capable of undergoing phosphorylation on tyrosine residue(s) in vitro. Such autophosphorylation of CSK might have a role in the regulation of its kinase activity.
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© 1993 Springer-Verlag Berlin Heidelberg
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Bougeret, C., Fischer, S., Benarous, R. (1993). Recombinant CSK Expressed in E.Coli is Phosphorylated on Tyrosine Residue(s) and Undergoes in Vitro Phosphorylation. In: Heilmeyer, L.M.G. (eds) Tyrosine Phosphorylation/Dephosphorylation and Downstream Signalling. NATO ASI Series, vol 76. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-78247-3_16
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DOI: https://doi.org/10.1007/978-3-642-78247-3_16
Publisher Name: Springer, Berlin, Heidelberg
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