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Submitted on May 19, 2006
Revised on July 31, 2006
Accepted on August 3, 2006

Peptide microarray analysis of substrate specificity of the transmembrane SER/THR kinase KPI-2 reveals reactivity with CFTR and phosphorylase

Hong Wang and David L. Brautigan

Center for Cell Signaling, University of Virginia, Charlottesville, VA 22908

Corresponding Author: db8g{at}virginia.edu

Human Lemur (Lmr) kinases are predicted to Tyr kinases based on sequences and are related to neurotrophin receptor Trk kinases. This study used homogeneous recombinant KPI-2 (Lmr2, LMTK2, Cprk, BREK) kinase domain and a library of 1154 peptides on a microarray to analyze substrate specificity. We found that KPI-2 is strictly a Ser/Thr kinase that reacts with Ser either preceded by or followed by Pro residues, but unlike other Pro-directed kinases does not strictly require an adjacent Pro residue. The most reactive peptide in the library corresponds to S737 of CFTR and the recombinant R domain of CFTR was a preferred substrate. Further, the KPI-2 kinase phosphorylated peptides corresponding to the single site in phosphorylase and purified phosphorylase b, making this only the second known phosphorylase b kinase. Phosphorylase was used as a specific substrate to show that KPI-2 is inhibited in living cells by addition of NGF or serum. The results demonstrate the utility of the peptide library to probe specificity and discover kinase substrates and offer a specific assay that reveals hormonal regulation of the activity of this unusual transmembrane kinase.


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