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Papers In Press, published online ahead of print March 19, 2001
Ruttenberg Cancer Center, Mount Sinai School of Medicine, New York, NY 10029
Corresponding Author: zeev.ronai{at}mssm.edu
Modification of the ATP pocket on protein kinases allows selective use of an ATP analogue that exhibits high affinity for the altered kinases. Using this approach, we altered the ATP binding site on JNK and identified N6(2-phenythyl) ATP, a modified form of ATP that exhibits high specificity and affinity for the modified, but not the wt form, of JNK. Using modified JNK and its ATP analogue enables the detection of novel JNK substrates. Among substrates identified using this approach is heterogeneous nuclear ribonucleoprotein K (hnRNP-K), which is involved in transcription and post-transcriptional mRNA metabolism. The newly identified substrate can be phosphorylated by JNK on amino acids 216 and 353, which contribute to hnRNP-K mediated transcriptional activities.
J. Biol. Chem, 10.1074/jbc.M011396200
Submitted on December 18, 2000
Revised on March 19, 2001
Accepted on March 19, 2001
Identification of a new JNK substrate using ATP pocket mutant ADK and a corresponding ATP analogue
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