Recognition of multiple substrate motifs by the c-ABL protein tyrosine kinase.
Using a combinatorial peptide library that is based on the one-bead one-peptide approach we identified 14 peptide substrates for the c-ABL protein tyrosine kinase, which define three distinct consensus sequence groups. This is distinct from many serine/threonine kinases, which often phosphorylate only one major consensus sequence. The three consensus sequences accurately predict phosphorylation sites in cellular ABL substrates proven to play a role in cell signaling. Our data suggest that protein tyrosine kinases have evolved to recognize multiple substrate motifs.
Wu
Jinzi J
JJ
UC Davis Cancer Center, Department of Internal Medicine, Division of Hematology/Oncology, University of California, Davis, Sacramento, CA 95817, USA.
Afar
Daniel E H
DE
Phan
Hoang
H
Witte
Owen N
ON
Lam
Kit S
KS
D020816:Amino Acid Motifs; D000818:Animals; D016367:Baculoviridae / Q000235:genetics; D001665:Binding Sites; D016384:Consensus Sequence; D006801:Humans; D010452:Peptide Biosynthesis; D019151:Peptide Library; D010455:Peptides / Q000302:isolation & purification; D016315:Proto-Oncogene Proteins c-abl / Q000235:genetics / Q000378:metabolism*; D018411:Spodoptera / Q000235:genetics / Q000821:virology; D013379:Substrate Specificity
D019151:Peptide Library; D010455:Peptides; D016315:Proto-Oncogene Proteins c-abl