ArticleBiochemistry2013
Profiling the substrate specificity of protein kinases by on-bead screening of peptide libraries.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- Synthetic Substrate Discovery for Hck Kinase via Phage Display.Biochemistry · 2026Article
- Catalytic activities of wild-type C. elegans DAF-2 kinase and dauer-associated mutants.The FEBS journal · 2024Article
- Biochemical characterization of the Drosophila insulin receptor kinase and longevity-associated mutants.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024Article
- Article
- Mitogen-Activated Protein Kinase and Substrate Identification in Plant Growth and Development.International journal of molecular sciences · 2022Review
- Kinase Substrate Profiling Using a Proteome-wide Serine-Oriented Human Peptide Library.Biochemistry · 2018Article
- Homing in: Mechanisms of Substrate Targeting by Protein Kinases.Trends in biochemical sciences · 2018Review
- Recognition of sites of functional specialisation in all known eukaryotic protein kinase families.PLoS computational biology · 2018Article
- Chromodomain Ligand Optimization via Target-Class Directed Combinatorial Repurposing.ACS chemical biology · 2016Article
- Identification and characterization of the role of c-terminal Src kinase in dengue virus replication.Scientific reports · 2016Article
- Rapid Identification of Protein Kinase Phosphorylation Site Motifs Using Combinatorial Peptide Libraries.Methods in molecular biology (Clifton, N.J.) · 2016Article
- Pim1 kinase promotes angiogenesis through phosphorylation of endothelial nitric oxide synthase at Ser-633.Cardiovascular research · 2016Article
- Diverse levels of sequence selectivity and catalytic efficiency of protein-tyrosine phosphatases.Biochemistry · 2014Article
- Correlated matrix-assisted laser desorption/ionization mass spectrometry and fluorescent imaging of photocleavable peptide-coded random bead-arrays.Rapid communications in mass spectrometry : RCM · 2014Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
A robust, high-throughput method has been developed to screen one-bead-one-compound peptide libraries to systematically profile the sequence specificity of protein kinases. Its ability to provide individual sequences of the preferred substrates permits the identification of sequence contextual effects and nonpermissive residues. Application of the library method to kinases Pim1, MKK6, and Csk revealed that Pim1 and Csk are highly active toward peptide substrates and recognize specific sequence motifs, whereas MKK6 has little activity or sequence selectivity against peptide substrates. Pim1 recognizes peptide substrates of the consensus RXR(H/R)X(S/T); it accepts essentially any amino acid at the S/T-2 and S/T+1 positions, but strongly disfavors acidic residues (Asp or Glu) at the S/T-2 position and a proline residue at the S/T+1 position. The selected Csk substrates show strong sequence covariance and fall into two classes with the consensus sequences of (D/E)EPIYϕXϕ and (D/E)(E/D)S(E/D/I)YϕXϕ (where X is any amino acid and ϕ is a hydrophobic amino acid). Database searches and in vitro kinase assays identified phosphatase PTP-PEST as a Pim1 substrate and phosphatase SHP-1 as a potential Csk substrate. Our results demonstrate that the sequence specificity of protein kinases is defined not only by favorable interactions between permissive residue(s) on the substrate and their cognate binding site(s) on the kinase but also by repulsive interactions between the kinase and nonpermissive residue(s).
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