title: Identification of Protein Kinase Substrates by the Kinase-Interacting Substrate Screening (KISS) Approach.
abstract: Identifying the substrates of protein kinases to understand their modes of action has been undertaken by various approaches and remains an ongoing challenge. Phosphoproteomic technologies have accelerated the accumulation of data concerning protein phosphorylation and have uncovered vast numbers of phosphorylation sites in vivo. In this unit, a novel in vitro screening approach for protein kinase substrates is presented, based on protein-protein interaction and mass spectrometry-based phosphoproteomic technology. © 2016 by John Wiley & Sons, Inc.
authors: Department of Cell Pharmacology, Graduate School of Medicine, Nagoya University, Nagoya, Aichi, Japan.
authors: Mutsuki
authors: M
authors: Amano
authors: Department of Cell Pharmacology, Graduate School of Medicine, Nagoya University, Nagoya, Aichi, Japan.
authors: Tomoki
authors: T
authors: Nishioka
authors: Department of Cell Pharmacology, Graduate School of Medicine, Nagoya University, Nagoya, Aichi, Japan.
authors: Yoshimitsu
authors: Y
authors: Yura
authors: Department of Cell Pharmacology, Graduate School of Medicine, Nagoya University, Nagoya, Aichi, Japan.
authors: Kozo
authors: K
authors: Kaibuchi
mesh_terms: D000645:Ammonium Sulfate / Q000737:chemistry; D000818:Animals; D001671:Biochemistry / Q000379:methods*; D001921:Brain / Q000378:metabolism; D011232:Chemical Precipitation; D002853:Chromatography, Liquid; D010748:Phosphopeptides / Q000032:analysis; D011485:Protein Binding; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D013379:Substrate Specificity; D053719:Tandem Mass Spectrometry; D014020:Tissue Extracts / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism
chemical_list: D010748:Phosphopeptides; D014020:Tissue Extracts; D011494:Protein Kinases; D014357:Trypsin; D000645:Ammonium Sulfate
keywords: kinase; kiss; mass spectrometry; phosphoproteomics; phosphorylation