Identification of Protein Kinase Substrates by the Kinase‐Interacting Substrate Screening (KISS) Approach. Issue 1 (1st September 2016)

• Record Type: Journal Article
• Authors: Amano, Mutsuki; Nishioka, Tomoki; Yura, Yoshimitsu; Kaibuchi, Kozo
• Editors: Bonifacino, Juan S.; Dasso, Mary; Harford, Joe B.; Lippincott‐Schwartz, Jennifer; Yamada, Kenneth M.
• Is Part Of: Current protocols in cell biology. Volume 72: Issue 1(2016)
• Page Start: 14.16.1
• Page End: 14.16.12
• Publication Date: 2016-09-01
• Subjects: kiss -- kinase -- phosphorylation -- phosphoproteomics -- mass spectrometry; Cytology -- Laboratory manuals; Cytological Techniques; Cytology; Periodicals; 571.6028
• DOI: 10.1002/cpcb.8
• Languages: English
• ISSNs: 1934-2500

Abstract

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.