Journal
JOURNAL OF CELL BIOLOGY
Volume 209, Issue 6, Pages 895-912Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201412008
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Funding
- Ministry of Education, Culture, Sports, Science and Technology of Japan (MEXT) [20227006, 25251021, 23590357, 25113513]
- MEXT
- Grants-in-Aid for Scientific Research [221S0003, 25113513, 23590357, 25251021, 15H01209, 20227006] Funding Source: KAKEN
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Protein kinases play pivotal roles in numerous cellular functions; however, the specific substrates of each protein kinase have not been fully elucidated. We have developed a novel method called kinase-interacting substrate screening (KISS). Using this method, 356 phosphorylation sites of 140 proteins were identified as candidate substrates for Rho-associated kinase (Rho-kinase/ROCK2), including known substrates. The KISS method was also applied to additional kinases, including PKA, MAPK1, CDK5, CaMK1, PAK7, PKN, LYN, and FYN, and a lot of candidate substrates and their phosphorylation sites were determined, most of which have not been reported previously. Among the candidate substrates for Rho-kinase, several functional clusters were identified, including the polarity-associated proteins, such as Scrib. We found that Scrib plays a crucial role in the regulation of subcellular contractility by assembling into a ternary complex with Rho-kinase and Shroom2 in a phosphorylation-dependent manner. We propose that the KISS method is a comprehensive and useful substrate screen for various kinases.
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