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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Hamaguchi, Tomonari Zhang, Xinjian Kozawa, Kei Kataoka, Chikako Amano, Mutsuki Shohag, Md Hasanuzzaman Yura, Yoshimitsu Kato, Katsuhiro Matsuura, Yoshiharu Nishioka, Tomoki Kaibuchi, Kozo |
| Description | Author Affiliation: Amano M ( Department of Cell Pharmacology, Graduate School of Medicine, Nagoya University, Showa-ku, Nagoya, Aichi 466-8550, Japan.); Hamaguchi T ( Department of Cell Pharmacology, Graduate School of Medicine, Nagoya University, Showa-ku, Nagoya, Aichi 466-8550, Japan.); Shohag MH ( Department of Cell Pharmacology, Graduate School of Medicine, Nagoya University, Showa-ku, Nagoya, Aichi 466-8550, Japan.); Kozawa K ( Department of Cell Pharmacology, Graduate School of Medicine, Nagoya University, Showa-ku, Nagoya, Aichi 466-8550, Japan.); Kato K ( Department of Cell Pharmacology, Graduate School of Medicine, Nagoya University, Showa-ku, Nagoya, Aichi 466-8550, Japan.); Zhang X ( Department of Cell Pharmacology, Graduate School of Medicine, Nagoya University, Showa-ku, Nagoya, Aichi 466-8550, Japan.); Yura Y ( Department of Cell Pharmacology, Graduate School of Medicine, Nagoya University, Showa-ku, Nagoya, Aichi 466-8550, Japan.); Matsuura Y ( Department of Molecular Virology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871, Japan.); Kataoka C ( Department of Molecular Virology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871, Japan.); Nishioka T ( Department of Cell Pharmacology, Graduate School of Medicine, Nagoya University, Showa-ku, Nagoya, Aichi 466-8550, Japan.); Kaibuchi K ( Department of Cell Pharmacology, Graduate School of Medicine, Nagoya University, Showa-ku, Nagoya, Aichi 466-8550, Japan kaibuchi@med.nagoya-u.ac.jp.) |
| Abstract | 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. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 6 |
| Volume Number | 209 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 2015-06-22 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | High-Throughput Screening Assays Membrane Proteins Metabolism Tumor Suppressor Proteins Rho-Associated Kinases Contractile Proteins Phosphorylation Substrate Specificity Research Support, Non-U.S. Gov't Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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