Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7754674 | Journal of Inorganic Biochemistry | 2016 | 7 Pages |
Abstract
The Mammalian Ste20 Kinase 3 (MST3) undergoes tyrosine phosphorylation. The proline-rich motif of MST3 may position it close to the oncoprotein Src Homology 3 (SH3) domains of adaptor proteins. The unusual tyrosine-phosphorylated MST3 may create a docking site for downstream molecules, resulting in MST3 involvement in various signals.145
Keywords
PLD1HEK 293SH3SH2MAP2KMAP kinase kinase kinaseMAP3KMDCKEGFRMAP kinase kinaseHPK1PAKGPCRste20PSPMST3DMEMMSTMAP4kCysPTPnuclear magnetic resonanceMAPKDulbecco's modified Eagle's mediumOkadaic acidTritonTriton X-100Kinase assayNMRCysteinePervanadateTyrosine phosphorylationPhospholipase D1Ionic strengthSrc Homology 2Src homology 3Protein tyrosine phosphataseProtein serine/threonine phosphatasehuman embryonic kidney 293Madin-Darby canine kidneyMAP kinasep21-activated kinaseEpidermal growth factor receptorG protein-coupled receptor
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
Wei-Chih Kan, Te-Ling Lu, Pin Ling, Te-Hsiu Lee, Chien-Yu Cho, Chi-Ying F. Huang, Wen-Yih Jeng, Yui-Ping Weng, Chun-Yen Chiang, Jin Bin Wu, Te-Jung Lu,