دورية أكاديمية
The intrinsic substrate specificity of the human tyrosine kinome.
| العنوان: | The intrinsic substrate specificity of the human tyrosine kinome. |
|---|---|
| المؤلفون: | Yaron-Barir, Tomer M, Joughin, Brian A, Huntsman, Emily M, Kerelsky, Alexander, Cizin, Daniel M, Cohen, Benjamin M, Regev, Amit, Song, Junho, Vasan, Neil, Lin, Ting-Yu, Orozco, Jose M, Schoenherr, Christina, Sagum, Cari, Bedford, Mark T, Wynn, R Max, Tso, Shih-Chia, Chuang, David T, Li, Lei, Li, Shawn S-C, Creixell, Pau, Krismer, Konstantin, Takegami, Mina, Lee, Harin, Zhang, Bin, Lu, Jingyi, Cossentino, Ian, Landry, Sean D, Uduman, Mohamed, Blenis, John, Elemento, Olivier, Frame, Margaret C, Hornbeck, Peter V, Cantley, Lewis C, Turk, Benjamin E, Yaffe, Michael B, Johnson, Jared L |
| بيانات النشر: | Springer Science and Business Media LLC //dx.doi.org/10.1038/s41586-024-07407-y Nature |
| سنة النشر: | 2024 |
| المجموعة: | Apollo - University of Cambridge Repository |
| مصطلحات موضوعية: | Animals, Humans, Amino Acid Motifs, Evolution, Molecular, Mass Spectrometry, Phosphoproteins, Phosphorylation, Phosphotyrosine, Protein-Tyrosine Kinases, Proteome, Proteomics, Signal Transduction, src Homology Domains, Substrate Specificity, Tyrosine |
| الوصف: | Acknowledgements: We thank M. J. Begley, F. M. White, G. Getz, S. R. Hubbard, N. Shah and M. L. Hemming for discussions; and Y. Ma, M. R. Lundquist, K. Liberatore, T. M. Levy, S. A. Beausoleil, J. Wong, S. Petovic, M. Tran and the staff at Signalchem Biotech for technical assistance. T.M.Y.-B. thanks D. Yaron-Barir, S. Yaron, N. Yaron, J. R. Haddad and S. Haddad for their support. J.L.J. thanks M. Bak-Johnson, C. Ahn, S. Bak, J. W. Erickson and R. A. Cerione for their support. This research was supported by Leukemia & Lymphoma Society Award (to J.L.J. and L.C.C.); the Claudia Adams Barr Program for Cancer Research Award (to J.L.J.); National Institute of Health grants P01 CA120964 (to L.C.C.), R35-CA197588 (to L.C.C.), P01-CA117969 (to L.C.C.), R35-ES028374 (to M.B.Y.), R01-CA226898 (to M.B.Y.), R01-GM135331 (to B.E.T.) and R01-GM104047 (to B.E.T. and M.B.Y.); the joint Cancer Research UK and Brain Tumour Charity funded Brain Tumour Award C42454/A28596 (to M.B.Y.); the Charles and Marjorie Holloway Foundation (to M.B.Y.); the MIT Center for Precision Cancer Medicine (to M.B.Y.); the Jane Coffin Childs Memorial Fund (to J.M.O.); the Howard Hughes Medical Institute Hanna H. Gray Fellow award (to J.M.O.); and Cancer Research UK grants C9685/A26398 (to P.C.) and C9545/A29580 (to P.C.). ; Phosphorylation of proteins on tyrosine (Tyr) residues evolved in metazoan organisms as a mechanism of coordinating tissue growth1. Multicellular eukaryotes typically have more than 50 distinct protein Tyr kinases that catalyse the phosphorylation of thousands of Tyr residues throughout the proteome1-3. How a given Tyr kinase can phosphorylate a specific subset of proteins at unique Tyr sites is only partially understood4-7. Here we used combinatorial peptide arrays to profile the substrate sequence specificity of all human Tyr kinases. Globally, the Tyr kinases demonstrate considerable diversity in optimal patterns of residues surrounding the site of phosphorylation, revealing the functional organization of the human Tyr kinome ... |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | application/pdf; application/zip; text/xml |
| اللغة: | English |
| العلاقة: | https://www.repository.cam.ac.uk/handle/1810/369025Test |
| الإتاحة: | https://www.repository.cam.ac.uk/handle/1810/369025Test |
| رقم الانضمام: | edsbas.6B2D954E |
| قاعدة البيانات: | BASE |
| الوصف غير متاح. |