Activation segment dimerization: a mechanism for kinase autophosphorylation of non-consensus sites
作者： Ashley C W Pike , Peter Rellos , Frank H Niesen , Andrew Turnbull , Antony W Oliver
DOI: 10.1038/EMBOJ.2008.8
关键词: Protomer 、 Protein kinase A 、 Active site 、 Autophosphorylation 、 Biophysics 、 Biochemistry 、 Protein structure 、 Biology 、 Phosphorylation 、 Kinase 、 Signal transduction
摘要: Protein kinase autophosphorylation of activation segment residues is a common regulatory mechanism in phosphorylation-dependent signalling cascades. However, the molecular mechanisms that guarantee specific and efficient phosphorylation these sites have not been elucidated. Here, we report on three novel diverse protein structures reveal an exchanged conformation. This dimeric arrangement results active conformation trans, with close proximity to site interacting protomer. Analytical ultracentrifugation chemical cross-linking confirmed presence dimers solution. Consensus substrate sequences for each showed identified are non-consensus sites. Based presented structural functional data, model at proposed likely be other kinases from subfamilies.
rcsb.org
unirioja.es
sussex.ac.uk
nature.com参考文章(47)
W. L. Delano, The PyMOL Molecular Graphics System DeLano Scientific. ,(2002)
Richard J. Morris, Anastassis Perrakis, Victor S. Lamzin, ARP/wARP and automatic interpretation of protein electron density maps. Methods in Enzymology. ,vol. 374, pp. 229- 244 ,(2003) , 10.1016/S0076-6879(03)74011-7
Taro Kawai, Makoto Matsumoto, Kiyoshi Takeda, Hideki Sanjo, Shizuo Akira, ZIP Kinase, a Novel Serine/Threonine Kinase Which Mediates Apoptosis Molecular and Cellular Biology. ,vol. 18, pp. 1642- 1651 ,(1998) , 10.1128/MCB.18.3.1642
Michelle Pirruccello, Holger Sondermann, Jeffrey G. Pelton, Patricia Pellicena, André Hoelz, Jonathan Chernoff, David E. Wemmer, John Kuriyan, A dimeric kinase assembly underlying autophosphorylation in the p21 activated kinases. Journal of Molecular Biology. ,vol. 361, pp. 312- 326 ,(2006) , 10.1016/J.JMB.2006.06.017
Jeyanthy Eswaran, Wen Hwa Lee, Judit É. Debreczeni, Panagis Filippakopoulos, Andrew Turnbull, Oleg Fedorov, Sean W. Deacon, Jeffrey R. Peterson, Stefan Knapp, Crystal Structures of the P21-Activated Kinases Pak4, Pak5, and Pak6 Reveal Catalytic Domain Plasticity of Active Group II Paks. Structure. ,vol. 15, pp. 201- 213 ,(2007) , 10.1016/J.STR.2007.01.001
Claudine N. Prowse, John Lew, Mechanism of Activation of ERK2 by Dual Phosphorylation Journal of Biological Chemistry. ,vol. 276, pp. 99- 103 ,(2001) , 10.1074/JBC.M008137200
Paul G. O'Reilly, Simona Wagner, Douglas J. Franks, Katia Cailliau, Edith Browaeys, Colette Dissous, Luc A. Sabourin, The Ste20-like Kinase SLK Is Required for Cell Cycle Progression through G2 Journal of Biological Chemistry. ,vol. 280, pp. 42383- 42390 ,(2005) , 10.1074/JBC.M510763200
Frank H Niesen, Helena Berglund, Masoud Vedadi, The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability Nature Protocols. ,vol. 2, pp. 2212- 2221 ,(2007) , 10.1038/NPROT.2007.321
Jessica E Hutti, Emily T Jarrell, James D Chang, Derek W Abbott, Peter Storz, Alex Toker, Lewis C Cantley, Benjamin E Turk, A rapid method for determining protein kinase phosphorylation specificity. Nature Methods. ,vol. 1, pp. 27- 29 ,(2004) , 10.1038/NMETH708
Chang-Hun Lee, Jay H. Chung, The hCds1 (Chk2)-FHA Domain Is Essential for a Chain of Phosphorylation Events on hCds1 That Is Induced by Ionizing Radiation Journal of Biological Chemistry. ,vol. 276, pp. 30537- 30541 ,(2001) , 10.1074/JBC.M104414200