Principles of Kinase Regulation

作者: Bostjan Kobe , Bruce E. Kemp

DOI: 10.1016/B978-0-12-374145-5.00074-7

关键词: Retinoblastoma-like protein 1cGMP-dependent protein kinaseProtein familyAutophagy-related protein 13Allosteric regulationBiologyc-RafBiochemistryVesicle-associated membrane protein 8Cell biologyProtein kinase A

摘要: Publisher Summary Protein kinases represent one of the largest protein families, corresponding to 2 percent eukaryotic proteins. Their importance is further reflected in fact that phosphorylation most abundant type cellular regulation, affecting essentially every process, including metabolism, growth, differentiation, motility, membrane transport, learning, and memory. kinase can be regulated diverse ways, ranging from transcriptional control through subcellular localization recruitment substrates, structural chemical modifications proteins themselves. The specificity cell determined by a combination “peptide specificity” kinase, substrate recruitment, phosphatase activity. This chapter focuses on principles regulation activity at level. Allosteric widespread mechanism function; effectors bind regulatory sites distinct active site, usually inducing conformational changes influence generally bear no resemblance their target protein's substrate. Intrasteric extends enzyme classes beyond enzymes receptors targeting domains, acts intrasteric autoregulatory sequences (IARseq) resemble specific substrates or ligands varying extents. interactions typically result inhibition function, mechanisms used for activation, activators ligands, phosphorylation, proteolysis, reduction disulfide bonds, combinations these.

参考文章(57)
Richard A Engh, Dirk Bossemeyer, The protein kinase activity modulation sites: Advances in Enzyme Regulation. ,vol. 41, pp. 121- 149 ,(2001) , 10.1016/S0065-2571(00)00010-8
K. R. Weiss, B. E. Kemp, B. Kobe, J. Heierhorst, S. C. Feil, M. W. Parker, G. M. Benian, Giant protein kinases: domain interactions and structural basis of autoregulation. The EMBO Journal. ,vol. 15, pp. 6810- 6821 ,(1996) , 10.1002/J.1460-2075.1996.TB01072.X
Alicia A. Russo, Lily Tong, Jie-Oh Lee, Philip D. Jeffrey, Nikola P. Pavletich, Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4a. Nature. ,vol. 395, pp. 237- 243 ,(1998) , 10.1038/26155
Bostjan Kobe, Bruce E. Kemp, Active site-directed protein regulation Nature. ,vol. 402, pp. 373- 376 ,(1999) , 10.1038/46478
Deborah H. Brotherton, Venugopal Dhanaraj, Scott Wick, Leonardo Brizuela, Peter J. Domaille, Elena Volyanik, Xu Xu, Emilio Parisini, Brian O. Smith, Sharon J. Archer, Manuel Serrano, Stephen L. Brenner, Tom L. Blundell, Ernest D. Laue, Crystal structure of the complex of the cyclin D-dependent kinase Cdk6 bound to the cell-cycle inhibitor p19INK4d. Nature. ,vol. 395, pp. 244- 250 ,(1998) , 10.1038/26164
Olga Mayans, Peter F. M. van der Ven, Matthias Wilm, Alexander Mues, Paul Young, Dieter O. Fürst, Matthias Wilmanns, Mathias Gautel, Structural basis for activation of the titin kinase domain during myofibrillogenesis Nature. ,vol. 395, pp. 863- 869 ,(1998) , 10.1038/27603
Ernst ter Haar, Joyce T. Coll, Douglas A. Austen, Hsun-Mei Hsiao, Lora Swenson, Jugnu Jain, Structure of GSK3beta reveals a primed phosphorylation mechanism. Nature Structural & Molecular Biology. ,vol. 8, pp. 593- 596 ,(2001) , 10.1038/89624
Patricia Pellicena, John Kuriyan, Protein-protein interactions in the allosteric regulation of protein kinases. Current Opinion in Structural Biology. ,vol. 16, pp. 702- 709 ,(2006) , 10.1016/J.SBI.2006.10.007
Matthew G Gold, David Barford, David Komander, Lining the pockets of kinases and phosphatases. Current Opinion in Structural Biology. ,vol. 16, pp. 693- 701 ,(2006) , 10.1016/J.SBI.2006.10.006
Philip D. Jeffrey, Alicia A. Russo, Kornelia Polyak, Emma Gibbs, Jerard Hurwitz, Joan Massagué, Nikola P. Pavletich, Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex Nature. ,vol. 376, pp. 313- 320 ,(1995) , 10.1038/376313A0