Three-dimensional docking in the MAPK p38α

Science Signaling

Volumn 4, Issue 204, 2011, Pages

  Goldsmith, Elizabeth J ^a  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE 7; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEIN C JUN; DUAL SPECIFICITY PHOSPHATASE; DUSP10 PROTEIN, HUMAN; MITOGEN ACTIVATED PROTEIN KINASE 14; MITOGEN ACTIVATED PROTEIN KINASE PHOSPHATASE;

BINDING SITE; MOLECULAR DOCKING; MUTATIONAL ANALYSIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN STRUCTURE; REVIEW; THREE DIMENSIONAL IMAGING; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; METABOLISM; PHYSIOLOGY; PROTEIN MOTIF; PROTEIN TERTIARY STRUCTURE; SIGNAL TRANSDUCTION;

AMINO ACID MOTIFS; ANIMALS; DUAL-SPECIFICITY PHOSPHATASES; HUMANS; MAP KINASE SIGNALING SYSTEM; MITOGEN-ACTIVATED PROTEIN KINASE 14; MITOGEN-ACTIVATED PROTEIN KINASE PHOSPHATASES; MODELS, MOLECULAR; PROTEIN STRUCTURE, TERTIARY;

EID: 84255190068     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2002697     Document Type: Review

References (23)

1. L. Bardwell, Mechanisms of MAPK signalling specificity. Biochem. Soc. Trans. 34, 837-841 (2006).
2. G. Pearson, F. Robinson, T. Beers Gibson, B. E. Xu, M. Karandikar, K. Berman, M. H. Cobb, Mitogen- activated protein (MAP) kinase pathways: Regulation and physiological functions. Endocr. Rev. 22, 153-183 (2001).
3. A. D. Sharrocks, S. H. Yang, A. Galanis, Docking domains and substrate-specificity determination for MAP kinases. Trends Biochem. Sci. 25, 448-453 (2000).
4. T. Tanoue, R. Maeda, M. Adachi, E. Nishida, Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions. EMBO J. 20, 466-479 (2001).
5. A. J. Bardwell, E. Frankson, L. Bardwell, Selectivity of docking sites in MAPK kinases. J. Biol. Chem. 284, 13165-13173 (2009).
6. B. Zhou, L. Wu, K. Shen, J. Zhang, D. S. Lawrence, Z. Y. Zhang, Multiple regions of MAP kinase phosphatase 3 are involved in its recognition and activation by ERK2. J. Biol. Chem. 276, 6506-6515 (2001).
7. B. Zhou, J. Zhang, S. Liu, S. Reddy, F. Wang, Z. Y. Zhang, Mapping ERK2-MKP3 binding interfaces by hydrogen/deuterium exchange mass spectrometry. J. Biol. Chem. 281, 38834-38844 (2006).
8. T. Tanoue, M. Adachi, T. Moriguchi, E. Nishida, A conserved docking motif in MAP kinases common to substrates, activators and regulators. Nat. Cell Biol. 2, 110-116 (2000).
9. C. I. Chang, B. E. Xu, R. Akella, M. H. Cobb, E. J. Goldsmith, Crystal structures of MAP kinase p38 complexed to the docking sites on its nuclear substrate MEF2A and activator MKK3b. Mol. Cell 9, 1241-1249 (2002).
10. Y. S. Heo, S. K. Kim, C. I. Seo, Y. K. Kim, B. J. Sung, H. S. Lee, J. I. Lee, S. Y. Park, J. H. Kim, K. Y. Hwang, Y. L. Hyun, Y. H. Jeon, S. Ro, J. M. Cho, T. G. Lee, C. H. Yang, Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125. EMBO J. 23, 2185-2195 (2004).
11. S. Liu, J. P. Sun, B. Zhou, Z. Y. Zhang, Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3. Proc. Natl. Acad. Sci. U.S.A. 103, 5326-5331 (2006).
12. T. Zhou, L. Sun, J. Humphreys, E. J. Goldsmith, Docking interactions induce exposure of activation loop in the MAP kinase ERK2. Structure 14, 1011-1019 (2006).
13. A. White, C. A. Pargellis, J. M. Studts, B. G. Werneburg, B. T. Farmer 2nd, Molecular basis of MAPK-activated protein kinase 2:p38 assembly. Proc. Natl. Acad. Sci. U.S.A. 104, 6353-6358 (2007).
14. Y.-Y. Zhang, J.-W. Wu, Z.-X. Wang, A distinct interaction mode revealed by the crystal structure of the kinase p38α with the MAPK binding domain of the phosphatase MKP5. Sci. Signal. 4, ra88 (2011).
15. R. Akella, X. Min, Q. Wu, K. H. Gardner, E. J. Goldsmith, The third conformation of p38α MAP kinase observed in phosphorylated p38α and in solution. Structure 18, 1571-1578 (2010).
16. X. Tao, L. Tong, Crystal structure of the MAP kinase binding domain and the catalytic domain of human MKP5. Protein Sci. 16, 880-886 (2007).
17. M. Muda, A. Theodosiou, N. Rodrigues, U. Boschert, M. Camps, C. Gillieron, K. Davies, A. Ashworth, S. Arkinstall, The dual specificity phosphatases M3/6 and MKP-3 are highly selective for inactivation of distinct mitogen-activated protein kinases. J. Biol. Chem. 271, 27205-27208 (1996).
18. A. Ranganathan, M. N. Yazicioglu, M. H. Cobb, The nuclear localization of ERK2 occurs by mechanisms both independent of and dependent on energy. J. Biol. Chem. 281, 15645-15652 (2006).
19. E. D. Gallagher, S. C. Xu, C. Moomaw, C. A. Slaughter, M. H. Cobb, Binding of JNK/SAPK to MEKK1 is regulated by phosphorylation. J. Biol. Chem. 277, 45785-45792 (2002).
20. J. Rodríguez, P. Crespo, Working without kinase activity: Phosphotransfer-independent functions of extracellular signal-regulated kinases. Sci. Signal. 4, re3 (2011).
21. W. A. Lim, T. Pawson, Phosphotyrosine signaling: Evolving a new cellular communication system. Cell 142, 661-667 (2010).
22. W. L. DeLano, The PyMOL Molecular Graphics System. Delano Scientific, San Carlos, CA, USA (2002).
23. T. Kallunki, T. Deng, M. Hibi, M. Karin, c-Jun can recruit JNK to phosphorylate dimerization partners via specific docking interactions. Cell 87, 929-939 (1996).