Dissection of binding between a phosphorylated tyrosine hydroxylase peptide and 14-3-3ζ: A complex story elucidated by NMR

Biophysical Journal

Volumn 107, Issue 9, 2014, Pages 2185-2194

  Hritz, Jozef ^a,b   Byeon, In Ja L ^a   Krzysiak, Troy ^a   Martinez, Aurora ^c   Sklenar, Vladimir ^b   Gronenborn, Angela M ^a  

^a UNIVERSITY OF PITTSBURGH SCHOOL OF MEDICINE   (United States)

^b MASARYK UNIVERSITY   (Czech Republic)

^c UNIVERSITY OF BERGEN   (Norway)

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; ISOENZYME; PEPTIDE; PHOSPHORUS; PROTEIN 14 3 3; PROTEIN BINDING; TYROSINE 3 MONOOXYGENASE; YWHAZ PROTEIN, HUMAN;

ALGORITHM; CHEMICAL STRUCTURE; CHEMISTRY; COMPUTER SIMULATION; DIMERIZATION; ESCHERICHIA COLI; GENETICS; HUMAN; NUCLEAR MAGNETIC RESONANCE; PHOSPHORYLATION; THERMODYNAMICS;

14-3-3 PROTEINS; ALGORITHMS; COMPUTER SIMULATION; DIMERIZATION; EPITOPES; ESCHERICHIA COLI; HUMANS; ISOENZYMES; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PHOSPHORUS ISOTOPES; PHOSPHORYLATION; PROTEIN BINDING; THERMODYNAMICS; TYROSINE 3-MONOOXYGENASE;

EID: 84908538422     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2014.08.039     Document Type: Article

References (28)

1. D.K. Morrison The 14-3-3 proteins: integrators of diverse signaling cues that impact cell fate and cancer development Trends Cell Biol. 19 2009 16 23
2. A.K. Gardino, and M.B. Yaffe 14-3-3 proteins as signaling integration points for cell cycle control and apoptosis Semin. Cell Dev. Biol. 22 2011 688 695
3. A.K. Freeman, and D.K. Morrison 14-3-3 proteins: diverse functions in cell proliferation and cancer progression Semin. Cell Dev. Biol. 22 2011 681 687
4. C. Johnson, and S. Crowther C. MacKintosh Bioinformatic and experimental survey of 14-3-3-binding sites Biochem. J. 427 2010 69 78
5. J. Jin, and F.D. Smith T. Pawson Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization Curr. Biol. 14 2004 1436 1450
6. T. Obsil, and V. Obsilova Structural basis of 14-3-3 protein functions Semin. Cell Dev. Biol. 22 2011 663 672
7. X. Yang, and W.H. Lee J.M. Elkins Structural basis for protein-protein interactions in the 14-3-3 protein family Proc. Natl. Acad. Sci. USA 103 2006 17237 17242
8. A.K. Gardino Structural determinants of 14-3-3 binding specificities and regulation of subcellular localization of 14-3-3-ligand complexes: a comparison of the x-ray crystal structures of all human 14-3-3 isoforms Semin. Cancer Biol. 16 2006 173 182
9. M.B. Yaffe, and K. Rittinger L.C. Cantley The structural basis for 14-3-3: phosphopeptide binding specificity Cell 91 1997 961 971
10. S. Ganguly, and J.L. Weller D.C. Klein Melatonin synthesis: 14-3-3-dependent activation and inhibition of arylalkylamine n-acetyltransferase mediated by phosphoserine-205 Proc. Natl. Acad. Sci. USA 102 2005 1222 1227
11. A. Aitken 14-3-3 proteins: a historical overview Semin. Cancer Biol. 16 2006 162 172
12. 2+ calmodulin-dependent protein kinase II FEBS Lett. 219 1987 79 82
13. T. Nagatsu, M. Levitt, and S. Udenfriend Tyrosine hydroxylase: the initial step in norepinephrine biosynthesis J. Biol. Chem. 239 1964 2910 2917
14. B. Grima, and A. Lamouroux J. Mallet A single human gene encoding multiple tyrosine hydroxylases with different predicted functional characteristics Nature 326 1987 707 711
15. N. Kaneda, and K. Kobayashi T. Nagatsu Isolation of a novel cDNA clone for human tyrosine hydroxylase: alternative RNA splicing produces four kinds of mRNA from a single gene Biochem. Biophys. Res. Commun. 146 1987 971 975
16. P.F. Fitzpatrick Tetrahydropterin-dependent amino acid hydroxylases Annu. Rev. Biochem. 68 1999 355 381
17. S.C. Daubner, T. Le, and S. Wang Tyrosine hydroxylase and regulation of dopamine synthesis Arch. Biochem. Biophys. 508 2011 1 12
18. R. Kleppe, K. Toska, and J. Haavik Interaction of phosphorylated tyrosine hydroxylase with 14-3-3 proteins: evidence for a phosphoserine 40-dependent association J. Neurochem. 77 2001 1097 1107
19. V. Obsilova, and E. Nedbalkova T. Obsil The 14-3-3 protein affects the conformation of the regulatory domain of human tyrosine hydroxylase Biochemistry 47 2008 1768 1777
20. C. Itagaki, and T. Isobe T. Ichimura Stimulus-coupled interaction of tyrosine hydroxylase with 14-3-3 proteins Biochemistry 38 1999 15673 15680
21. A.A. Skjevik, and M. Mileni A. Martinez The N-terminal sequence of tyrosine hydroxylase is a conformationally versatile motif that binds 14-3-3 proteins and membranes J. Mol. Biol. 426 2013 150 168
22. R. Kleppe, and S. Rosati A. Martinez Phosphorylation dependence and stoichiometry of the complex formed by tyrosine hydroxylase and 14-3-3γ Mol. Cell. Proteomics 13 2014 2017 2030
23. M.B. Yaffe How do 14-3-3 proteins work? Gatekeeper phosphorylation and the molecular anvil hypothesis FEBS Lett. 513 2002 53 57
24. R. Kleppe, and S. Ghorbani J. Haavik Modeling cellular signal communication mediated by phosphorylation dependent interaction with 14-3-3 proteins FEBS Lett. 588 2014 92 98
25. L.Y. Lian, and G.C.K. Roberts Effects of chemical exchange on NMR spectra R.C.K. Robert, NMR of Macromolecules. A Practical Approach 1993 IRL Press Oxford, United Kingdom 153 182
26. A.D. Bain Chemical exchange in NMR Prog. Nucl. Magn. Reson. Spectrosc. 43 2003 63 103
27. B. Kostelecky, and A.T. Saurin N.Q. McDonald Recognition of an intra-chain tandem 14-3-3 binding site within PKCε EMBO Rep. 10 2009 983 989
28. M. Molzan, and C. Ottmann Synergistic binding of the phosphorylated S233-and S259-binding sites of C-RAF to one 14-3-3 ζ-dimer J. Mol. Biol. 423 2012 486 495