Crystal Structure of the MH2 domain of Drosophila Mad

Science in China, Series C: Life Sciences

Volumn 52, Issue 6, 2009, Pages 539-544

  Wang, Chong ^a   Chen, Lei ^a   Wang, Le ^a   Wu, Jia Wei ^a  

^a TSINGHUA UNIVERSITY   (China)

Author keywords

Crystal structure; Homotrimerization; MH2 domain; Smad protein family; TGF signaling

Indexed keywords

MAMMALIA;

DNA BINDING PROTEIN; DROSOPHILA PROTEIN; MAD PROTEIN, DROSOPHILA; PROTEIN SUBUNIT; SERINE; TRANSCRIPTION FACTOR;

ANIMAL; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; DROSOPHILA MELANOGASTER; GENETICS; METABOLISM; MOLECULAR GENETICS; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

ANIMALS; CRYSTALLOGRAPHY, X-RAY; DNA-BINDING PROTEINS; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; SERINE; TRANSCRIPTION FACTORS;

EID: 70149107862     PISSN: 10069305     EISSN: 18622798     Source Type: Journal    
DOI: 10.1007/s11427-009-0080-x     Document Type: Article

References (30)

1. Massagué J. TGF-beta signal transduction. Annu Rev Biochem, 1998, 67: 753-791.
2. Attisano L, Wrana J L. Signal transduction by the TGF-beta superfamily. Science, 2002, 296: 1646-1647.
3. Shi Y, Massagué J. Mechanisms of TGF-beta signaling from cell membrane to the nucleus. Cell, 2003, 113: 685-700.
4. Raftery L A, Sutherland D J. TGF-beta family signal transduction in Drosophila development: from Mad to Smads. Dev Biol, 1999, 210: 251-268.
5. Raftery L A, Twombly V, Wharton K, et al. Genetic screens to identify elements of the decapentaplegic signaling pathway in Drosophila. Genetics, 1995, 139: 241-254.
6. Sekelsky J J, Newfeld S J, Raftery L A, et al. Genetic characterization and cloning of mothers against dpp, a gene required for decapentaplegic function in Drosophila melanogaster. Genetics, 1995, 139: 1347-1358.
7. Derynck R, Zhang Y, Feng X H. Smads: transcriptional activators of TGF-beta responses. Cell, 1998, 95: 737-740.
8. Attisano L, Wrana J L. Smads as transcriptional co-modulators. Curr Opin Cell Biol, 2000, 12: 235-243.
9. Massagué J, Seoane J, Wotton D. Smad transcription factors. Genes Dev, 2005, 19: 2783-810.
10. Shi Y. Structural insights on Smad function in TGFbeta signaling. Bioessays, 2001, 23: 223-232.
11. Abdollah S, Macías-Silva M, Tsukazaki T, et al. TbetaRI phosphorylation of Smad2 on Ser465 and Ser467 is required for Smad2-Smad4 complex formation and signaling. J Biol Chem, 1997, 272: 27678-27685.
12. Souchelnytskyi S, Tamaki K, Engström U, et al. Phosphorylation of Ser465 and Ser467 in the C terminus of Smad2 mediates interaction with Smad4 and is required for transforming growth factor-beta signaling. J Biol Chem, 1997, 272: 28107-28115.
13. Wu G, Chen Y G, Ozdamar B, et al. Structural basis of Smad2 recognition by the Smad anchor for receptor activation. Science, 2000, 287: 92-97.
14. Qin B Y, Lam S S, Correia J J, et al. Smad3 allostery links TGF-beta receptor kinase activation to transcriptional control. Genes Dev, 2002, 16: 1950-1963.
15. Chacko B M, Qin B, Correia J J, et al. The L3 loop and C-terminal phosphorylation jointly define Smad protein trimerization. Nat Struct Biol, 2001, 8: 248-253.
16. Wu J W, Hu M, Chai J, et al. Crystal structure of a phosphorylated Smad2: Recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-beta signaling. Mol Cell, 2001, 8: 1277-1289.
17. Qin B Y, Chacko B M, Lam S S, et al. Structural basis of Smad1 activation by receptor kinase phosphorylation. Mol Cell, 2001, 8: 1303-1312.
18. Chacko B M, Qin B Y, Tiwari A, et al. Structural basis of heteromeric smad protein assembly in TGF-beta signaling. Mol Cell, 2004, 15: 813-823.
19. Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol, 1997, 276: 307-326.
20. McCoy A J, Grosse-Kunstleve R W, Adams P D, et al. Phaser crystallographic software. J Appl Cryst, 2007, 40: 658-674.
21. Hao R, Chen L, Wu J W, et al. Structure of Drosophila Mad MH2 domain. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2008, 64: 986-990.
22. Adams P D, Grosse-Kunstleve R W, Hung L W, et al. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr D Biol Crystallogr, 2002, 58: 1948-1954.
23. Emsley P, Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr, 2004, 60: 2126-2132.
24. Morris A L, MacArthur M W, Hutchinson E G, et al. Stereochemical quality of protein structure coordinates. Proteins, 1992, 12: 345-364.
25. Izzi L, Attisano L. Regulation of the TGFbeta signalling pathway by ubiquitin-mediated degradation. Oncogene, 2004, 23: 2071-2078.
26. Shi Y, Hata A, Lo R S, et al. A structural basis for mutational inactivation of the tumour suppressor Smad4. Nature, 1997, 388: 87-93.
27. Qin B, Lam S S, Lin K. Crystal structure of a transcriptionally active Smad4 fragment. Structure, 1999, 7: 1493-1503.
28. Wu J W, Krawitz A R, Chai J, et al. Structural mechanism of Smad4 recognition by the nuclear oncoprotein Ski: insights on Ski-mediated repression of TGF-beta signaling. Cell, 2002, 111: 357-367.
29. Wu J W, Fairman R, Penry J, et al. Formation of a stable heterodimer between Smad2 and Smad4. J Biol Chem, 2001, 276: 20688-20694.
30. Kretzschmar M, Liu F, Hata A, et al. The TGF-beta family mediator Smad1 is phosphorylated directly and activated functionally by the BMP receptor kinase. Genes Dev, 1997, 11: 984-995.