Solution structure of the first SH3 domain of human vinexin and its interaction with vinculin peptides

Biochemical and Biophysical Research Communications

Volumn 357, Issue 4, 2007, Pages 931-937

  Zhang, Jiahai ^a   Li, Xiang ^a   Yao, Bo ^a   Shen, Weiqun ^a   Sun, Hongbin ^a   Xu, Chao ^a   Wu, Jihui ^a   Shi, Yunyu ^a  

^a UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

Author keywords

Chemical shift perturbation; Nuclear magnetic resonance; SH3 domain; Solution structure; Vinculin; Vinexin

Indexed keywords

GENE PRODUCT; PEPTIDE; PROLINE; PROTEIN SH3; UNCLASSIFIED DRUG; VINCULIN; VINEXIN;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; HUMAN; HUMAN TISSUE; LIGAND BINDING; NUCLEAR MAGNETIC RESONANCE; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SURFACE PLASMON RESONANCE;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; AMINO ACID SEQUENCE; BINDING SITES; COMPUTER SIMULATION; HUMANS; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN CONFORMATION; SRC HOMOLOGY DOMAINS; VINCULIN;

EID: 34247880175     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.04.029     Document Type: Article

References (34)

1. Kioka N., Ueda K., and Amachi T. Vinexin, CAP/ponsin, ArgBP2: a novel adaptor protein family regulating cytoskeletal organization and signal transduction. Cell Struct. Funct. 27 (2002) 1-7
2. Kioka N., Sakata S., Kawauchi T., Amachi T., Akiyama S.K., Okazaki K., Yaen C., Yamada K.M., and Aota S. Vinexin: a novel vinculin-binding protein with multiple SH3 domains enhances actin cytoskeletal organization. J. Cell Biol. 144 (1999) 59-69
3. Mandai K., Nakanishi H., Satoh A., Takahashi K., Satoh K., Nishioka H., Mizoguchi A., and Takai Y. Ponsin/SH3P12: an l-afadin- and vinculin-binding protein localized at cell-cell and cell-matrix adherens junctions. J. Cell Biol. 144 (1999) 1001-1017
4. Borgon R.A., Vonrhein C., Bricogne G., Bois P.R., and Izard T. Crystal structure of human vinculin. Structure 12 (2004) 1189-1197
5. Gumbiner B.M. Cell adhesion: the molecular basis of tissue architecture and morphogenesis. Cell 84 (1996) 345-357
6. Giancotti F.G., and Ruoslahti E. Integrin signaling. Science 285 (1999) 1028-1032
7. Siu M.K., and Cheng C.Y. Extracellular matrix: recent advances on its role in junction dynamics in the seminiferous epithelium during spermatogenesis. Biol. Reprod. 71 (2004) 375-391
8. Chandrasekar I., Stradal T.E., Holt M.R., Entschladen F., Jockusch B.M., and Ziegler W.H. Vinculin acts as a sensor in lipid regulation of adhesion-site turnover. J. Cell Sci. 118 (2005) 1461-1472
9. Winkler J., Lunsdorf H., and Jockusch B.M. The ultrastructure of chicken gizzard vinculin as visualized by high-resolution electron microscopy. J. Struct. Biol. 116 (1996) 270-277
10. Miller G.J., Dunn S.D., and Ball E.H. Interaction of the N- and C-terminal domains of vinculin. Characterization and mapping studies. J. Biol. Chem. 276 (2001) 11729-11734
11. Zamir E., and Geiger B. Molecular complexity and dynamics of cell-matrix adhesions. J. Cell Sci. 114 (2001) 3583-3590
12. Weekes J., Barry S.T., and Critchley D.R. Acidic phospholipids inhibit the intramolecular association between the N- and C-terminal regions of vinculin, exposing actin-binding and protein kinase C phosphorylation sites. Biochem. J. 314 Pt 3 (1996) 827-832
13. Akamatsu M., Aota S., Suwa A., Ueda K., Amachi T., Yamada K.M., Akiyama S.K., and Kioka N. Vinexin forms a signaling complex with Sos and modulates epidermal growth factor-induced c-Jun N-terminal kinase/stress-activated protein kinase activities. J. Biol. Chem. 274 (1999) 35933-35937
14. Suwa A., Mitsushima M., Ito T., Akamatsu M., Ueda K., Amachi T., and Kioka N. Vinexin beta regulates the anchorage dependence of ERK2 activation stimulated by epidermal growth factor. J. Biol. Chem. 277 (2002) 13053-13058
15. Mitsushima M., Suwa A., Amachi T., Ueda K., and Kioka N. Extracellular signal-regulated kinase activated by epidermal growth factor and cell adhesion interacts with and phosphorylates vinexin. J. Biol. Chem. 279 (2004) 34570-34577
16. Kawauchi T., Ikeya M., Takada S., Ueda K., Shirai M., Takihara Y., Kioka N., and Amachi T. Expression of vinexin alpha in the dorsal half of the eye and in the cardiac outflow tract and atrioventricular canal. Mech. Dev. 106 (2001) 147-150
17. Mitsushima M., Sezaki T., Akahane R., Ueda K., Suetsugu S., Takenawa T., and Kioka N. Protein kinase A-dependent increase in WAVE2 expression induced by the focal adhesion protein vinexin. Genes Cells 11 (2006) 281-292
18. Mitsushima M., Ueda K., and Kioka N. Vinexin beta regulates the phosphorylation of epidermal growth factor receptor on the cell surface. Genes Cells 11 (2006) 971-982
19. Matsuyama M., Mizusaki H., Shimono A., Mukai T., Okumura K., Abe K., Shimada K., and Morohashi K. A novel isoform of vinexin, vinexin gamma regulates Sox9 gene expression through activation of MAPK cascade in mouse fetal gonad. Genes Cells 10 (2005) 421-434
20. Takahashi H., Mitsushima M., Okada N., Ito T., Aizawa S., Akahane R., Umemoto T., Ueda K., and Kioka N. Role of interaction with vinculin in recruitment of vinexins to focal adhesions. Biochem. Biophys. Res. Commun. 336 (2005) 239-246
21. Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., and Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6 (1995) 277-293
22. Cornilescu G., Delaglio F., and Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13 (1999) 289-302
23. Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.S., Kuszewski J., Nilges M., Pannu N.S., Read R.J., Rice L.M., Simonson T., and Warren G.L. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54 (1998) 905-921
24. Laskowski R.A., Rullmannn J.A., MacArthur M.W., Kaptein R., and Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8 (1996) 477-486
25. Hu H.Y., Horton J.K., Gryk M.R., Prasad R., Naron J.M., Sun D.A., Hecht S.M., Wilson S.H., and Mullen G.P. Identification of small molecule synthetic inhibitors of DNA polymerase beta by NMR chemical shift mapping. J. Biol. Chem. 279 (2004) 39736-39744
26. Li X., Zhang J., Cao Z., Wu J., and Shi Y. Solution structure of GOPC PDZ domain and its interaction with the C-terminal motif of neuroligin. Protein Sci. 15 (2006) 2149-2158
27. Koyama S., Yu H., Dalgarno D.C., Shin T.B., Zydowsky L.D., and Schreiber S.L. Structure of the PI3K SH3 domain and analysis of the SH3 family. Cell 72 (1993) 945-952
28. Morton C.J., Pugh D.J., Brown E.L., Kahmann J.D., Renzoni D.A., and Campbell I.D. Solution structure and peptide binding of the SH3 domain from human Fyn. Structure 4 (1996) 705-714
29. Holm L., and Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233 (1993) 123-138
30. Feng S., Chen J.K., Yu H., Simon J.A., and Schreiber S.L. Two binding orientations for peptides to the Src SH3 doma: development of a general model for SH3-ligand interactions. Science 266 (1994) 1241-1247
31. Mayer B.J. SH3 domains: complexity in moderation. J. Cell Sci. 114 (2001) 1253-1263
32. Kami K., Takeya R., Sumimoto H., and Kohda D. Diverse recognition of non-PxxP peptide ligands by the SH3 domains from p67(phox), Grb2 and Pex13p. EMBO J. 21 (2002) 4268-4276
33. Mongiovi A.M., Romano P.R., Panni S., Mendoza M., Wong W.T., Musacchio A., Cesareni G., and Di Fiore P.P. A novel peptide-SH3 interaction. EMBO J. 18 (1999) 5300-5309
34. Kang H., Freund C., Duke-Cohan J.S., Musacchio A., Wagner G., and Rudd C.E. SH3 domain recognition of a proline-independent tyrosine-based RKxxYxxY motif in immune cell adaptor SKAP55. EMBO J. 19 (2000) 2889-2899