The SH3 domain of a M7 interacts with its C-terminal proline-rich region

Protein Science

Volumn 16, Issue 2, 2007, Pages 189-196

  Wang, Qinghua ^a   Deloia, Matthew A ^a   Kang, Yang ^a   Litchke, Casey ^a   Zhang, Naixia ^a   Titus, Margaret A ^a   Walters, Kylie J ^a  

^a UNIVERSITY OF MINNESOTA   (United States)

Author keywords

Myosin; NMR spectroscopy; PxxP motif; SH3 domain

Indexed keywords

MYOSIN; PROLINE; PROTEIN SH3;

ARTICLE; CARBOXY TERMINAL SEQUENCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BINDING SITES; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MYOSINS; PROLINE; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SRC HOMOLOGY DOMAINS;

DICTYOSTELIUM;

EID: 33846514062     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062496807     Document Type: Article

References (33)

1. Agrawal, V. and Kishan, K.V. 2002. Promiscuous binding nature of SH3 domains to their target proteins. Protein Pept. Lett. 9: 185-193.
2. Andreotti, A.H., Bunnell, S.C., Feng, S., Berg, L.J., and Schreiber, S.L. 1997. Regulatory intramolecular association in a tyrosine kinase of the Tec family. Nature 385: 93-97.
3. Bartels, C., Xia, T.-H., Billeter, M., Güntert, P., and Wüthrich, K. 1995. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR 6: 1-10.
4. Brünger, A.T. 1993. XPLOR version 3.1: A system for X-ray crystallography and NMR. Yale University Press, New Haven, CT.
5. Cornilescu, G., Delaglio, F., and Bax, A. 1999. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13: 289-302.
6. Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A. 1995. NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6: 277-293.
7. Evangelista, M., Klebl, B.M., Tong, A.H., Webb, B.A., Leeuw, T., Leberer, E., Whiteway, M., Thomas, D.Y., and Boone, C. 2000. A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex. J. Cell Biol. 148: 353-362.
8. Feng, S., Chen, J.K., Yu, H., Simon, J.A., and Schreiber, S.L. 1994. Two binding orientations for peptides to the Src SH3 domain: Development of a general model for SH3-ligand interactions. Science 266: 1241-1247.
9. Ishikawa, T., Cheng, N., Liu, X., Korn, E.D., and Steven, A.C. 2004. Subdomain organization of the Acanthamoeba myosin IC tail from cryoelectron microscopy. Proc. Natl. Acad. Sci. 101: 12189-12194.
10. Jung, G., Remmert, K., Wu, X., Volosky, J.M., and Hammer III, J.A. 2001. The Dictyostelium CARMIL protein links capping protein and the Arp2/3 complex to type I myosins through their SH3 domains. J. Cell Biol. 153: 1479-1497.
11. Kanelis, V., Donaldson, L., Muhandiram, D., Rotin, D., Forman-Kay, J., and Kay, L.E. 2000. Sequential assignment of proline-rich regions in proteins: Application to modular binding domain complexes. J. Biomol. NMR 16: 253-259.
12. Kang, Y., Vossler, R.A., Diaz-Martinez, L.A., Winter, N.S., Clarke, D.J., and Walters, K.J. 2006. UBL/UBA ubiquitin receptor proteins bind a common tetraubiquitin chain. J. Mol. Biol. 356: 1027-1035.
13. Kapeller, R., Prasad, K.V., Janssen, O., Hou, W., Schaffhausen, B.S., Rudd, C.E., and Cantley, L.C. 1994. Identification of two SH3-binding motifs in the regulatory subunit of phosphatidylinositol 3-kinase. J. Biol. Chem. 269: 1927-1933.
14. Kieke, M.C. and Titus, M.A. 2003. The myosin superfamily - An overview. In Molecular motors (ed. M. Schliwa), pp. 3-44. Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, Germany.
15. Koch, C.A., Anderson, D., Moran, M.F., Ellis, C., and Pawson, T. 1991. SH2 and SH3 domains: Elements that control interactions of cytoplasmic signaling proteins. Science 252: 668-674.
16. Krendel, M. and Mooseker, M.S. 2005. Myosins: Tails (and heads) of functional diversity. Physiology 20: 239-251.
17. Lechler, T., Shevchenko, A., and Li, R. 2000. Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization. J. Cell Biol. 148: 363-373.
18. Lee, W.L., Ostap, E.M., Zot, H.G., and Pollard, T.D. 1999. Organization and ligand binding properties of the tail of Acanthamoeba myosin-IA. Identification of an actin-binding site in the basic (tail homology-1) domain. J. Biol. Chem. 274: 35159-35171.
19. Lee, W.L., Bezanilla, M., and Pollard, T.D. 2000. Fission yeast myosin-I, Myo1p, stimulates actin assembly by Arp2/3 complex and shares functions with WASp. J. Cell Biol. 151: 789-800.
20. Lim, W.A., Richards, F.M., and Fox, R.O. 1994. Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains. Nature 372: 375-379.
21. Liu, F., Zhang, N., Zhou, X., Hanna, P.E., Wagner, C.R., Koepp, D.M., and Walters, K.J. 2006a. Protein aggregation and constitutive ubiquitylation of arylamine N-acetyltransferase. J. Mol. Biol. 361: 482-492.
22. Liu, J., Taylor, D.W., Krementsova, E.B., Trybus, K.M., and Taylor, K.A. 2006b. Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography. Nature 442: 208-211.
23. Maniak, M. 2001. Cell adhesion: Ushering in a new understanding of myosin VII. Curr. Biol. 11: R315-R317.
24. Musacchio, A., Noble, M., Pauptit, R., Wierenga, R., and Saraste, M. 1992. Crystal structure of a Src-homology 3 (SH3) domain. Nature 359: 851-855.
25. Noble, M.E., Musacchio, A., Saraste, M., Courtneidge, S.A., and Wierenga, R.K. 1993. Crystal structure of the SH3 domain in human Fyn; Comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin. EMBO J. 12: 2617-2624.
26. Thirumurugan, K., Sakamoto, T., Hammer III, J.A., Sellers, J.R., and Knight, P.J. 2006. The cargo-binding domain regulates structure and activity of myosin 5. Nature 442: 212-215.
27. Tuxworth, R.I., Weber, I., Wessels, D., Addicks, G.C., Soll, D.R., Gerisch, G., and Titus, M.A. 2001. A role for myosin VII in dynamic cell adhesion. Curr. Biol. 11: 318-329.
28. Walters, K.J., Ferentz, A.E., Hare, B.J., Hidalgo, P., Jasanoff, A., Matsuo, H., and Wagner, G. 2001. Characterizing protein-protein complexes and oligomers by nuclear magnetic resonance spectroscopy. Methods Enzymol. 339: 238-258.
29. Walters, K.J., Lech, P.J., Goh, A.M., Wang, Q., and Howley, P.M. 2003. DNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5a. Proc. Natl. Acad. Sci. 100: 12694-12699.
30. Wang, Q., Goh, A.M., Howley, P.M., and Walters, K.J. 2003. Ubiquitin recognition by the DNA repair protein hHR23a. Biochemistry 42: 13529-13535.
31. Weng, Z., Rickles, R.J., Feng, S., Richard, S., Shaw, A.S., Schreiber, S.L., and Brugge, J.S. 1995. Structure-function analysis of SH3 domains: SH3 binding specificity altered by single amino acid substitutions. Mol. Cell. Biol. 15: 5627-5634.
32. Wüthrich, K. 1986. NMR of proteins and nucleic acids. Wiley, New York.
33. Yu, H., Rosen, M.K., Shin, T.B., Seidel-Dugan, C., Brugge, J.S., and Schreiber, S.L. 1992. Solution structure of the SH3 domain of Src and identification of its ligand-binding site. Science 258: 1665-1668.