Solution structures of the C-terminal headpiece subdomains of human villin and advillin, evaluation of headpiece F-actin-binding requirements

Protein Science

Volumn 13, Issue 5, 2004, Pages 1276-1287

  Vermeulen, Wim ^a   Vanhaesebrouck, Peter ^a   Van Troys, Marleen ^b,c   Verschueren, Mieke ^a   Fant, Franky ^a   Goethals, Marc ^b,c   Ampe, Christophe ^b,c   Martins, José C ^a   Borremans, Frans A M ^a  

^a GHENT UNIVERSITY   (Belgium)

^b GHENT UNIVERSITY   (Belgium)

^c DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

Author keywords

Actin binding protein; Advillin; Headpiece subdomain; NMR solution structure; Villin

Indexed keywords

ADVILLIN; F ACTIN; INDOLE; LYSINE; PROLINE; PROTEIN; UNCLASSIFIED DRUG; VILLIN;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CHICKEN; HUMAN; MOLECULAR MODEL; MUTATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE;

ACTINS; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; HUMANS; MICROFILAMENT PROTEINS; MOLECULAR SEQUENCE DATA; NEUROFILAMENT PROTEINS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; STRUCTURAL HOMOLOGY, PROTEIN; STRUCTURE-ACTIVITY RELATIONSHIP; TRYPTOPHAN;

GALLUS GALLUS;

EID: 1942505724     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03518104     Document Type: Article

References (51)

1. Arpin, M., Pringault, E., Finidori, J., Garcia, A., Jeltsch, J.-M., Vandekerckhove, J., and Louvard, D. 1988. Sequence of human villin-a large duplicated domain homologous with other actin-severing proteins and a unique small carboxy-terminal domain related to villin specificity. J. Cell. Biol. 107: 1759-1766.
2. Bazari, W.L., Matsudaira, P.T., Wallek, M., Smeal, T., and Jakes, R. 1988. Villin sequence and peptide map identify 6 homologous domains. Proc. Natl. Acad. Sci. 85: 4986-4990.
3. Bretscher, A. and Weber, K. 1980. Villin is a major protein of the microvillus cytoskeleton which binds both G- and F-actin in a calcium-dependent manner. Cell 20: 839-847.
4. Case, D.A. 1995. Calibration of ring-current effects in proteins and nucleic acids. J. Biomol. NMR 6: 341-346.
5. Craig, S.W. and Powell, L.D. 1980. Regulation of actin polymerization by villin, a 95,000 Dalton cytoskeletal component of intestinal brush-borders. Cell 22: 739-746.
6. Doering, D.S. and Matsudaira, P.T. 1996. Cysteine scanning mutagenesis at 40 of 76 positions in villin headpiece maps the F-actin binding site and structural features of the domain. Biochemistry 35: 12677-12685.
7. Eberstadt, M., Gremmecker, G., Mierke, D., and Kessler, H. 1995. Scalar coupling-constants-their analysis and their application for the elucidation of structures. Angew. Chem. Int. Ed. Engl. 34: 1671-1695.
8. Friederich, E., Vancompernolle, K., Huet, C., Goethals, M., Finidori, J., Vandekerckhove, J., and Louvard, D. 1992. An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin. Cell 70: 81-92.
9. Glenney Jr., J.R., and Weber, K. 1981. Calcium control of microfilaments-uncoupling the F-actin severing and F-actin bundling activity of villin by limited proteolysis in vitro. Proc. Natl. Acad. Sci. 78: 2810-2814.
10. 2+ dependent nucleation and capping of the barbed end. Cell 24: 471-480.
11. Griesinger, C., Sorensen, O., and Ernst, R. 1985. Two-dimensional correlation of connected NMR transitions. J. Am. Chem. Soc. 110: 7870-7872.
12. 1H spin system identification in macromolecules. J. Am. Chem. Soc. 110: 7870-7872.
13. Güntert, P., Mumenthaler, C., and Wüthrich, K. 1997. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273: 283-298.
14. Kabsch, W. and Sander, C. 1983. Dictionary of protein secondary structure-pattern recognition of hydrogen bonded and geometrical features. Biopolymers A47: 392-400.
15. Kessler, H. and Oschkinat, H. 1985. Simplification of spectra for the determination of coupling-constants from homonuclear correlated 2D NMR spectra. Angew. Chem. Int. Ed. Engl. 24: 690-692.
16. Kim, Y. and Prestegard, J.H. 1989. Measurement of vicinal couplings from cross peaks in COSY spectra. J. Magn. Reson. 84: 9-13.
17. Kjæer, M., Andersen, K.V., and Poulsen, F.M. 1994. Automated and semiautomated analysis of homo- and heteronuclear multidimensional nuclear magnetic resonance spectra of proteins: The program PRONTO. Methods Enzymol. 239: 288-308.
18. Koradi, R., Billeter, M., and Wüthrich, K. 1996. MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graph. 14: 51-55.
19. 2O solutions of biological macromolecules by two-dimensional NMR experiments. Biochem. Biophys. Res. Comm. 96: 1156-1163.
20. Laskowski, R.A., Rullmann, J.A.C., MacArthur, M.W., Kaptein, R., and Thornton, J. 1996. AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8: 477-486.
21. 1H spin coupling constants in proteins. Biochem. Biophys. Res. Comm. 113: 967-974.
22. Marion, D., Ikura, M., and Bax, A. 1989. Improved solvent suppression in one-dimensional and two-dimensional NMR-spectra by convolution of time-domain data. J. Magn. Res. 84: 425-430.
23. Marion, D., Ikura, M., Tschudin, R., and Bax, A. 1991. Rapid recording of 2D-NMR spectra without phase cycling-application to the study of hydrogen exchange in proteins. J. Magn. Reson. 85: 393-399.
24. Markley, J.L., Bax, A., Arata, Y., Hilbers, C.W., Kaptein, R., Sykes, B.D., Wright, P.E., and Wüthrich, K. 1998. Recommendations for the presentation of NMR structures of proteins and nucleic acids. Pure Appl. Chem. 70: 117-142.
25. McKnight, C.J., Doering, D.S., Matsudaira, P.T., and Kim, P.S. 1996. A thermostable 35-residue subdomain within villin headpiece. J. Mol. Biol. 260: 126-134.
26. McKnight, C.J., Matsudaira, P.T., and Kim, P.S. 1997. NMR structure of the 35-residue villin headpiece subdomain. Nat. Struct. Biol. 4: 180-184.
27. Mooseker, M.S., Graves, T.A., Wharton, K.A., Falco, N., and Howe, C.L. 1980. Regulation of microvillus structure-calcium-dependent solation and cross-linking of actin filaments in the microvilli of intestinal epithelial cells. J. Cell. Biol. 87: 809-822.
28. HαHβ in the basic pancreatic trypsin-inhibitor measured by two-dimensional J-resolved NMR spectroscopy. Eur. J. Biochem. 115: 653-657.
29. 1H NMR techniques for the identification of the amino-acid-proton spin systems in proteins-rabbit methallothionein-2. Eur. J. Biochem. 151: 257-273.
30. Osapay, K. and Case, D.A. 1991. A new analysis of proton chemical-shifts in proteins. J. Am. Chem. Soc. 113: 9436-9444.
31. Piotto, M., Saudek, V., and Sklenar, V. 1992. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2: 661-665.
32. 1H NMR spectra of proteins via double quantum filtering Biochem. Biophys. Res. Comm. 117: 479-785.
33. Ravenall, S.J., Gavazzi, I., Wood, J.N., and Akopian, A.N. 2002. A peripheral nervous system actin-binding protein regulates neurite outgrowth. Eur. J. Neurosci. 15: 281-290.
34. Roof, D.J., Hayes, A., Adamian, M., Chishti, A., and Li, T. 1997. Molecular characterization of abLIM, a novel actin-binding and double zinc finger protein. J. Cell. Biol. 138: 575-588.
35. Rossenu, S., Leyman, S., Dewitte, D., Peelaers, D., Jonckheere, V., Van Troys, M., Vandekerckhove, J., and Ampe, C. 2003. A phage display based method for determination of relative affinities of mutants; application to the actin binding motifs in thymosin β4 and villin headpiece. J. Biol. Chem. 278: 16642-16650.
36. 1H NMR studies of molten globule proteins in aqueous media. J. Biomol. NMR 4: 859-862.
37. Spudich, J.A. and Watt, S. 1971. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and with the proteolytic fragments of myosin. J. Biol. Chem. 246: 4866-4871.
38. Vancompernolle, K., Goethals, M., Huet, C., Louvard, D., and Vandekerckhove, J. 1992. G- to F-actin modulation by a single amino acid substitution in the actin binding site of actobindin & thymosin β4. EMBO J. 11: 4739-4746.
39. Van Troys, M., Dewitte, D., Goethals, M., Carlier, M.F., Vandekerckhove, J., and Ampe, C. 1996. The actin binding site of thymosin β4 mapped by mutational analysis. EMBO J. 15: 201-210.
40. Vardar, D., Buckley, D.A., Frank, B.S., and McKnight, C.J. 1999. NMR structure of an F-actin-binding "headpiece" motif from villin. J. Mol. Biol. 294: 1299-1310.
41. Vardar, D., Chishti, A.H., Frank, B.S., Luna, E.J., Noegel, A.A., Oh, S.W., Schleicher, M., and McKnight, C.J. 2002. Villin-type headpiece domains show a wide range of F-actin-binding affinities. Cell Motil. Cytoskel. 52: 9-21.
42. Vriend, G. 1990. What If-a molecular modelling and drug design program. J. Mol. Graph. 8: 52-56.
43. Weiner, S.J., Kollman, P.A., Case, D.A., Singh, C., Ghio, C., Alagona, G., Profeta, S., and Weiner, P. 1984. A new force field for molecular mechanical simulation of nucleic acids and proteins. J. Am. Chem. Soc. 106: 765-784.
44. Widmer, H., Billeter, M., and Wüthrich, K. 1989. Three-dimensional structure of the neurotoxin ATX Ia from Anemonia sulcata in aqueous solution determined by nuclear magnetic resonance spectroscopy. Proteins 6: 357-371.
45. Wilmot, C.M. and Thornton, J.M. 1990. β-Sheets and their distortions-a proposed new nomenclature. Protein Eng. 3: 479-493.
46. Wishart, D.S. and Nip, A.M. 1998. Protein chemical shift analysis: A practical guide. Biochem. Cell. Biol. 76: 153-163.
47. Wishart, D.S., Sykes, B.D., and Richards, F.M. 1992. The chemical shift index-a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31: 1647-1651.
48. 15N chemical shift referencing in biomolecular NMR. J. Biomol. NMR 6: 135-140.
49. Wüthrich, K. 1986. NMR of proteins and nucleic acids. Wiley-Interscience, New York.
50. Wüthrich, K., Billeter, M., and Braun, W. 1983. Pseudo-structures for the 20 common amino-acids for use in studies of protein conformations by measurements of intramolecular proton proton distance constraints with nuclear magnetic resonance. J. Mol. Biol. 169: 949-961.
51. Zhai, L., Zhao, P., Panebra, A., Guerrerio, A.L., and Khurana, S. 2001. Tyrosine phosphorylation of villin regulates the organisation of the actin cytoskeleton. J. Biol. Chem. 276: 36163-36167.