Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein

Nature

Volumn 404, Issue 6774, 2000, Pages 151-158

  Kim, Annette S ^a   Kakalis, Lazaros T ^a   Abdul Manan, Norzehan ^a   Liu, Grace A ^a   Rosen, Michael K ^a  

^a MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CELL CYCLE PROTEIN; GLUTATHIONE TRANSFERASE; GUANOSINE TRIPHOSPHATASE; RHO FACTOR;

ACTIN FILAMENT; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME BINDING; HUMAN; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; WISKOTT ALDRICH SYNDROME;

AMINO ACID SEQUENCE; BINDING SITES; CDC42 GTP-BINDING PROTEIN; CIRCULAR DICHROISM; CLONING, MOLECULAR; FUNGAL PROTEINS; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MICROFILAMENT PROTEINS; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEINS; SACCHAROMYCES CEREVISIAE PROTEINS; SIGNAL TRANSDUCTION; THERMODYNAMICS; WISKOTT-ALDRICH SYNDROME; WISKOTT-ALDRICH SYNDROME PROTEIN;

VESPIDAE;

EID: 0034624753     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35004513     Document Type: Article

References (44)

1. Bourne, H. R., Sanders, D. A. & McCormick, F. The GTPase superfamily: a conserved switch for diverse cell functions. Nature 348, 125-131 (1990).
2. Hall, A. Rho GTPases and the actin cytoskeleton. Science 279, 509-514 (1998).
3. Machesky, L. M. & Insall, R. H. Signaling to actin dynamics. J. Cell Biol. 146, 267-272 (1999).
4. Derry, J. M. J., Ochs, H. D. & Francke, U. Isolation of a novel gene mutated in the Wiskott-Aldrich syndrome. Cell 78, 635-644 (1994).
5. Burbelo, P. D., Drechsel, D. & Hall, A. A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases. J. Biol. Chem. 270, 29071-29074 (1995).
6. Abdul-Manan, N. et al. Structure of Cdc42 in complex with the GTPase binding domain of the Wiskott-Aldrich syndrome protein. Nature 399, 379-383 (1999).
7. Miki, H. et al. Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP. Nature 391, 93-96 (1998).
8. Rohatgi, R. et al. The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 97, 221-231 (1999).
9. Rudolph, M. et al. The Cdc42/Rac interactive binding region motif of the Wiskott Aldrich syndrome protein (WASP) is necessary but not sufficient for tight binding to Cdc42 and structure formation. J. Biol. Chem. 273, 18067-18076 (1998).
10. Buck, M. Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins. Quart. Rev. Biophys. 31, 297-355 (1998).
11. Cornilescu, G., Delaglio, F. & Bax, A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13, 289-302 (1999).
12. Rohl, C. A., Chakrabartty, A. & Baldwin, R. L. Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume precent trifluoroethanol. Protein Sci. 5, 2623-2637 (1996).
13. Machesky, L. M. et al. Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex. Proc. Natl Acad. Sci. USA 96, 3739-3744 (1999).
14. Winter, D., Lechler, T. & Li, R. Activation of the yeast Arp2/3 complex by Bee1p, a WASP-family protein. Curr. Biol. 9, 501-504 (1999).
15. Yarar, D. et al. The Wiskott-Aldrich syndrome protein directs actin-based motility by stimulating actin nucleation with the Arp2/3 complex. Curr. Biol. 9, 555-558 (1999).
16. Bi, E. & Zigmond, S. H. Actin polymerization: where the WASP stings. Curr. Biol. 9, R160-R163 (1999).
17. Sharman, G. J. & Searle, M. S. Cooperative interaction between the three strands of a designed antiparallel β-sheet. J. Am. Chem. Soc. 120, 5291-5300 (1998).
18. Oda, A. et al. Collagen induces tyrosine phosphorylation of Wiskott-Aldrich syndrome protein in human platelets. Blood 92, 1852-1858 (1998).
19. Baba, Y. et al. Involvement of Wiskott-Aldrich syndrome protein in B-cell cytoplasmic tyrosine kinase pathway. Blood 93, 2003-2012 (1999).
20. Guinamard, R. et al. Tyrosine phosphorylation of the Wiskott-Aldrich syndrome protein by Lyn and Btk regulated by CDC42. FEBS Lett. 434, 431-436 (1998).
21. Kwan, S. et al. Scanning of the Wiskott-Aldrich syndrome (WAS) gene: identification of 18 novel alternations including a possible mutation hotspot at ARG86 resulting in thrombocytopenia, a mild WAS phenotype. Hum. Mol. Genet. 4, 1995-1998 (1995).
22. Villa, A. et al. X-Linked thrombocytopenia and Wiskott-Aldrich syndrome are allelic diseases with mutations in the WASP gene. Nature Genet. 9, 414-417 (1995).
23. Shcherbina, A., Rosen, F. S. & Remold-O'Donnell, E. WASP levels in platelets and lymphocytes of Wiskott-Aldrich syndrome patients correlate with cell dysfunction. J. Immunol. 163, 6314-6320 (1999).
24. Derry, J. M. J. et al. WASP gene mutations in Wiskott-Aldrich syndrome and X-linked thrombocytopenia. Hum. Mol. Genet. 4, 1127-1135 (1995).
25. Kolluri, R. et al. Identification of WASP mutations in patients with Wiskott-Aldrich syndrome and isolated thrombocytopenia reveals allelic heterogeneity at the WAS locus. Hum. Mol. Genet. 4, 1119-1126 (1995).
26. Block, C. et al. Quantitative structure-activity analysis correlation Ras/Raf interaction in vitro to Raf activation in vivo. Nature Struct. Biol. 3, 244-251 (1996).
27. Campbell, S. et al. Increasing complexity of Ras signaling. Oncogene 17, 1395-1413 (1998).
28. Zhao, Z. S. et al. A conserved negative regulatory region in alphaPAK: inhibition of PAK kinases reveals their morphological roles downstream of Cdc42 and Rac1. Mol. Cell. Biol. 18, 2153-2163 (1998).
29. Manser, E. et al. A brain serine/threonine protein kinase activated by Cdc42 and Rac1. Nature 367, 40-46 (1994).
30. Stokoe, D. et al. Activation of Raf as a result of recruitment to the plasma membrane. Science 264, 1463-1467 (1994).
31. Spolar, R. S. & Record, M. T. Jr Coupling of local folding to site-specific binding of proteins to DNA. Science 263, 777-784 (1994).
32. Wright, P. E. & Dyson, H. J. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293, 321-331 (1999).
33. 2H labeled proteins with high sensitivity. J. Am. Chem. Soc. 116, 11655-11666 (1994).
34. Logan, T. M. et al. A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experiments. J. Biomol. NMR 3, 225-231 (1993).
35. Kay, L. E. et al. A gradient-enhanced HCCH-TOCSY experiment for recording side-chain proton and carbon-13 correlations in water samples of proteins. J. Magn. Reson. Ser. B 101, 333-337 (1993).
36. Kuboniwa, H. et al. Measurement of HN-H alpha J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods. J. Biomol. NMR 4, 871-878 (1994).
37. 13C labeling. Biochemistry 28, 7510-7516 (1989).
38. Farrow, N. A. et al. Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation. Biochemistry 33, 5984-6003 (1994).
39. Brunger, A. T. et al. Crystallography & NMR system a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
40. Nilges, M. et al. Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta-spectrin. J. Mol. Biol. 269, 408-422 (1997).
41. Brünger, A. T. X-PLOR manual. (Yale Univ. Press, New Haven, 1993).
42. Laskowski, R. A. et al. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8, 477-486 (1996).
43. Carson, M. J. Ribbons 2, 0. J. Appl. Crystallogr. 24, 958-961 (1991).
44. Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281-296 (1991).