Phosducin induces a structural change in transducin βγ

Structure

Volumn 6, Issue 8, 1998, Pages 1007-1019

  Loew, Andreas ^a   Ho, Yee Kin ^a   Blundell, Tom ^b   Bax, Benjamin ^c  

^a UNIVERSITY OF ILLINOIS   (United States)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^c UNIVERSITY OF LONDON   (United Kingdom)

Author keywords

Heterotrimeric G protein; Prenylation; Rhoclopsin; Signal transduction; Transducin

Indexed keywords

ANIMALIA; BOS TAURUS; BOVINAE;

EID: 0032528863     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00102-6     Document Type: Article

References (43)

1. Bourne, H.R. (1997). How receptors talk to trimeric G proteins. Curr. Opin. Cell Biol. 9, 134-142.
2. Farrens, D.L., Altenbach, C., Yang, K., Hubbell, W.L. & Khorana, H.G. (1996). A light activated conformational switch in rhodopsin. Science 274, 768-770.
3. βγ and transducin complexes in developing normal mice and in mice and dogs with inherited retinal degeneration. Exp. Eye Res. 51, 325-333.
4. Lee, R.H., Brown, B.M. & Lolley, R.N. (1984). Light-induced dephosphorylation of a 33K protein in rod outer segments of rat retina. Biochemistry 23, 1972-1977.
5. Sagoo, M.S. & Lagnado, L. (1997). G-protein deactivation is rate-limiting for shut-off of the phototransduction cascade. Nature 389, 392-395.
6. Lee, R.H., Lieberman, B.S. & Lolley, R.N. (1987). A novel complex from bovine visual cells of a 33000-dalton phosphoprotein with β- and γ-transducin: purification and subunit structure. Biochemistry 26, 3983-3990.
7. Reig, J.A., Yu, L. & Klein, D.C. (1990). Pineal transduction: adrenergic cyclic AMP-dependent phosphorylation of cytoplasmic 33-kDa protein (MEKA) which binds βγ-complex of transducin. J. Biol. Chem. 265, 5816-5824.
8. Bauer, P.H., et al., & Lohse, M.J. (1992). Phosducin is a protein kinase A-regulated G-protein regulator. Nature 358, 73-76.
9. Danner, S. & Lohse, M.J. (1996). Phosducin is a ubiquitous G-protein regulator. Proc. Natl Acad. Sci. USA 93, 10145-10150.
10. Sprang, S.R. (1997). G protein mechanisms: insights from structural analysis. Annu. Rev. Biochem. 66, 639-678.
11. Clapham, D.E. & Nerr, E.J. (1997). G protein βγ subunits. Annu. Rev. Pharmacol. Toxicol. 37, 167-203.
12. Gaudet, R., Bohm, A. & Sigler, P.B. (1996). Crystal structure at 2.4 Å resolution of the complex of transducin βγ and its regulator, phosducin. Cell 87, 577-588.
13. Sondek, J., Bohm, A., Lambright, D.G., Hamm, H.E. & Sigler, P.B. (1996). Crystal structure of a G protein βγ dimer at 2.1 Å resolution. Nature 379, 369-374.
14. 2;. Cell 83, 1047-1058.
15. Lambright, D.G., Sondek, J., Bohm, A., Skiba, N., Hamm, J. & Sigler, P. (1996). The 2.0 Å crystal structure of a heterotrimeric G protein. Nature 379, 311-319.
16. Renault, L., et al., & Wittinghofer, A. (1998). The 1.7 Å structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed β-propeller. Nature 392, 97-101.
17. Xu, J., Wu, D., Slepak, V.Z. & Simon, M.I. (1995). The N terminus of phosducin is involved in binding of βγ subunits of G protein. Proc. Natl Acad. Sci. USA 92, 2086-2090.
18. Blüml, K., et al., & Lohse, M.J. (1997). A small region in phosducin inhibits G-protein βγ-subunit function. EMBO J. 16, 4908-4915.
19. Schröder, S., Blüml, K., Dees, C. & Lohse, M.J. (1997). Identification of a C-terminal binding site for G-protein βγ-subunits in phosducin-like protein. FEBS Lett. 401, 243-246.
20. Leeuw, T., Wu, C., Schrag, J.D., Whiteway, M., Thomas, D.Y. & Leberer, E. (1998). Interaction of a G-protein β-subunit with a conserved sequence in Ste20/PAK family of protein kinases. Nature 391, 191-195.
21. Chen, F. & Lee, R.H. (1997). Phosducin and βγ-transducin interaction I: effects of post-translational modifications. Biochem. Biophys. Res. Commun. 233, 370-374.
22. Yoshida, T., et al., & Bitensky, M.W. (1994). The phosphorylation state of phosducin determines its ability to block transducin subunit interactions and inhibit transducin binding to activated rhodopsin. J. Biol. Chem. 269, 24050-24057.
23. Keep, N.H. et al., & Roberts, G.C. (1997) A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm. Structure 5, 623-633.
24. Gosser, Y.Q. et al., & Rosen, M.K. (1997). C-terminal binding domain of Rho GDP-dissociation inhibitor directs N-terminal inhibitory peptide to GTPases. Nature 387, 814-819.
25. Schalk, I. et al., & Balch, W.E. (1996). Structure and mutational analysis of Rab GDP-dissociation inhibitor. Nature 381, 42-48.
26. 2+ and the βγ-subunit complex on the interactions of guanine nucleotides with G proteins. J. Biol. Chem., 262, 762-766.
27. Lee, R.H., Ting, T.D., Lieberman, B.S., Tobias, D.E., Lolley, R.N. & Ho, Y-K. (1992). Regulation of retinal cGMP cascade by phosducin in bovine rod photoreceptor cells. Interaction of phosducin and transducin. J. Biol. Chem. 267, 25104-25112.
28. Loew, A. & Bax, B. (1998). Purification, crystallization and preliminary crystallographic analysis of bovine brain-type creatine kinase. Acta Cryst. D 54, in press.
29. Chayen, N.E. and Stewart, P.D.S. (1992). Microbatch crystallization under oil - a new technique allowing many small-volume crystallization trials. J. Crystal Growth 122, 176-180.
30. Kabsch, W.J. (1993). Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Cryst. 26, 795-800.
31. Otwinowski, Z. & Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
32. Navaza, J. (1994). Amore - an automated package for molecular replacement. Acta Cryst. A 50, 157-163.
33. Brünger, A.T. (1992). X-PLOR. Version 3.1. A System for X-ray crystallography and NMR. Yale University, New Haven, CT.
34. Read, R.J. (1986). Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Cryst. 42, 140-149.
35. Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
36. Kleywegt, G.J. & Jones, T.A. (1994). Halloween... masks and bones. In From First Map To Final Model. (Bailey, S., Hubbard, R. & Waller, D., eds), pp. 59-66, SERC Daresbury Laboratory, Warrington, UK.
37. Kendall, R.L., Yamada, R. & Bradshaw, R.A. (1990). Cotranslational amino-terminal processing. Methods Enzymol. 185, 398-407.
38. Matsuda, T. et al., & Fukada, Y. (1994). Characterization of interactions between transducin α/βγ-subunits and lipid membranes. J. Biol. Chem. 269, 30358-30363.
39. Sayle, R. & Milner-White, E.J. (1995). RasMol: biomolecular graphics for all. Trends Biochem. Sci. 20, 374.
40. Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
41. Merritt, E.A. & Bacon, D.J. (1997). Raster3D: photorealistic molecular graphics. Methods Enzymol. 277, 505-524.
42. Esnouf, R.M. (1997). An extensively modified version of MolScript that includes greatly enhanced colouring capabilities. J. Mol. Graphics 15, 132-143.
43. Nicholls, A., Sharp, K.A. & Honig, B.J. (1991). Protein folding and association: insight from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 218-296.