The myristoylated amino terminus of Gαi1 plays a critical role in the structure and function of Gαi1 subunits in solution

Biochemistry

Volumn 42, Issue 26, 2003, Pages 7931-7941

  Preininger, Anita M ^a   Van Eps, Ned ^c   Yu, Nan Jun ^c   Medkova, Martina ^a   Hubbell, Wayne L ^c   Hamm, Heidi E ^b  

^a NORTHWESTERN UNIVERSITY   (United States)

^b VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANISOTROPY; FLUORESCENCE; PARAMAGNETIC RESONANCE; PROTEINS;

MYRISTOYLATION;

BIOCHEMISTRY;

CYSTEINE; GUANINE NUCLEOTIDE BINDING PROTEIN;

ALPHA CHAIN; AMINO TERMINAL SEQUENCE; ANISOTROPY; ARTICLE; CONFORMATIONAL TRANSITION; ELECTRON SPIN RESONANCE; FLUORESCENCE; MUTATION; MYRISTYLATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; STEADY STATE; STRUCTURE ACTIVITY RELATION;

ALUMINUM COMPOUNDS; CYSTEINE; DNA PRIMERS; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FLUORESCENT DYES; FLUORIDES; GTP-BINDING PROTEIN ALPHA SUBUNITS, GI-GO; GUANOSINE 5'-O-(3-THIOTRIPHOSPHATE); GUANOSINE DIPHOSPHATE; HUMANS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MYRISTIC ACID; PROTEIN BINDING; PROTEIN CONFORMATION; SPIN LABELS; STRUCTURE-ACTIVITY RELATIONSHIP; SULFHYDRYL COMPOUNDS;

EID: 0038723729     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0345438     Document Type: Article

References (53)

1. Yang, C. S., Skiba, N. P., Mazzoni, M. R., and Hamm, H. E. (1999) Conformational changes at the carboxyl terminus of Gα occur during G protein activation, J. Biol. Chem. 274, 2379-2385.
2. Lambright, D. G., Noel, J. P., Hamm, H. E., and Sigler, P. B. (1994) Structural determinants for activation of the α-subunit of a heterotrimeric G protein, Nature 369, 621-628.
3. Noel, J. P., Hamm, H. E., and Sigler, P. B. (1993) The 2.2 Å crystal structure of transducin-α complexed with GTPγS, Nature 366, 654-663.
4. i1 and the mechanism of GTP hydrolysis, Science 265, 1405-1412.
5. i1 induced by GTP hydrolysis, Science 270, 954-960.
6. Wang, J., Frost, J. A., Cobb, M. H., and Ross, E. H. (1999) Reciprocal signaling between heterotrimeric G proteins and the p21-stimulated protein kinase, J. Biol. Chem. 274, 31641-31647.
7. i3 with a reduced affinity for βγ dimers and altered guanosine 5′-3-O-(thio)-triphosphate binding, J. Biol. Chem. 267, 24307-24314.
8. Lambright, D. G., Sondek, J., Bohm, A., Skiba, N. P., Hamm, H. E., and Sigler, P. B. (1996) The 2.0 Å crystal structure of a heterotrimeric G protein, Nature 379, 311-319.
9. 2, Cell 83, 1047-1058.
10. Resh, M. D. (1999) Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins, Biochim. Biophys. Acta 1451, 1-16.
11. Linder, M. E., Pang, I. H., Duronio, R. J., Gordon, J. I., Stemweis, P. C., and Gilman, A. G. (1991) Lipid modifications of G protein subunits. Myristoylation of Go alpha increases its affinity for beta gamma, J. Biol. Chem. 266, 4654-4659.
12. Kokame, K., Fukada, Y., Yoshizawa, T., Takao, T., and Shimonishi, Y. (1992) Lipid modification at the N terminus of photoreceptor G-protein α-subunit, Nature 359, 749-752.
13. s, Biochemistry 28, 611-616.
14. van der Neut, R., Pantaloli, C., Nebout, I., Bockaert, J., and Audigier, Y. (1993) Mutagenesis of the amino terminal glycine to alanine in Gαs subunit alters βγ dependent properties and decreases adenylyl cyclase activation, J. Biol. Chem. 268, 436-441.
15. i1 by 2-hydroxymyristate does not interfere with its palmitoylation or membrane association. Evidence that palmitoylation, but not myristoylation, regulates membrane attachment, Biochem. J. 313, 717-720.
16. Moffett, S., Brown, D. A., and Linder, M. E. (2000) Lipid-dependent targeting of G proteins into rafts, J. Biol. Chem. 175, 2191-2198.
17. i1) and c-Src tyrosine kinase to caveolae membranes: clarifying the role of N-myristoylation, Cell. Mol. Biol. 43, 293-303.
18. i1 by expressing the proteins from chimeric open reading frames, J. Biol. Chem. 272, 24673-24678.
19. z signaling, J. Biol. Chem. 270, 9667-9675.
20. Bigay, J., Faurobert, E., Franco, M., and Chabre, M. (1994) Roles of lipid modifications of transducin subunits in their GDP-dependent association and membrane binding, Biochemistry 33, 14081-14090.
21. Wang, Y., Windh, R. T., Chen, C. A., and Manning, D. R. (1999) N-Myristoylation and βγ play roles beyond anchorage in the palmitoylation of the G protein α(o) subunit, J. Biol. Chem. 274, 37435-37442.
22. i2 polypeptide, a G protein α subunit, is required for its signaling and transformation functions, Proc. Natl. Acad. Sci. U.S.A. 89, 9695-9699.
23. t with four proteases defines monoclonal antibody epitope, J. Biol. Chem. 266, 14072-14081.
24. t/i1 chimeras, J. Biol. Chem. 271, 413-424.
25. i1 following dissociation from Gβγ subunit and activation, Biochemistry 41, 9962-9972.
26. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
27. Phillips, W. J., and Cerione, R. A. (1991) Labeling of the βγ subunit complex of transducin with an environmentally sensitive cysteine reagent. Use of fluorescence spectroscopy to monitor transducin subunit interactions, J. Biol. Chem. 266, 11017-11024.
28. Mumby, S. M., and Linder, M. E. (1994) Myristoylation of G-protein α subunits, Methods Enzymol. 237, 255-268.
29. Mazzoni, M. R., and Hamm, H. E. (1993) Tryptophan207 is involved in the GTP-dependent conformational switch in the α subunit of the G protein transducin: chymotryptic digestion patterns of the GTPγS and GDP-bound forms, J. Protein Chem. 12, 215-221.
30. Goldman, S. A., Bruno, G. V., and Freed, J. H. (1972) J. Phys. Chem. 76, 1858-1860.
31. Freed, J. H. (1976) in Spin Labeling: Theory and Application (Berliner, L. J., Ed.) pp 53-132, Academic Press, New York.
32. Budil, D. E., Lee, S., Saxena, S., and Freed, J. H. (1996) Nonlinear-least-squares analysis of slow motion EPR spectra in one and two dimensions using a modified Levenbert-Marquart algorithm, J. Magn. Reson., Ser. A 120, 155-189.
33. Towler, D. A., Adams, S. P., Eubanks, S. R., Towery, D. S., Jackson-Machelski, E., Glaser, L., and Gordon, J. I. (1987) Purification and characterization of yeast myristoyl CoA:protein N-myristoylyl transferase, Proc. Natl. Acad. Sci. U.S.A. 84, 2708-2712.
34. Duronio, R. J., Jackson-Machelski, E., Heuckeroth, R. O., Olins, P. O., Devine, C. S., Yonemoto, W., Slice, L. W., Taylor, S. S., and Gordon, J. I. (1990) Protein N-myristoylation in Escherichia coli: reconstitution of a eukaryotic protein modification in bacteria, Proc. Natl. Acad. Sci. U.S.A. 87, 1506-1510.
35. Mittal, R., Cerione, R. A., and Erickson, J. W. (1994) Aluminum fluoride activation of bovine transducin induces two distinct conformational changes in the α subunit, Biochemistry 33, 10178-10184.
36. i1 and βγ binding. Measuring high affinity interactions in a lipid environment using flow cytometry, J. Biol. Chem. 273, 7934-7940.
37. Lakowicz, J. R. (1999) Principles of fluorescence spectroscopy, 2nd ed., Kluwer Academic/Plenum Publishers, Dordrecht, The Netherlands.
38. Muradov, K. G., and Artemyev, N. O. (2000) Coupling between the N- and C-terminal domains influences transducin-α intrinsic GDP/GTP exchange, Biochemistry 39, 3937-3942.
39. Remmers, A. E., Engel, C., Liu, M., and Neubig, R. R. (1999) Interdomain interactions regulate GDP release from heterotrimeric G proteins, Biochemistry 38, 13795-13800.
40. Thomas, T. O., Bae, H., Medkova, M., and Hamm, H. E. (2001) An intramolecular contact in Gα transducin that participates in maintaining intrinsic GDP release rate, Mol. Cell Biol. Res. Commun. 4, 282-291.
41. Seitz, H. R., Heck, M., Hofmann, K. P., Alt, T., Pellaud, J., and Seelig, A. (1999) Molecular determinants of the reversible membrane anchorage of the G-protein transducin, Biochemistry 38, 7950-7960.
42. s, Cell 77, 1063-1070.
43. Justice, J. M., Bliziotes, M. M., Stevens, L. A., Moss, J., and Vaughan, M. (1995) Involvement of N-myristoylation in monoclonal antibody recognition on chimeric G protein α subunits, J. Biol. Chem. 270, 6436-6439.
44. t, Biochemistry 28, 9873-9880.
45. Morales, J., Fishburn, C. S., Wilson, P. T., and Bourne, H. R. (1998) Plasma membrane localization of G alpha z requires two signals, Mol. Biol. Cell 10, 1-14.
46. Ames, J. B., Tanaka, T., Ikura, M., and Streyer, L. (1995) Nuclear magnetic resonance evidence for a calcium induced extrusion of the myristoyl group of recoverin, J. Biol. Chem. 270, 30909-30913.
47. Tanaka, T., Ames, J. B., Harvey, T. S., Stryer, L., and Ikura, M. (1995) Sequestration of the membrane targeting myristoyl group of recoverin in the calcium-free state, Nature 376, 444-447.
48. Serafini, T., Orci, L., Amherdt, M., Brunner, M., Kahn, R. A., and Rothman, J. E. (1991) ADP ribosylation factor is a subunit of the golgi derived COP-coated vesicles: a novel role for a GTP binding protein, Cell 67, 239-253.
49. 2+ levels, J. Biol. Chem. 270, 1337-1341.
50. Zheng, J., Knighton, D. R., Xuong, N. H., Taylor, S. S., Sowadski, J. M., and Ten Eyck, L. F. (1993) Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations, Protein Sci. 2, 1559-1573.
51. Tholey, A., Pipkorn, R., Bossemeyer, D., Kinzel, V., and Reed, J. (2001) Influence of myristoylation, phosphorylation, and deamidation on the structural behavior of the N-terminus of the catalytic subunit of CAMP-dependent protein kinase, Biochemistry 40, 225-231.
52. McLauglin, S., and Adarem, A. (1995) The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions, Trends Biochem. Sci. 20, 272-276.
53. t, FEBS Lett. 362, 286-290.