N-terminal domain of Gpa1 (G protein α subunit) is sufficient for plasma membrane targeting in yeast Saccharomyces cerevisiae

Journal of Cell Science

Volumn 111, Issue 21, 1998, Pages 3235-3244

  Gillen, Kathy M ^a,c   Pausch, Mark ^b   Dohlman, Henrik G ^a  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b PFIZER INC   (United States)

^c KENYON COLLEGE   (United States)

Author keywords

GPA1; Pheromone; Yeast

Indexed keywords

CELL SURFACE RECEPTOR; CHIMERIC PROTEIN; GLUTATHIONE TRANSFERASE; GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN SUBUNIT; SUCROSE;

ARTICLE; CELL MEMBRANE; CHIMERA; FRACTIONATION; PRIORITY JOURNAL; PROTEIN DOMAIN; SACCHAROMYCES CEREVISIAE; SIGNAL TRANSDUCTION; YEAST;

AMINO ACID SEQUENCE; ANIMALS; BIOLOGICAL TRANSPORT; CELL MEMBRANE; FUNGAL PROTEINS; GENETIC COMPLEMENTATION TEST; GTP-BINDING PROTEIN ALPHA SUBUNITS; GTP-BINDING PROTEINS; HETEROTRIMERIC GTP-BINDING PROTEINS; PROTEIN STRUCTURE, TERTIARY; RATS; RECEPTORS, PURINERGIC P1; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SPECIES SPECIFICITY; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0031720851     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (36)

1. Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A. and Struhl, K. (eds) (1987). Current Protocols in Molecular Biology. Wiley-Interscience.
2. Blumer, K. J. and Thorner, J. (1990). β and γ subunits of a yeast guanine nucleotide-binding protein are not essential for membrane association of the α subunit but are required for receptor coupling. Proc. Nat. Acad. Sci. USA 87, 4363-4367.
3. Bohm, A., Gaudet, R. and Sigler, P. B. (1997). Structural aspects of heterotrimeric G-protein signaling. Curr. Opin. Biotechnol. 8, 480-487.
4. Busconi, L. and Denker, B. M. (1997). Analysis of the N-terminal binding domain of Goα. Biochhem. J. 328, 23-31.
5. Busconi, L., Boutin, P. M. and Denker, B. M. (1997) N-terminal binding domain of Gα subunits: involvement of amino acids 11-14 of Gαo in membrane attachment. Biochem. J. 323, 239-244.
6. Conklin, B. R. and Bourne, H. R. (1993). Structural elements of Gα subunits that interact with Gβγ, receptors, and effectors. Cell 73, 631-641.
7. Dietzel, C. and Kurjan, J. (1987). The yeast SCG1 gene: A Gα-like protein implicated in the a-and α-factor response pathway. Cell 50, 1001-1010.
8. DiPaolo, G., Lutjens, R., Pellier, V., Stimpson, S. A., Beuchat, M. H., Catsicas, S. and Grenningloh, G. (1997). Targeting of SCG10 to the area of the Golgi complex is mediated by its NH2-terminal region. J. Biol. Chem. 272, 5175-5182.
9. Dohlman, H. G., Thorner, J., Caron, M. G. and Lefkowitz, R. J. (1991). Model systems for the study of seven-transmembrane-segment receptors. Annu. Rev. Biochem. 60, 653-688.
10. Dohlman, H. G., Goldsmith, P., Spiegel, A. M. and Thorner, J. (1993). Pheromone action regulates G-protein α subunit myristoylation in the yeast Saccharomyces cerevisiae. Proc. Nat. Acad. Sci. USA 90, 9688-9692.
11. Dohlman, H. G., Song, J., Ma, D., Courchesne, W. E. and Thorner, J. (1996). Sst2, a factor required for recovery from pheromone-induced cell cycle arrest in the yeast Saccharomyces cerevisiae: Expression, co-localization and genetic interactions with Gpa1 (G-protein α subunit). Mol. Cell Biol. 16, 5194-5209.
12. Guarente, L. (1983). Yeast promoters and lacZ fusions designed to study expression of cloned genes in yeast. Meth. Enzymol. 101, 181-191.
13. Hager, K. M., Mandala, S. M., Davenport, J. W., Speicher, D. W., Benz, E. J. and Slayman, C. W. (1986). Amino acid sequence of the plasma membrane ATPase of Neurospora crassa: deduction from genomic and cDNA sequences. Proc. Nat. Acad. Sci. USA 83, 7693-7697.
14. Hepler, J. R., Biddlecome, G. H., Kleuss, C., Camp, L. A., Hofmann, S. L., Ross, E. M. and Gilman, A. G. (1996). Functional importance of the amino terminus of Gqα. J. Biol. Chem. 271, 496-504.
15. Hirsch, J. P. and Cross, F. R. (1992). Pheromone response in yeast. BioEssays 14, 367-373.
16. Jahng, K. Y., Ferguson, J. and Reed, S. I. (1988). Mutations in a gene encoding the α subunit of a Saccharomyces cerevisiae G protein indicate a role in mating pheromone signaling. Mol. Cell Biol. 8, 2484-2493.
17. Johnson, D. R., Bhatnagar, R. S., Knoll, L. J. and Gordon, J. I. (1994). Genetic and biochemical studies of protein N-myristoylation. Annu. Rev. Biochem. 63, 869-914.
18. Jones, E. (1991). Tackling the protease problem in Saccharomyces cerevisiae. Meth. Enzymol. 194, 428-453.
19. Jones, T. L., Simonds, W. F., Merendino, J. J., Jr., Brann, M. R. and Spiegel, A. M. (1990). Myristoylation of an inhibitory GTP-binding protein α subunit is essential for its membrane attachment. Proc. Nat. Acad. Sci. USA 87, 568-572.
20. Kang, Y., Kane, J., Kurjan, J., Stadel, J. M. and Tipper, D. J. (1990). Effects of expression of mammalian Gα and hybrid mammalian-yeast Gα proteins on the yeast pheromone response signal transduction pathway. Mol. Cell Biol. 10, 2582-2590.
21. Keefer, J. R., Kennedy, M. E. and Limbird, L. E. (1994). Unique structural features important for stabilization versus polarization of the α2A-adrenergic receptor on the basolateral membrane of Madin-Darby canine kidney cells. J. Biol. Chem. 269, 16425-16432.
22. Kurjan, J. (1992). Pheromone response in yeast. Annu. Rev. Biochem. 61, 1097-1129.
23. Liu, J., Hughes, T. E. and Sessa, W. C. (1997) The first 35 amino acids and fatty acylation sites determine the molecular targeting of endothelial nitric oxide synthase into the Golgi region of cells: a green fluorescent protein study. J. Cell Biol. 137, 1525-1535.
24. Miyajima, I., Nakafuku, M., Nakayama, N., Brenner, C., Miyajima, A., Kaibuchi, K., Arai, K. I., Kaziro, Y. and Matsumoto, K. (1987). GPA1, a haploid-specific essential gene, encodes a yeast homolog of mammalian G protein which may be involved in the mating factor-mediated signal transduction pathway. Cell 50, 1011-1019.
25. Mumby, S. M., Heukeroth, R. O., Gordon, J. I. and Gilman, A. G. (1990). G-protein α-subunit expression, myristoylation, and membrane association in COS cells. Proc. Nat. Acad. Sci. USA 87, 728-732.
26. Neer, E. J. (1995). Heterotrimeric G proteins: Organizers of transmembrane signals. Cell 80, 249-257.
27. Price, L. A., Strnad, J., Pausch, M. H. and Hadcock, J. R. (1996). Pharmacological characterization of the rat A2a adenosine receptor functionally coupled to the yeast pheromone response pathway. Mol. Pharmacol. 50, 829-837.
28. Saunders, C. and Limbird, L. E. (1997). Disruption of microtubules reveals two independent apical targeting mechanisms for G-protein-coupled receptors in polarized renal epithelial cells. J. Biol. Chem. 272, 19035-19045.
29. Simonds, W. F., Collins, R. M., Spiegel, A. M. and Brann, M. R. (1989). Membrane attachment of recombinant G-protein α-subunits in excess of βγ subunits in a eukaryotic expression system. Biochem. Biophys. Res. Commun. 164, 46-53.
30. Song, J. and Dohlman, H. G. (1996). Partial constitutive activation of pheromone responses by a palmitoylation site mutant of a G protein α subunit in yeast. Biochemistry 35, 14806-14817.
31. Song, J., Hirschman, J., Gunn, K. and Dohlman, H. G. (1996). Regulation of membrane and subunit interactions by N-myristoylation of a G protein α subunit in yeast. J. Biol. Chem. 271, 20273-20283.
32. Sprang, S. R. (1997). G protein mechanisms: insights from structural analysis. Annu. Rev. Biochem. 66, 639-678.
33. Wedegaertner, P. B., Wilson, P. T. and Bourne, H. R. (1995). Lipid modifications of trimeric G proteins. J. Biol. Chem. 270, 503-506.
34. Whiteway, M., Hougan, L., Dignard, D., Thomas, D. Y., Bell, L., Saari, G. C., Grant, F. J., O'Hara, P. and MacKay, V. L. (1989). The STE4 and STE18 genes of yeast encode potential β and γ subunits of the mating factor receptor-coupled G protein. Cell 56, 467-477.
35. Wilson, P. T. and Bourne, H. R. (1995). Fatty acylation of αz. Effects of palmitoylation and myristoylation on αz signaling. J. Biol. Chem. 270, 9667-9675.
36. Wolven, A., Okamura, H., Rosenblatt, Y. and Resh, M. D. (1997). Palmitoylation of p59fyn is reversible and sufficient for plasma membrane association. Mol. Biol. Cell 8, 1159-1173.