Pitfalls in the use of transfected overexpression systems to study membrane proteins function: The case of TSH receptor and PRA1

Molecular and Cellular Endocrinology

Volumn 209, Issue 1-2, 2003, Pages 71-75

  Jacobs, Christine ^a   Pirson, Isabelle ^a  

^a FREE UNIVERSITY OF BRUSSELS   (Belgium)

Author keywords

Membrane proteins; PRA1; Transfection

Indexed keywords

COMPLEMENTARY DNA; CYCLIC AMP; CYCLIN D3; GUANINE NUCLEOTIDE BINDING PROTEIN; MEMBRANE PROTEIN; RAB PROTEIN; THYROTROPIN RECEPTOR;

ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL CULTURE; DOG; GENE EXPRESSION SYSTEM; GENE OVEREXPRESSION; GENETIC TRANSFECTION; HORMONE RECEPTOR INTERACTION; IMMUNOFLUORESCENCE; MOLECULAR CLONING; MOLECULAR INTERACTION; NONHUMAN; PRENYLATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN STRUCTURE; SPECIES DIFFERENCE; TWO HYBRID SYSTEM;

EID: 0242361156     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mce.2003.07.002     Document Type: Article

References (19)

1. Bergeron D., Barbeau B., Leger C., Rassart E. Experimental bias in the evaluation of the cellular transient expression in DNA co-transfection experiments. Cell. Mol. Biol. Res. 41(3):1995;155.
2. Allgeier A., Offermanns S., Van Sande J., Spicher K., Schultz G., Dumont J.E. The human thyrotropin receptor activates G-proteins Gs and Gq/11. J. Biol. Chem. 269(19):1994;13733-13735.
3. Allgeier A., Laugwitz K.L., Van Sande J., Schultz G., Dumont J.E. Multiple G-protein coupling of the dog thyrotropin receptor. Mol. Cell. Endocrinol. 127(1):1997;81-90.
4. Bucci C., De Gregorio L., Bruni C.B. Expression analysis and chromosomal assignment of PRA1 and RILP genes. Biochem. Biophys. Res. Commun. 286(4):2001;815-819.
5. El Housni H., Vandenbroere I., Perez-Morga D., Christophe D., Pirson I. A rare case of false positive in a yeast two-hybrid screening: the selection of rearranged bait constructs that produce a functional gal4 activity. Anal. Biochem. 262(1):1998;94-96.
6. Evans D.T., Tillman K.C., Desrosiers R.C. Envelope glycoprotein cytoplasmic domains from diverse lentiviruses interact with the prenylated Rab acceptor. J. Virol. 76(1):2002;327-337.
7. Fenster S.D., Chung W.J., Zhai R., Cases-Langhoff C., Voss B., Garner A.M., Kaempf U., Kindler S., Gundelfinger E.D., Garner C.C. Piccolo, a presynaptic zinc finger protein structurally related to bassoon. Neuron. 25(1):2000;203-214.
8. Fields S., Song O. A novel genetic system to detect protein-protein interactions. Nature. 340(6230):1989;245-246.
9. Figueroa C., Taylor J., Vojtek A.B. Prenylated Rab acceptor protein is a receptor for prenylated small GTPases. J. Biol. Chem. 276(30):2001;28219-28225.
10. Hutt D.M., Da-Silva L.F., Chang L.H., Prosser D.C., Ngsee J.K. PRA1 inhibits the extraction of membrane-bound rab GTPase by GDI1. J. Biol. Chem. 275(24):2000;18511-18519.
11. Kosugi S., Ban T., Kohn L.D. Identification of thyroid-stimulating antibody-specific interaction sites in the N-terminal region of the thyrotropin receptor. Mol. Endocrinol. 7:1993;114.
12. Laurent E., Mockel J., Van Sande J., Graff I., Dumont J.E. Dual activation by thyrotropin of the phospholipase C and cyclic AMP cascades in human thyroid. Mol. Cell. Endocrinol. 52(3):1987;273-278.
13. Li S., Liu X., Ascoli M. p38JAB1 binds to the intracellular precursor of the lutropin/choriogonadotropin receptor and promotes its degradation. J. Biol. Chem. 275(18):2000;13386-13393.
14. Li L.Y., Shih H.M., Liu M.Y., Chen J.Y. The cellular protein PRA1 modulates the anti-apoptotic activity of Epstein-Barr virus BHRF1, a homologue of Bcl-2, through direct interaction. J. Biol. Chem. 276(29):2001;27354-27362.
15. Liang Z., Li G. Mouse prenylated Rab acceptor is a novel Golgi membrane protein. Biochem. Biophys. Res. Commun. 275(2):2000;509-516.
16. Martincic I., Peralta M.E., Ngsee J.K. Isolation and characterization of a dual prenylated Rab and VAMP2 receptor. J. Biol. Chem. 272(43):1997;26991- 26998.
17. Onishi Y., Tsukada K., Yokota J., Raz A. Overexpression of autocrine motility factor receptor (AMFR) in NIH3T3 fibroblasts induces cell transformation. Clin. Exp. Metastasis. 20(1):2003;51-58.
18. Stafford L.J., Xia C., Ma W., Cai Y., Liu M. Identification and characterization of mouse metastasis-suppressor KiSS1 and its G-protein-coupled receptor. Cancer Res. 62(19):2002;5399-5404.
19. Van Sande J., Swillens S., Gerard C., Allgeier A., Massart C., Vassart G., Dumont J.E. In Chinese hamster ovary K1 cells dog and human thyrotropin receptors activate both the cyclic AMP and the phosphatidylinositol 4,5-bisphosphate cascades in the presence of thyrotropin and the cyclic AMP cascade in its absence. Eur. J. Biochem. 229(2):1995;338-343.