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Titolo:
Agonist-independent and -dependent oligomerization of doparnine D-2 receptors by fusion to fluorescent proteins
Autore:
Wurch, T; Matsumoto, A; Pauwels, PJ;
Indirizzi:
Ctr Rech Pierre Fabre, Dept Cellular & Mol Biol, F-81106 Castres, France Ctr Rech Pierre Fabre Castres France F-81106 ol, F-81106 Castres, France
Titolo Testata:
FEBS LETTERS
fascicolo: 1, volume: 507, anno: 2001,
pagine: 109 - 113
SICI:
0014-5793(20011019)507:1<109:AA-OOD>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
ENERGY-TRANSFER BRET; C6-GLIAL CELL-LINES; COUPLED RECEPTORS; DIMERS; EXPRESSION; DIMERIZATION; BINDING; HETERODIMERIZATION; SYSTEM; LIGHT;
Keywords:
D-2 receptor; oligomerization; fluorescence resonance energy transfer fluorescent protein; intact Cos-7 cell;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Wurch, T Ctr Rech Pierre Fabre, Dept Cellular & Mol Biol, 17 Ave Jean Moulin, F-81106 Castres, France Ctr Rech Pierre Fabre 17 Ave Jean Moulin Castres France F-81106
Citazione:
T. Wurch et al., "Agonist-independent and -dependent oligomerization of doparnine D-2 receptors by fusion to fluorescent proteins", FEBS LETTER, 507(1), 2001, pp. 109-113

Abstract

Oligomerization of the short (D-2S) and long (D-2L) isoforms of the dopamine D-2 receptor was explored in transfected Cos-7 cells by their C-terminalfusion to either an enhanced cyan or enhanced yellow fluorescent protein (ECFP or EYFP) and the fluorescent fusion protein interaction was monitored by, a fluorescence resonance energy transfer (FRET) assay. The pharmacological properties of the fluorescent fusion proteins, as measured by both displacement of \ H-3 \ nemonapride binding and agonist-mediated Stimulation Of\ S-35 \ GTP gammaS binding upon co-expression with a G(alpha0)Cys(351) Ile protein, were not different from the respective wild-type D2S and D2L receptors. Co-expression of D2S:ECFP+D2S:EYFP in a 1:1 ratio and D2L:ECFP+D2L:EYFP in a 27:1 ratio resulted, respectively, in an increase of 26% and 16% in the EYFP-specific fluorescent signal. These data are consistent with a close proximity of both D-2S and D2L receptor pairs of fluorescent fusion proteins in the absence of ligand. The agonist-independent D-2S receptor oligomerization could be attenuated by co-expression with either a wild-type, non-fluorescent D2S or D2L receptor subtype, but not with a distinct beta (2)-adrenoceptor. Incubation with the agonist (-)-norpropylapomorphine dose-dependently (EC50: 0.23 +/-0.06 nM) increased the FRET signal for the co-expression of D2S:ECFP and D2S:EYFP, in support of agonist-dependent D-2S receptor oligomerization. In conclusion, our data strongly suggest the occurrence of dopamine D2 receptor oligomers in intact Cos-7 cells. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 23:09:58