Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
REGULATION OF CAMP-MEDIATED GENE-TRANSCRIPTION BY WILD-TYPE AND MUTATED G-PROTEIN ALPHA-SUBUNITS - INHIBITION OF ADENYLYL-CYCLASE ACTIVITY BY MUSCARINIC RECEPTOR-ACTIVATED AND CONSTITUTIVELY ACTIVATED G(0)ALPHA
Autore:
MIGEON JC; THOMAS SL; NATHANSON NM;
Indirizzi:
UNIV WASHINGTON,DEPT PHARMACOL SEATTLE WA 98195 UNIV WASHINGTON,DEPT PHARMACOL SEATTLE WA 98195
Titolo Testata:
The Journal of biological chemistry
fascicolo: 46, volume: 269, anno: 1994,
pagine: 29146 - 29152
SICI:
0021-9258(1994)269:46<29146:ROCGBW>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEOTIDE-BINDING-PROTEIN; CELL-SPECIFIC EXPRESSION; HUMAN PITUITARY-TUMORS; SIGNAL-TRANSDUCTION; BOVINE BRAIN; BETA-GAMMA; MEMBRANE ASSOCIATION; LIPID MODIFICATIONS; CHICK HEART; MYRISTOYLATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
54
Recensione:
Indirizzi per estratti:
Citazione:
J.C. Migeon et al., "REGULATION OF CAMP-MEDIATED GENE-TRANSCRIPTION BY WILD-TYPE AND MUTATED G-PROTEIN ALPHA-SUBUNITS - INHIBITION OF ADENYLYL-CYCLASE ACTIVITY BY MUSCARINIC RECEPTOR-ACTIVATED AND CONSTITUTIVELY ACTIVATED G(0)ALPHA", The Journal of biological chemistry, 269(46), 1994, pp. 29146-29152

Abstract

We have used a luciferase reporter gene under the transcriptional control of a cAMP response element (CRE) to monitor the effects of G-protein alpha subunits on cAMP-regulated gene expression and to examine muscarinic acetylcholine receptor (mAChR) functional coupling to G-proteins. Expression in JEG-3 cells of a mutationally activated G(i) alpha-2 in which glutamine 205 is replaced with leucine (Q205L) decreased forskolin-stimulated expression from the CRE-luciferase gene by up to 75%. Similarly, mutation of glycine 43 (corresponding to glycine 12 in p21(ras)) to valine decreased forskolin-stimulated expression from the CRE-luciferase gene by a maximum of 50%, indicating that this mutationactivates the G-protein and is potentially oncogenic. Transfection ofthe activated Q205L G(o) alpha subunit decreased forskolin stimulation of CRE-luciferase expression. Transfected wild type G(o) alpha was also able to couple the m4 mAChR receptor to inhibition of AC. The amino-terminal myristoylation site was removed from wild type G(i) alpha-2and Q205L G(i) alpha-2 by changing glycine 2 to alanine (G2A). G(i) alpha-2 with the G2A and Q205L mutations was unable to decrease forskolin stimulation of CRE-mediated luciferase activity. Furthermore, G2A G(i) alpha-2 was unable to couple the m4 mAChR to inhibition of AC. Thus, myristoylation is required both for the function of constitutively active Q205L G(i) alpha-2 and for receptor-mediated activation of wildtype G(i) alpha-2.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 18:46:32