Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
IDENTIFICATION OF A DOMAIN IN THE CARBOXY-TERMINUS OF CCK RECEPTOR THAT AFFECTS ITS INTRACELLULAR TRAFFICKING
Autore:
GO WY; HOLICKY EL; HADAC EM; RAO RV; MILLER LJ;
Indirizzi:
MAYO CLIN & MAYO FDN,CTR BASIC RES DIGEST DIS,GUGGENHEIM 17 ROCHESTERMN 55905 MAYO CLIN & MAYO FDN,CTR BASIC RES DIGEST DIS ROCHESTER MN 55905
Titolo Testata:
American journal of physiology: Gastrointestinal and liver physiology
fascicolo: 1, volume: 38, anno: 1998,
pagine: 56 - 62
SICI:
0193-1857(1998)38:1<56:IOADIT>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
PANCREATIC ACINAR CELL; PROTEIN-COUPLED RECEPTOR; CHOLECYSTOKININ RECEPTOR; PEPTIDE RECEPTOR; BETA(2)-ADRENERGIC RECEPTOR; MEDIATED INTERNALIZATION; CYTOPLASMIC TAIL; DOWN-REGULATION; BETA-ARRESTIN; PHOSPHORYLATION;
Keywords:
G PROTEIN-COUPLED RECEPTOR; RECEPTOR INTERNALIZATION; RECEPTOR TRAFFICKING; ENDOCYTOSIS; CHOLECYSTOKININ;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
41
Recensione:
Indirizzi per estratti:
Citazione:
W.Y. Go et al., "IDENTIFICATION OF A DOMAIN IN THE CARBOXY-TERMINUS OF CCK RECEPTOR THAT AFFECTS ITS INTRACELLULAR TRAFFICKING", American journal of physiology: Gastrointestinal and liver physiology, 38(1), 1998, pp. 56-62

Abstract

The carboxyterminal region of many guanine nucleotide-binding protein(G protein)-coupled receptors contains important regulatory sequencessuch as an NP(x)(2-3)Y motif, a site of fatty acid acylation, and serine-and threonine-rich domains. The type A CCK receptor contains all of these, yet their significance has not been examined. We have, therefore, constructed a series of receptor site mutants and truncations that interfere with each of these motifs and expressed each in Chinese hamster ovary cells where they were studied for radioligand binding, cell signaling, receptor internalization, and intracellular trafficking. Each construct was synthesized and transported appropriately to the cell surface, where CCK bound with high affinity, elicited an inositol 1,4,5-trisphosphate response, and resulted in internalization and normal trafficking. Thus modification or elimination of each of these established sequence motifs had no substantial effect on any of these parameters of receptor and cellular function. However, an additional construct that truncated the carboxy terminus, eliminating an additional 15-amino-acid segment devoid of any currently recognized sequence motifs,resulted in a marked change in receptor trafficking, with all other parameters of receptor function normal. This mutant receptor construct was delayed at the stage of early endosomes, delaying its progress to the lysosome-enriched perinuclear compartment from the rapid time course followed by wildtype receptor and all of the other constructs. It is proposed that this region of the CCK receptor tail contains a new motif important for intracellular receptor trafficking.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 04:43:42