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Titolo:
Phosphorylation of human gp130 at Ser-782 adjacent to the di-leucine internalization motif - Effects on expression and signaling
Autore:
Gibson, RM; Schiemann, WP; Prichard, LB; Reno, JM; Ericsson, LH; Nathanson, NM;
Indirizzi:
Univ Washington, Dept Pharmacol, Seattle, WA 98195 USA Univ Washington Seattle WA USA 98195 ept Pharmacol, Seattle, WA 98195 USA Univ Washington, Dept Biochem, Seattle, WA 98195 USA Univ Washington Seattle WA USA 98195 Dept Biochem, Seattle, WA 98195 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 29, volume: 275, anno: 2000,
pagine: 22574 - 22582
SICI:
0021-9258(20000721)275:29<22574:POHGAS>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
LEUKEMIA INHIBITORY FACTOR; ACTIVATED PROTEIN-KINASE; MUSCARINIC ACETYLCHOLINE-RECEPTOR; LIGAND-INDUCED ENDOCYTOSIS; FACTOR-II RECEPTOR; T-CELL RECEPTOR; CYTOPLASMIC DOMAIN; TRANSDUCER GP130; DOWN-REGULATION; GROWTH-FACTOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
57
Recensione:
Indirizzi per estratti:
Indirizzo: Nathanson, NM Univ Washington, Dept Pharmacol, Box 357750, Seattle, WA 98195 USA Univ Washington Box 357750 Seattle WA USA 98195 WA 98195 USA
Citazione:
R.M. Gibson et al., "Phosphorylation of human gp130 at Ser-782 adjacent to the di-leucine internalization motif - Effects on expression and signaling", J BIOL CHEM, 275(29), 2000, pp. 22574-22582

Abstract

The receptor for leukemia inhibitory factor (LIF) consists of two polypeptides, the LIF receptor and gp130. Agonist stimulation has been shown previously to cause phosphorylation of gp130 on serine, threonine, and tyrosine residues. We found that gp130 fusion proteins were phosphorylated exclusively on Ser-782 by LIF- and growth factor-stimulated 3T3-L1 cell extracts. Ser-780 was required for phosphorylation of Ser-782 but was not itself phosphorylated. Ser-782 is located immediately N-terminal to the di-leucine motif of gp130, which regulates internalization of the receptor. Transient expression of chimeric granulocyte colony-stimulating factor receptor (G-CSFR)-gp130(S782A) receptors resulted in increased cell surface expression in COS-7cells and increased ability to induce vasoactive intestinal peptide gene expression in IMR-32 neuroblastoma cells when compared with expression of chimeric receptors containing wild-type gp130 cytoplasmic domains. These results identify Ser-782 as the major phosphorylated serine residue in human gp130 and indicate that this site regulates cell surface expression of the receptor polypeptide.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 07:08:27