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Titolo:
PHOSPHORYLATION OF THE HUMAN LEUKEMIA INHIBITORY FACTOR (LIF) RECEPTOR BY MITOGEN-ACTIVATED PROTEIN-KINASE AND THE REGULATION OF LIF RECEPTOR FUNCTION BY HETEROLOGOUS RECEPTOR ACTIVATION
Autore:
SCHIEMANN WP; GRAVES LM; BAUMANN H; MORELLA KK; GEARING DP; NIELSEN MD; KREBS EG; NATHANSON NM;
Indirizzi:
UNIV WASHINGTON,DEPT PHARMACOL SEATTLE WA 98195 UNIV WASHINGTON,DEPT PHARMACOL SEATTLE WA 98195 ROSWELL PK CANC INST,DEPT MOLEC BIOL BUFFALO NY 14263 ROSWELL PK CANC INST,DEPT CELLULAR BIOL BUFFALO NY 14263 IMMUNEX RES & DEV CORP SEATTLE WA 98101
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 12, volume: 92, anno: 1995,
pagine: 5361 - 5365
SICI:
0027-8424(1995)92:12<5361:POTHLI>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
IL-6 SIGNAL TRANSDUCER; CILIARY NEUROTROPHIC FACTOR; ONCOSTATIN-M; GP130; EXPRESSION; CLONING; CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
25
Recensione:
Indirizzi per estratti:
Citazione:
W.P. Schiemann et al., "PHOSPHORYLATION OF THE HUMAN LEUKEMIA INHIBITORY FACTOR (LIF) RECEPTOR BY MITOGEN-ACTIVATED PROTEIN-KINASE AND THE REGULATION OF LIF RECEPTOR FUNCTION BY HETEROLOGOUS RECEPTOR ACTIVATION", Proceedings of the National Academy of Sciences of the United Statesof America, 92(12), 1995, pp. 5361-5365

Abstract

We used a bacterially expressed fusion protein containing the entire cytoplasmic domain of the human leukemia inhibitory factor (LIF) receptor to study its phosphorylation in response to LIF stimulation. The dose- and time-dependent relationships for phosphorylation of this construct in extracts of LIF-stimulated 3T3-L1 cells were superimposable with those for the stimulation of mitogen-activated protein kinase (MAPK). Indeed, phosphorylation of the cytoplasmic domain of the low-affinity LIF receptor alpha-subunit (LIFR) in Mono Q-fractionated, LIF-stimulated 3T3-L1 extracts occurred only in those fractions containing activated MAPK; Ser-1044 served as the major phosphorylation site in the human LIFR for MAPK both in agonist-stimulated 3T3-L1 lysates and by recombinant extracellular signal-regulated kinase 2 in vitro. Expression in rat H-35 hepatoma cells of LIFR or chimeric granulocyte-colony-stimulating factor receptor (G-CSFR)-LIFR mutants lacking Ser-1044 failed to affect cytokine-stimulated expression of a reporter gene under the control of the beta-fibrinogen gene promoter but eliminated the insulin-induced attenuation of cytokine-stimulated gene expression, Thus, our results identify the human LIFR as a substrate for MAPK and suggest a mechanism of heterologous receptor regulation of LIFR signaling occurring at Ser-1044.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 19:43:19