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Titolo:
Differential regulation of leukemia inhibitory factor-stimulated neuronal gene expression by protein phosphatases SHP-1 and SHP-2 through mitogen-activated protein kinase-dependent and -independent pathways
Autore:
Bartoe, JL; Nathanson, NM;
Indirizzi:
Univ Washington, Dept Pharmacol, Seattle, WA 98195 USA Univ Washington Seattle WA USA 98195 ept Pharmacol, Seattle, WA 98195 USA
Titolo Testata:
JOURNAL OF NEUROCHEMISTRY
fascicolo: 5, volume: 74, anno: 2000,
pagine: 2021 - 2032
SICI:
0022-3042(200005)74:5<2021:DROLIF>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
CILIARY NEUROTROPHIC FACTOR; TRANSDUCING RECEPTOR COMPONENT; MULTIPLE SIGNALING PATHWAYS; CYTOKINE RESPONSE ELEMENT; EPIDERMAL GROWTH-FACTOR; TYROSINE-PHOSPHATASE; PHOSPHATIDYLINOSITOL 3-KINASE; NEURONOTROPHIC FACTOR; SYMPATHETIC NEURONS; BETA-RECEPTOR;
Keywords:
neurokine; gene induction; leukemia inhibitory factor; mitogen-activated protein kinase; SHP-1; SHP-2;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
64
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:
J.L. Bartoe e N.M. Nathanson, "Differential regulation of leukemia inhibitory factor-stimulated neuronal gene expression by protein phosphatases SHP-1 and SHP-2 through mitogen-activated protein kinase-dependent and -independent pathways", J NEUROCHEM, 74(5), 2000, pp. 2021-2032

Abstract

The neurally active cytokine leukemia inhibitory factor (LIF) signals through a bipartite receptor complex composed of LIF receptor alpha (LIFR) and gp130. gp130 and LIFR contain consensus binding motifs for the protein tyrosine phosphatase SHP-2 surrounding tyrosines 118 and 115 (Y118 and Y115) oftheir cytoplasmic domains, respectively. These sites are necessary for maximal activation of mitogen-activated protein kinase (MAPK). Coexpression ofcatalytically inactive, but not wild-type, SHP-2 reduced LIFR- and gp130-mediated activation of MAPK up to 75%. Conversely, coexpression of the wild-type, but not catalytically inactive, SHP-1, a related phosphatase, reducedactivity up to 80%, demonstrating that SHP-2 and SHP-1 have opposing effects on the MAPK pathway. Mutation of Y115 of the cytoplasmic domain of LIFR eliminates receptor-mediated tyrosine phosphorylation of SHP-2. In contrast, SHP-1 association with gp130 and LIFR is constitutive and independent of Y118 and Y115, respectively. SHP-1 has a positive regulatory role on LIF-stimulated vasoactive intestinal peptide (VIP) reporter gene expression in neuronal cells, whereas the effect of SHP-2 is negative. Furthermore, LIF-stimulated MAPK activation negatively regulates this VIP reporter gene induction. SHP-2 also negatively regulates LIF-dependent expression of choline acetyltransferase, but this regulation could be dissociated from its effects on MAPK activation. These data indicate that SHP-1 and SHP-2 are important regulators of LIF-dependent neuronal gene expression via both MAPK-dependentand -independent pathways.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/11/20 alle ore 21:33:10