Stimulation of Leukemia Inhibitory Factor Receptor Degradation by Extracellular Signal-regulated Kinase
Leukemia inhibitory factor (LIF) signals via the heterodimeric receptor complex comprising the LIF receptor α subunit (LIFRα) and the common signal transducing subunit for interleukin-6 cytokine receptors, gp130. This study demonstrates that in different cell types, the level of LIFRα decreases d...
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Published in | The Journal of biological chemistry Vol. 275; no. 37; pp. 28793 - 28801 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
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American Society for Biochemistry and Molecular Biology
15.09.2000
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Abstract | Leukemia inhibitory factor (LIF) signals via the heterodimeric receptor complex comprising the LIF receptor α subunit (LIFRα)
and the common signal transducing subunit for interleukin-6 cytokine receptors, gp130. This study demonstrates that in different
cell types, the level of LIFRα decreases during treatment with LIF or the closely related cytokine oncostatin M (OSM). Moreover,
insulin and epidermal growth factor induce a similar LIFRα down-regulation. The regulated loss of LIFRα is specific since
neither gp130 nor OSM receptor β shows a comparable change in turnover. LIFRα down-regulation correlates with reduced cell
responsiveness to LIF. Using protein kinase inhibitors and point mutations in LIFRα, we demonstrate that LIFRα down-regulation
depends on activation of extracellular signal-regulated kinase 1/2 and phosphorylation of the cytoplasmic domain of LIFRα
at serine 185. This modification appears to promote the endosomal/lysosomal pathway of the LIFRα. These results suggest that
extracellular signal-regulated kinase-activating factors like OSM and growth factors have the potential to lower specifically
LIF responsiveness in vivo by regulating LIFRα half-life. |
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AbstractList | Leukemia inhibitory factor (LIF) signals via the heterodimeric receptor complex comprising the LIF receptor alpha subunit (LIFR alpha ) and the common signal transducing subunit for interleukin-6 cytokine receptors, gp130. This study demonstrates that in different cell types, the level of LIFR alpha decreases during treatment with LIF or the closely related cytokine oncostatin M (OSM). Moreover, insulin and epidermal growth factor induce a similar LIFR alpha down- regulation. The regulated loss of LIFR alpha is specific since neither gp130 nor OSM receptor beta shows a comparable change in turnover. LIFR alpha down-regulation correlates with reduced cell responsiveness to LIF. Using protein kinase inhibitors and point mutations in LIFR alpha , we demonstrate that LIFR alpha down-regulation depends on activation of extracellular signal-regulated kinase 1/2 and phosphorylation of the cytoplasmic domain of LIFR alpha at serine 185. This modification appears to promote the endosomal/lysosomal pathway of the LIFR alpha . These results suggest that extracellular signal-regulated kinase-activating factors like OSM and growth factors have the potential to lower specifically LIF responsiveness in vivo by regulating LIFR alpha half-life. Leukemia inhibitory factor (LIF) signals via the heterodimeric receptor complex comprising the LIF receptor α subunit (LIFRα) and the common signal transducing subunit for interleukin-6 cytokine receptors, gp130. This study demonstrates that in different cell types, the level of LIFRα decreases during treatment with LIF or the closely related cytokine oncostatin M (OSM). Moreover, insulin and epidermal growth factor induce a similar LIFRα down-regulation. The regulated loss of LIFRα is specific since neither gp130 nor OSM receptor β shows a comparable change in turnover. LIFRα down-regulation correlates with reduced cell responsiveness to LIF. Using protein kinase inhibitors and point mutations in LIFRα, we demonstrate that LIFRα down-regulation depends on activation of extracellular signal-regulated kinase 1/2 and phosphorylation of the cytoplasmic domain of LIFRα at serine 185. This modification appears to promote the endosomal/lysosomal pathway of the LIFRα. These results suggest that extracellular signal-regulated kinase-activating factors like OSM and growth factors have the potential to lower specifically LIF responsiveness in vivo by regulating LIFRα half-life. Leukemia inhibitory factor (LIF) signals via the heterodimeric receptor complex comprising the LIF receptor alpha subunit (LIFRalpha) and the common signal transducing subunit for interleukin-6 cytokine receptors, gp130. This study demonstrates that in different cell types, the level of LIFRalpha decreases during treatment with LIF or the closely related cytokine oncostatin M (OSM). Moreover, insulin and epidermal growth factor induce a similar LIFRalpha down-regulation. The regulated loss of LIFRalpha is specific since neither gp130 nor OSM receptor beta shows a comparable change in turnover. LIFRalpha down-regulation correlates with reduced cell responsiveness to LIF. Using protein kinase inhibitors and point mutations in LIFRalpha, we demonstrate that LIFRalpha down-regulation depends on activation of extracellular signal-regulated kinase 1/2 and phosphorylation of the cytoplasmic domain of LIFRalpha at serine 185. This modification appears to promote the endosomal/lysosomal pathway of the LIFRalpha. These results suggest that extracellular signal-regulated kinase-activating factors like OSM and growth factors have the potential to lower specifically LIF responsiveness in vivo by regulating LIFRalpha half-life. |
Author | Heinz Baumann Yannick Jacques Olivier Robledo Yanping Wang Anne Godard Frédéric Blanchard Erin Kinzie Vincent Pitard Laurence Duplomb |
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BackLink | https://www.ncbi.nlm.nih.gov/pubmed/10858440$$D View this record in MEDLINE/PubMed |
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Snippet | Leukemia inhibitory factor (LIF) signals via the heterodimeric receptor complex comprising the LIF receptor α subunit (LIFRα)
and the common signal... Leukemia inhibitory factor (LIF) signals via the heterodimeric receptor complex comprising the LIF receptor alpha subunit (LIFRalpha) and the common signal... Leukemia inhibitory factor (LIF) signals via the heterodimeric receptor complex comprising the LIF receptor alpha subunit (LIFR alpha ) and the common signal... |
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SubjectTerms | 3T3 Cells Amino Acid Motifs Animals Down-Regulation Endocytosis Enzyme Activation glycoprotein gp130 Growth Inhibitors - pharmacology HeLa Cells Humans interleukin 6 receptors Interleukin-6 Leukemia Inhibitory Factor Leukemia Inhibitory Factor Receptor alpha Subunit leukemia inhibitory factor receptors Liver Neoplasms - metabolism Lymphokines - pharmacology Lysosomes - metabolism Mice Mitogen-Activated Protein Kinase 1 - physiology Mitogen-Activated Protein Kinase 3 Mitogen-Activated Protein Kinases - physiology oncostatin M Rats Receptors, Cytokine - metabolism Receptors, OSM-LIF |
Title | Stimulation of Leukemia Inhibitory Factor Receptor Degradation by Extracellular Signal-regulated Kinase |
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