Abstract
Leukaemia inhibitory factor (LIF) signals via a heterodimeric receptor complex comprised of the LIF receptor (LIFR) and the interleukin (IL)-6 signal transducer gp130. Upon binding to its cognate receptor LIF is internalized. In this study, we show that the LIFR is endocytosed independently of gp130. By using a heterochimaeric receptor system we identified a dileucine-based internalization motif within the cytoplasmic domain of the LIFR. Our findings suggest that a heterodimeric LIFR/gp130 complex and homodimeric gp130/gp130 complex are endocytosed via distinct internalization signals.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Antigens, CD / metabolism
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Base Sequence
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COS Cells
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Cell Line
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Cytokine Receptor gp130
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Cytoplasm / metabolism*
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DNA Primers
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Endocytosis*
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Flow Cytometry
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Growth Inhibitors*
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Humans
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Interleukin-6*
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Isoleucine / metabolism*
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Kinetics
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Leucine / metabolism*
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Leukemia Inhibitory Factor
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Leukemia Inhibitory Factor Receptor alpha Subunit
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Lymphokines / metabolism
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Membrane Glycoproteins / metabolism
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Microscopy, Fluorescence
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Receptors, Cytokine / chemistry
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Receptors, Cytokine / metabolism*
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Receptors, OSM-LIF
Substances
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Antigens, CD
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DNA Primers
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Growth Inhibitors
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IL6ST protein, human
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Interleukin-6
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LIF protein, human
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LIFR protein, human
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Leukemia Inhibitory Factor
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Leukemia Inhibitory Factor Receptor alpha Subunit
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Lymphokines
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Membrane Glycoproteins
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Receptors, Cytokine
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Receptors, OSM-LIF
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Isoleucine
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Cytokine Receptor gp130
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Leucine