Reference : Identification of a Leu-lle internalization motif within the cytoplasmic domain of th...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Identification of a Leu-lle internalization motif within the cytoplasmic domain of the leukaemia inhibitory factor receptor
Thiel, S. [> >]
Behrmann, Iris mailto [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit >]
Timmermann, A. [> >]
Dahmen, H. [> >]
Müller-Newen, G. [> >]
Schaper, F. [> >]
Tavernier, J. [> >]
Pitard, V. [> >]
Heinrich, P. C. [> >]
Graeve, L. [> >]
Biochemical Journal
Portland Press
339 (Pt 1)
Yes (verified by ORBilu)
United Kingdom
[en] Animals ; Isoleucine ; Kinetics ; Leucine ; Leukemia Inhibitory Factor ; Leukemia Inhibitory Factor Receptor alpha Subunit ; Lymphokines ; Membrane Glycoproteins ; Microscopy, Fluorescence ; Receptors, Cytokine ; Interleukin-6 ; Humans ; Growth Inhibitors ; Antigens, CD ; Base Sequence ; COS Cells ; Cell Line ; Cytokine Receptor gp130 ; Cytoplasm ; DNA Primers ; Endocytosis ; Flow Cytometry ; Receptors, OSM-LIF
[en] 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.

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