[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.
Disciplines :
Biochimie, biophysique & biologie moléculaire
Identifiants :
UNILU:UL-ARTICLE-2008-739
Auteur, co-auteur :
Thiel, S.
BEHRMANN, Iris ; 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.
Langue du document :
Anglais
Titre :
Identification of a Leu-lle internalization motif within the cytoplasmic domain of the leukaemia inhibitory factor receptor
