Identification of a Leu-Ile internalization motif within the cytoplasmic domain of the leukaemia inhibitory factor receptor

Authors
Thiel, S Behrmann, I Timmermann, A Dahmen, H Muller-Newen, G Schaper, F Tavernier, J Pitard, V Heinrich, PC Graeve, L
Citation
S. Thiel et al., Identification of a Leu-Ile internalization motif within the cytoplasmic domain of the leukaemia inhibitory factor receptor, BIOCHEM J, 339, 1999, pp. 15-19
Citations number
22
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL JOURNAL
ISSN journal
02646021 → ACNP
Volume
339
Year of publication
1999
Part
1
Pages
15 - 19
Database
ISI
SICI code
0264-6021(19990401)339:<15:IOALIM>2.0.ZU;2-Y
Abstract
Leukaemia inhibitory factor (LIF) signals via a heterodimeric receptor comp lex 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-base d internalization motif within the cytoplasmic domain of the LIFR. Our find ings suggest that a heterodimeric LIFR/gp130 complex and homodimeric gp130/ gp130 complex are endocytosed via distinct internalization signals.