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

نویسندگان

  • S Thiel
  • I Behrmann
  • A Timmermann
  • H Dahmen
  • G Müller-Newen
  • F Schaper
  • J Tavernier
  • V Pitard
  • P C Heinrich
  • L Graeve
چکیده

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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عنوان ژورنال:
  • The Biochemical journal

دوره 339 ( Pt 1)  شماره 

صفحات  -

تاریخ انتشار 1999