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

Biochem J. 1999 Apr 1;339 ( Pt 1)(Pt 1):15-9.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antigens, CD / metabolism
  • Base Sequence
  • COS Cells
  • Cell Line
  • Cytokine Receptor gp130
  • Cytoplasm / metabolism*
  • DNA Primers
  • Endocytosis*
  • Flow Cytometry
  • Growth Inhibitors*
  • Humans
  • Interleukin-6*
  • Isoleucine / metabolism*
  • Kinetics
  • Leucine / metabolism*
  • Leukemia Inhibitory Factor
  • Leukemia Inhibitory Factor Receptor alpha Subunit
  • Lymphokines / metabolism
  • Membrane Glycoproteins / metabolism
  • Microscopy, Fluorescence
  • Receptors, Cytokine / chemistry
  • Receptors, Cytokine / metabolism*
  • Receptors, OSM-LIF

Substances

  • Antigens, CD
  • DNA Primers
  • Growth Inhibitors
  • IL6ST protein, human
  • Interleukin-6
  • LIF protein, human
  • LIFR protein, human
  • Leukemia Inhibitory Factor
  • Leukemia Inhibitory Factor Receptor alpha Subunit
  • Lymphokines
  • Membrane Glycoproteins
  • Receptors, Cytokine
  • Receptors, OSM-LIF
  • Isoleucine
  • Cytokine Receptor gp130
  • Leucine