Leptin receptor (OB-R) oligomerizes with itself but not with its closely related cytokine signal transducer gp130

Kinichi Nakashima, Masashi Narazaki, Tetsuya Taga

Research output: Contribution to journalArticle

73 Citations (Scopus)

Abstract

Leptin (OB) exerts weight-reducing effects in mice. The structure of tile receptor for this factor, OB-R, is considerably similar to those of gp130, the common signal transducing receptor component for the interleukin-6 (IL-6) family of cytokines, and leukemia inhibitory factor receptor (LIFR). Since the IL-6 family of cytokines signal through gp130 homodimer or gp130/LIFR heterodimer, we have examined in this study the possible involvement of gp130 and LIFR in leptin signaling through OB-R. Leptin stimulation induces tyrosine phosphorylation of neither gp130 nor LIFR, while LIF stimulation does both. As examined by using two differently epitope-tagged OB-R molecules, the spontaneous homo-oligomerization of OB-R has been elucidated. Ba/F3 cells, which do not express gp130, are non-responsive to leptin and exhibit increased DNA synthesis in response to leptin after transfection of OB-R cDNA alone. OB-R appears to transduce the signal via its homo-oligomerization without interaction with gp130 or LIFR.

Original languageEnglish
Pages (from-to)79-82
Number of pages4
JournalFEBS Letters
Volume403
Issue number1
DOIs
Publication statusPublished - Feb 10 1997
Externally publishedYes

Fingerprint

OSM-LIF Receptors
Cytokine Receptor gp130
Leptin Receptors
Leptin
Cytokines
Oligomerization
R388
Interleukin-6
Phosphorylation
Tile
Transfection
Tyrosine
Epitopes
Complementary DNA
Weights and Measures
Molecules
DNA

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Leptin receptor (OB-R) oligomerizes with itself but not with its closely related cytokine signal transducer gp130. / Nakashima, Kinichi; Narazaki, Masashi; Taga, Tetsuya.

In: FEBS Letters, Vol. 403, No. 1, 10.02.1997, p. 79-82.

Research output: Contribution to journalArticle

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