Premium
Overlapping and distinct signals through leptin receptor (OB‐R) and a closely related cytokine signal transducer, gp130
Author(s) -
Nakashima Kinichi,
Narazaki Masashi,
Taga Tetsuya
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01430-5
Subject(s) - glycoprotein 130 , protein tyrosine phosphatase , tyrosine phosphorylation , receptor , tyrosine , phosphorylation , leptin receptor , biology , microbiology and biotechnology , stimulation , chemistry , leptin , endocrinology , stat3 , biochemistry , obesity
The structure of leptin receptor (OB‐R) is highly homologous to that of gp130, the common signal transducing receptor component for the interleukin‐6 family of cytokines. Based on this structural similarity, we examined signaling processes initiated by OB‐R in comparison with those by gp130. Stimulation of either a long form of OB‐R or gp130 led to tyrosine phosphorylation of STAT3, whereas stimulation of the truncated form of OB‐R that is predominantly expressed in db / db mice failed to do so. Stimulation of the long form OB‐R did not induce tyrosine phosphorylation of a Src homology domain 2 containing protein tyrosine phosphatase, SHP‐2, while stimulation of gp130 did. In contrast, activation of p42 ERK2 is mediated by either the long form OB‐R or gp130. Two closely related molecules, OB‐R and gp130, thus appear to mediate overlapping but distinct signaling procedures.