TY - JOUR
T1 - Overlapping and distinct signals through leptin receptor (OB-R) and a closely related cytokine signal transducer, gp130
AU - Nakashima, Kinichi
AU - Narazaki, Masashi
AU - Taga, Tetsuya
N1 - Funding Information:
We wish to thank Dr. F. de Sauvage (Genentech Inc., CA) for leptin materials. K.N. and M.N. were supported by Research Fellowships of the Japan Society for the Promotion of Science for Young Scientists. This work was supported by a Grant-in-Aid from the Ministry of Education, Science and Culture, Japan (K.N., M.N., T.T.) and Human Frontier Science Program (T.T.).
PY - 1997/1/13
Y1 - 1997/1/13
N2 - 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.
AB - 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.
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U2 - 10.1016/S0014-5793(96)01430-5
DO - 10.1016/S0014-5793(96)01430-5
M3 - Article
C2 - 9003804
AN - SCOPUS:0031036842
SN - 0014-5793
VL - 401
SP - 49
EP - 52
JO - FEBS Letters
JF - FEBS Letters
IS - 1
ER -