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Volume 272, Number 7, Issue of February 14, 1997 pp. 4065-4071
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Leptin Receptor (OB-R) Signaling
CYTOPLASMIC DOMAIN MUTATIONAL ANALYSIS AND EVIDENCE FOR RECEPTOR HOMO-OLIGOMERIZATION

(Received for publication, July 11, 1996, and in revised form, November 15, 1996)

David W. White Dagger , Karen K. Kuropatwinski § , Rene Devos , Heinz Baumann § and Louis A. Tartaglia Dagger

From Dagger  Millennium Pharmaceuticals, Cambridge, Massachusetts 02215-2406, § Roswell Park Cancer Institute, Department of Molecular and Cellular Biology, Buffalo, New York 14263, and  Roche Research Gent, Jozef Plateaustraat 22, B-9000 Gent, Belgium

The leptin receptor (OB-R) mediates the weight regulatory effects of the adipocyte secreted hormone leptin (OB). Previously we have shown that the long form of OB-R, expressed predominantly in the hypothalamus, can mediate ligand-induced activation of signal transducer and activator of transcription factors 1, 3, and 5 and stimulate transcription via interleukin-6 and hematopoietin receptor responsive gene elements. Here we report that deletion and tyrosine substitution mutagenesis of OB-R identifies two distinct regions of the intracellular domain important for signaling. In addition, granulocyte-colony stimulatory factor receptor/OB-R and OB-R/granulocyte-colony stimulatory factor receptor chimeras are signaling competent and provide evidence that aggregation of two OB-R intracellular domains is sufficient for ligand-induced receptor activation. However, signaling by full-length OB-R appears to be relatively resistant to dominant negative repression by signaling-incompetent OB-R, suggesting that mechanisms exist to permit signaling by the long form of OB-R even in the pretence of excess naturally occurring short form of OB-R.


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