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• W2054406052 abstract "The adipocyte secreted hormone leptin (OB) and its receptor (OB-R) are key regulators of mammalian body weight homeostasis. Two predominant isoforms of OB-R have been described: long form (OB-RL) characterized as a signal transducing receptor that is highly expressed in specific nuclei of the hypothalamus; and a short, signaling-defective form (OB-RS) of indeterminate function that is ubiquitously expressed throughout the body. Receptor chimera studies indicate that OB-RL signals via homo-oligomers. However, co-expression experiments have demonstrated that signaling by OB-RL is only marginally susceptible to dominant negative suppression by OB-RS. In the present study we have used receptor epitope tagging to analyze the ligand-independent and -dependent association properties of OB-RS and OB-RL. We present evidence for ligand-independent homo-oligomerization by both receptor isoforms. Ligand treatment of these complexes does not dramatically augment homo-oligomerization. In contrast, hetero-oligomerization between long and short OB-R cannot be detected in the absence of ligand but can be resolved in the presence of ligand. Deletion and substitution mutagenesis of the OB-RL intracellular domain indicates that ligand-independent homo-oligomerization by OB-RL is sensitive to reduction in JAK kinase recruitment capability, suggesting that JAK interaction and signaling competency may provide means for isoform specific OB-R sorting. These results are discussed with regard to possible mechanisms permitting efficient leptin-induced signaling by OB-RL in tissues that co-express OB-RS. J. Cell. Biochem. 73:278–288, 1999. © 1999 Wiley-Liss, Inc." @default.
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• W2054406052 date "1999-05-01" @default.
• W2054406052 modified "2023-10-15" @default.
• W2054406052 title "Evidence for ligand-independent homo-oligomerization of leptin receptor (OB-R) isoforms: A proposed mechanism permitting productive long-form signaling in the presence of excess short-form expression" @default.
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• W2054406052 doi "https://doi.org/10.1002/(sici)1097-4644(19990501)73:2<278::aid-jcb13>3.0.co;2-w" @default.
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