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Chimeric Granulocyte/Macrophage Colony-stimulating Factor/Transforming Growth Factor-β (TGF-β) Receptors Define a Model System for Investigating the Role of Homomeric and Heteromeric Receptors in TGF-β Signaling *

Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 271, Issue: 36, Page: 21758-21766
1996
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Article Description

Transforming growth factor-β (TGF-β) belongs to a family of ligands that regulate cell growth and differentiation. The most commonly observed receptors are referred to as the type I, type II, and type III (betaglycan) TGF-β receptors. Two receptor models have been presented to account for the various cellular responses to TGF-β. The first proposes that all TGF-β signaling results from the formation of a heteromeric type I/type II complex, while the second suggests that distinct type I or type II TGF-β receptor combinations mediate aspects of TGF-β signaling. We have addressed this general question relating to TGF-β signaling by constructing chimeric receptors consisting of the extracellular domain of the granulocyte/macrophage colony-stimulating factor (GM-CSF) α or β receptor fused to the transmembrane and cytoplasmic domain of the type I or type II TGF-β receptor. Since high affinity GM-CSF binding requires dimerization of the α and β ligand binding subunits, the response elicited by defined type I and/or type II TGF-β receptor cytoplasmic domain homomers or heteromers can be examined. We show in mesenchymal AKR-2B cells that while TGF-β-dependent transient luciferase activity, endogenous gene activity, and long-term biological responses are similarly induced by activating the chimeric heteromeric receptors with GM-CSF as the endogenous TGF-β receptor, chimeric homomeric type I/type I or type II/type II receptors are signaling-incompetent.

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