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Updated: May 11, 2026

Studying TGF-β Signaling and TGF-β-induced Epithelial-to-mesenchymal Transition in Breast Cancer and Normal Cells
Published on: October 27, 2020
Dlg5 interacts with the TGF-β receptor and promotes its degradation
Takuhito Sezaki1, Lucia Tomiyama, Yasuhisa Kimura
1Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo, Kyoto 606-8502, Japan.
Abstract:
Discs large homolog 5 (Dlg5) is a member of the membrane-associated guanylate kinase adaptor family of proteins and is involved in epithelial-to-mesenchymal transition via transforming growth factor-β (TGF-β) signaling. However, the mechanism underlying the regulation of TGF-β signaling is unclear. We show here that Dlg5 interacts and colocalizes with both TGF-β type I (TβRI) and type II (TβRII) receptors at the plasma membrane. TβRI activation is not required for this interaction. Furthermore, the overexpression of Dlg5 enhances the degradation of TβRI. Proteasome inhibitors inhibited this enhanced degradation. These results suggest that Dlg5 interacts with TβRs and promotes their degradation.
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