Downloads: 175

Files in This Item:
File Description SizeFormat 
j.febslet.2013.04.015.pdf863.87 kBAdobe PDFView/Open
Title: Dlg5 interacts with the TGF-β receptor and promotes its degradation.
Authors: Sezaki, Takuhito
Tomiyama, Lucia
Kimura, Yasuhisa  kyouindb  KAKEN_id
Ueda, Kazumitsu  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0003-2980-6078 (unconfirmed)
Kioka, Noriyuki  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0002-2708-537X (unconfirmed)
Author's alias: 木岡, 紀幸
Keywords: Discs large homolog 5
TGF-β receptor
Protein degradation
Crohn’s disease
Epithelial to mesenchymal transition
Issue Date: 5-Jun-2013
Publisher: Elsevier B.V.
Journal title: FEBS letters
Volume: 587
Issue: 11
Start page: 1624
End page: 1629
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.
Rights: © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V.
URI: http://hdl.handle.net/2433/175271
DOI(Published Version): 10.1016/j.febslet.2013.04.015
PubMed ID: 23624079
Appears in Collections:Journal Articles

Show full item record

Export to RefWorks


Export Format: 


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.