UCHL5 binds SMAD7 in complex with ubiquitinated TGFBR1

Stable Identifier
Reaction [binding]
Homo sapiens
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

Ubiquitin C-terminal hydrolase UCHL5 (UCH37) strongly binds to SMAD7 and is thereby recruited to TGF-beta receptor complex (Wicks et al. 2005). Another ubiquitin peptidase, USP15, has recently been found to associate with ubiquitinated TGFBR1 through SMAD7 (Eichhorn et al. 2012). The role of UCHL5 was inferred from experiments using recombinant mouse Uchl5 and Smad7 with recombinant human TGF-beta receptors. The role of USP15 was established by experiments with human proteins.

Literature References
PubMed ID Title Journal Year
16027725 The deubiquitinating enzyme UCH37 interacts with Smads and regulates TGF-beta signalling

Wicks, SJ, Haros, K, Maillard, M, Song, L, Cohen, RE, Dijke, PT, Chantry, A

Oncogene 2005
22344298 USP15 stabilizes TGF-? receptor I and promotes oncogenesis through the activation of TGF-? signaling in glioblastoma

Eichhorn, PJ, Rodón, L, Gonzàlez-Juncà, A, Dirac, A, Gili, M, Martínez-Sáez, E, Aura, C, Barba, I, Peg, V, Prat, A, Cuartas, I, Jimenez, J, García-Dorado, D, Sahuquillo, J, Bernards, R, Baselga, J, Seoane, J

Nat Med 2012
Participant Of
Inferred From
Cite Us!