RHOBTB2 binds interacting proteins at the endosome membrane

Stable Identifier
R-HSA-9018787
Type
Reaction [binding]
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
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

RHOBTB2, like other RHOBTB family members, RHOBTB1 and RHOBTB3, binds CUL3 (cullin-3) (Berthold et al. 2008), a core component of BTB-CUL3-RBX1 E3 ubiquitin ligase complexes. Binding of GTP to RHOBTB2, facilitated by the HSP90 chaperone complex, enables binding of RHOBTB2 to CUL3 (Manjarrez et al. 2014). RHOBTB2 is thought to act as the regulatory BTB component of the BTB-CUL3-RBX1 complex by recruiting target proteins for ubiquitination and subsequent proteasome-mediated degradation (Wilkins et al. 2004). RHOBTB2 is a substrate adaptor for Musashi 2 (MSI2), targeting it to CUL3 complexes for ubiquitination and proteasomal degradation, thus suppressing tumorigenesis (Choi et al. 2017).

Literature References
PubMed ID Title Journal Year
15107402 RhoBTB2 is a substrate of the mammalian Cul3 ubiquitin ligase complex

Wilkins, A, Ping, Q, Carpenter, CL

Genes Dev. 2004
24608665 Hsp90-dependent assembly of the DBC2/RhoBTB2-Cullin3 E3-ligase complex

Manjarrez, JR, Sun, L, Prince, T, Matts, RL

PLoS ONE 2014
27941885 DBC2/RhoBTB2 functions as a tumor suppressor protein via Musashi-2 ubiquitination in breast cancer

Choi, YM, Kim, KB, Lee, JH, Chun, YK, An, IS, An, S, Bae, S

Oncogene 2017
18835386 Characterization of RhoBTB-dependent Cul3 ubiquitin ligase complexes--evidence for an autoregulatory mechanism

Berthold, J, Schenkova, K, Ramos, S, Miura, Y, Furukawa, M, Aspenström, P, Rivero, F

Exp. Cell Res. 2008
Participants
Participant Of
Orthologous Events
Authored
Reviewed
Created
Cite Us!