Tob belongs to the anti-proliferative Tob/BTG family. The level of Tob throughout the cell cycle is regulated by the SCF (Skp1/Cullin/F-box protein) Skp2 ubiquitin ligase (E3) complex. Here, we show that Coronin7 (CRN7) is also involved in Tob degradation. We identified CRN7 as a Tob-interacting molecule. A sequence containing two of the six WD motifs in the middle of CRN7 was responsible for the interaction. CRN7 enhanced the polyubiquitination of Tob in vitro, and overexpression of CRN7 promoted proteasome-dependent degradation of Tob. Furthermore, CRN7 interacted with Cullin1 and Roc1 to form a novel SCF-like E3 complex, suggesting that Tob protein is regulated by multiple ubiquitination machineries.
Structured summary:
Cullin1 physically interacts with CRN7:shown by anti tag coimmunoprecipitation (view interaction)
Roc1 physically interacts with CRN7:shown by anti tag coimmunoprecipitation (view interaction)
CRN7 physically interacts with Tob1:shown by anti tag coimmunoprecipitation (view interaction)
CDC34 physically interacts with CRN7:shown by anti tag coimmunoprecipitation (view interaction)
Tob1 and CRN7 colocalize:shown by fluorescence microscopy (view interaction)
Elongin B physically interacts with CRN7:shown by anti tag coimmunoprecipitation (view interaction)
Elongin C physically interacts with CRN7:shown by anti tag coimmunoprecipitation (view interaction)
Tob1 physically interacts with CRN7:shown by two hybrid (view interaction) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.