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Fig. 1 | Journal of Biomedical Science

Fig. 1

From: E26 transformation-specific transcription variant 5 in development and cancer: modification, regulation and function

Fig. 1

The structure and protein-protein interactions of ETV5. A ETV5 contains four functional domains: N-terminal (N-ter) TAD, NRD, ETS, DBD and C-terminal (C-ter) TAD. ETV5 is subjected to modification at the post-translational level by phosphorylation, SUMOylation and ubiquitylation. The sites of PKA-dependent phosphorylation and SUMOylation, as well as protein binding are marked. Note that the phosphorylation and ubiquitylation sites have not been identified. B ETV5 interacts with Mediator complex subunit 25 (MED25) as a coactivator and recruits cofactor mediator of RNA polymerase II transcription (Mediator) to the MMP1 promoter. C1, C2, C3 ETV5 suppresses PS1 transcription by interacting with zinc finger MYM-type containing 5 (ZMYM5). ETV5 interacts with E-box of MYC proto-oncogene (MYC) symmetrically on human TERTp promoter. ETV5 promotes BAX transcription by interacting with upstream transcription factor 1 (USF1) without binding the promoter. D Formation of the CRL4COP1/DET1 complex leads to proteasome-mediated degradation of ETV5 protein. Fusion of ETV5 with TMPRSS2 and phosphorylation of DET1 inhibits this degradation pathway of ETV5. COP1 interacts with ETV5 to suppresses its transcription activity

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