The AlphaFold predicted structure of the TRAIP protein Q9BWF2. The highlighted region has been found to bind to the PCNA PIP box. This image was generated using ChimeraX version 1.7.1.Detailed view of residue sequence 447-469 of the TRAIP protein in its binding conformation with the PCNA PIP box.[5] This This image was generated using ChimeraX version 1.7.1.
This gene encodes a protein that contains an N-terminal RING finger motif and a putative coiled-coil domain. A similar murine protein interacts with TNFR-associated factor 1 (TRAF1), TNFR-associated factor 2 (TRAF2), and cylindromatosis. The interaction with TRAF2 inhibits TRAF2-mediated nuclear factor kappa-B, subunit 1 activation that is required for cell activation and protection against apoptosis.[7]
Mitotic DNA synthesis (MiDAS) is thought to be a DNA repair mechanism to salvage DNA that has not finished replication during S phase, which may be due to DNA replication stress (RS).[9] Intrinsic sources of RS include transcription-replication conflicts and “difficult-to-replicate’’ regions.[9] Extrinsic RS includes exposure to genotoxic agents, depletion of dNTPs, and premature S phase activity which can occur in precancerous cells after oncogene activation.[9] Some MiDAS pathways require the TRAIP protein to disassemble the replication complex at the stalled replication fork in cases where RS causes the fork to stall during replication.[9]
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