Recombinant Human RAD18 protein (GST tag N-Terminus)

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RAD18 also known as E3 ubiquitin-protein ligase RAD18 weighs approximately 56 kDa. It functions as a E3 ubiquitin ligase and is key to the post-replication repair (PRR) pathway. RAD18 is ubiquitously expressed across many tissues including the testis heart and thymus indicating its fundamental role in DNA repair processes. Its primary mechanical job involves the monoubiquitination of PCNA a process important for DNA damage bypass.

Biological function summary

The protein interacts with other repair proteins to ensure the stability of the genome. RAD18 forms part of the larger PRR pathway complex engaging with partner proteins like RAD6 to facilitate the repair of damaged DNA. It orchestrates the recruitment of translesion synthesis (TLS) polymerases at sites of damage playing an instrumental role in resolving stalled replication forks an important aspect of maintaining cellular health and replication fidelity.

Pathways

A significant role emerges for RAD18 in the DNA damage repair and cell cycle checkpoint pathways. Within these pathways RAD18 interacts closely with members of the RAD6 and FANCD2 proteins. It acts as a bridge connecting ubiquitin-mediated signaling and the activation of downstream proteins required for efficient DNA lesion bypass. This highlights its pivotal position in preserving genomic integrity and cellular division processes.

RAD18's malfunction links to cancer development and Fanconi anemia. Its impaired function in the DNA damage repair cascade can lead to genomic instability a hallmark of cancer progression. Additionally through pathways that involve the FANCD2 protein RAD18 deficiencies have been associated with the symptoms of Fanconi anemia a disorder characterized by bone marrow failure and cancer predisposition. Understanding RAD18's role furthers insights into therapeutic strategies for such conditions.