Toxoplasma gondii is an obligate intracellular apicomplexan parasite that chronically infects approximately 30–50% of the global population. Following initial infection, the parasite establishes a lifelong latent state by differentiating into bradyzoites, which persist within host cells. Reactivation of these dormant forms into rapidly replicating tachyzoites can cause severe disease in immunocompromised individuals and congenitally infected newborns. Understanding the molecular mechanisms that govern this developmental switch is crucial for identifying therapeutic strategies to control infection. Recent studies have identified the Toxoplasma GID/CTLH E3 ubiquitin ligase complex as a key regulator of this transition. Here, we present preliminary data aimed at dissecting the role and mechanism of this E3 ligase in T. gondii. By characterizing its function and identifying substrates, this work will inform the development of novel therapeutics, including parasite-specific protein degraders, with applications not only against toxoplasmosis but also other apicomplexan diseases such as malaria.