Gabarapl2, also known as GABA type A receptor associated protein like 2, was initially linked to protein transport and membrane fusion, but is now well-known for its role in autophagy. It belongs to the GABARAP subfamily, along with GABARAP and GABARAPL1. While there is functional redundancy among subfamily members, Gabarapl2 has a multifaceted role, involved in processes from cellular differentiation to intracellular degradation [1].

In the context of autophagy, Gabarapl2 has been shown to be upregulated in ammonia-induced autophagy and mitophagy, regulated by SIRT5. In this process, SIRT5 controls ammonia production by regulating glutamine metabolism, and changes in SIRT5 levels impact autophagy and mitophagy, with Gabarapl2 serving as one of the autophagy markers [2]. Also, in IFN-γ-treated HeLa cells, Gabarapl2 plays a critical role in restricting the growth of Toxoplasma gondii. It is recruited to membrane structures surrounding parasitophorous vacuoles, and autophagy adaptors are required for its proper localization and function in this IFN-γ-induced immune response [3].

In conclusion, Gabarapl2 is a key player in autophagy-related processes. Its functions in ammonia-induced autophagy and in the IFN-γ-mediated restriction of Toxoplasma gondii growth highlight its importance in maintaining cellular homeostasis and in the immune response. These findings from model-based research contribute to our understanding of autophagy-related diseases and infectious diseases [2,3].