RALBP1-associated Eps domain-containing protein 1 (REPS1) neoantigen (REPS1)

RALBP1-associated Eps domain-containing protein 1 (REPS1) is a multidomain adaptor protein primarily involved in clathrin-mediated endocytosis and intracellular signaling pathways, particularly those mediated by the Ral GTPase (UniProt Q96D71). It contains an Eps15-homology (EH) domain and interacts with RALBP1 to regulate vesicle trafficking and growth factor receptor internalization. In the field of oncology, REPS1 is recognized as a significant source of neoantigens—mutated proteins unique to tumor cells that can be recognized by the immune system. Specifically, in the MC38 murine colon carcinoma model, a point mutation (P45L) in the Reps1 gene creates a highly immunogenic epitope presented by MHC class I (H-2Db), which has become a benchmark for studying neoantigen-specific T-cell responses (Yadav et al., Nature 2014). Consequently, REPS1 neoantigens are targets for personalized cancer immunotherapies, including mRNA-based vaccines and TCR-engineered T-cell therapies, designed to elicit a precise anti-tumor immune response while minimizing damage to healthy tissues (Gubin et al., Nature 2014).

Other names

RALBP1-associated Eps domain-containing protein 1REPS1P95RalBP1-associated Eps15-homology domain-containing protein 1EH domain-containing protein 1

Targeting of mutated REPS1 peptide-MHC complexes by cytotoxic T-lymphocytes to induce tumor cell lysis.