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The ubiquitin–proteasome system is a highly conserved machinery that plays a crucial role in plant defense against viruses. However, the number of E3 ligases targeting viral proteins remains limited. Although RING‐between‐RING (RBR)‐type E3 ligases are evolutionarily conserved across organisms, their functions in plant responses to biotic stress remain largely unknown. Herein, it is found that the triple gene block 1 (TGB1) protein of the barley stripe mosaic virus (BSMV) undergoes ubiquitination during viral infection. Immunoprecipitation combined with mass spectrometry identified an RBR‐type E3 ligase that interacted with TGB1 in vivo and in vitro. The overexpression of Ariadne‐like protein 8 (ARI8) inhibits, whereas its knockout enhances, the local and systemic spread of BSMV. ARI8 mediated the ubiquitination of TGB1, and its Cys311 residue is required for the ARI8‐mediated degradation of TGB1 and inhibition of BSMV infection. In addition to BSMV, ARI8 negatively regulates infection by other TGB‐containing viruses, including potato virus X and beet necrotic yellow vein virus. Collectively, the findings identified a new E3 ligase that targets a plant viral protein and reveals a previously uncharacterized role for RBR‐type E3 ligases in plant responses to biotic stress, providing a potential molecular target for the development of antiviral strategies in plants. The plant RING‐between‐RING (RBR)‐type E3 ligase, Ariadne‐like protein 8 (ARI8), ubiquitinates and degrades a viral movement protein, restricting virus spread. ARI8 also inhibits other triple gene block 1 (TGB1)‐containing viruses, revealing a broad‐spectrum antiviral role. This study uncovers a previously unknown function of RBR‐type E3 ligases in plant immunity and offers a potential target for antiviral crop improvement.