The post-translational modification of proteins plays a pivotal role in regulating cellular functions and orchestrating complex biological processes. Protein arginylation, a relatively recently discovered modification, involves the covalent attachment of an arginine residue to the N-terminus of a protein, catalyzed by arginyltransferase enzymes. This modification has emerged as a key regulator of protein stability, localization and activity, impacting a wide range of cellular processes. In this review, we explore the interplay between functional dynamics and protein arginylation, shedding light on the diverse roles of this modification in health and disease. We discuss the molecular mechanisms underlying arginylation, its regulation and its impact on protein function. Furthermore, we highlight recent advancements in the field, including the identification of novel substrates and the development of potential therapeutic strategies targeting arginylation. This comprehensive overview provides insights into the multifaceted nature of protein arginylation and its significance in cellular biology and human health.
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