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Functions and Molecular Mechanisms of Deltex Family Ubiquitin E3 Ligases in Development and Disease

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FRONTIERS MEDIA SA
DOI: 10.3389/fcell.2021.706997

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Deltex family proteins; ubiquitination; ubiquitin E3 ligase; ubiquitin code; protein homeostasis; post-translational modification

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Ubiquitination is a significant posttranslational modification affecting protein stability and function, with the specificity of substrate recognition determined by ubiquitin E3 ligase. The human Deltex (DTX) protein family, functioning as E3 ligases, has five members and plays crucial roles in various physiological and pathological processes, although there is still limited understanding of their structural features and mechanisms of action despite extensive research.
Ubiquitination is a posttranslational modification of proteins that significantly affects protein stability and function. The specificity of substrate recognition is determined by ubiquitin E3 ligase during ubiquitination. Human Deltex (DTX) protein family, which functions as ubiquitin E3 ligases, comprises five members, namely, DTX1, DTX2, DTX3, DTX3L, and DTX4. The characteristics and functional diversity of the DTX family proteins have attracted significant attention over the last decade. DTX proteins have several physiological and pathological roles and are closely associated with cell signal transduction, growth, differentiation, and apoptosis, as well as the occurrence and development of various tumors. Although they have been extensively studied in various species, data on structural features, biological functions, and potential mechanisms of action of the DTX family proteins remain limited. In this review, recent research progress on each member of the DTX family is summarized, providing insights into future research directions and potential strategies in disease diagnosis and therapy.

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