Abstract
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.
Highlights
Intracellular protein homeostasis, i.e., proteostasis, is influenced by the dynamic equilibrium between protein synthesis, localization, maintenance, and degradation, all of which are regulated by protein-protein interaction networks (Zhong et al, 2019)
We aim to provide a comprehensive view on characteristic structural features, functions and associated molecular mechanisms of DTX family proteins
The results suggest that 2,087 peptides, corresponding to 1,035 proteins, could be ubiquitinated by DTX2
Summary
Intracellular protein homeostasis, i.e., proteostasis, is influenced by the dynamic equilibrium between protein synthesis, localization, maintenance, and degradation, all of which are regulated by protein-protein interaction networks (Zhong et al, 2019).
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