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

Lidong Wang1, Xiaodan Sun2, Jingni He1

  • 1Department of General Surgery, Shengjing Hospital of China Medical University, Shenyang, China.

Insights

The Deltex (DTX) protein family, crucial ubiquitin E3 ligases, impacts protein stability and cell functions. This review summarizes DTX protein research, highlighting their roles in disease and potential therapeutic strategies.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Ubiquitination is a key posttranslational modification regulating protein stability and function.
  • Ubiquitin E3 ligases, like the human Deltex (DTX) protein family, dictate substrate specificity in ubiquitination.
  • The DTX family (DTX1-4, DTX3L) plays significant roles in cellular processes and disease.

Purpose of the Study:

  • To review recent advancements in understanding the DTX protein family.
  • To consolidate knowledge on the structural features, biological functions, and mechanisms of DTX proteins.
  • To identify future research directions and therapeutic strategies related to DTX proteins.

Main Methods:

  • Literature review of recent research on DTX family proteins.
  • Synthesis of data on structural characteristics and biological functions.
  • Analysis of DTX protein involvement in physiological and pathological processes.

Main Results:

  • DTX proteins are involved in cell signaling, growth, differentiation, and apoptosis.
  • The DTX family is implicated in the development of various tumors.
  • Despite extensive study, detailed structural and mechanistic data for DTX proteins remain limited.

Conclusions:

  • The DTX protein family exhibits diverse functions and is critical in cellular regulation and disease.
  • Further research is needed to elucidate the structural and mechanistic aspects of DTX proteins.
  • Understanding DTX proteins offers potential for novel diagnostic and therapeutic approaches in diseases like cancer.

Related Concept Videos

Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
7.9K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
8.0K
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR...
2.3K
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
1.2K
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
3.2K
Canonical Wnt Signaling Pathway02:54

Canonical Wnt Signaling Pathway

The gene encoding the main signaling molecules of the Wnt signaling pathways (the Wnt proteins) was discovered almost four decades ago by Nüsslein-Volhard and Wieschaus. They identified and originally named the gene "wingless" (wg) after a phenotype discovered during their landmark genetic screen in Drosophila for body pattern defects. At around the same time, another researcher named Harold Varmus found that a murine tumor virus activates the mammalian wg homolog, Int-1, which...
9.3K