Target Name: DDB1
NCBI ID: G1642
Review Report on DDB1 Target / Biomarker Content of Review Report on DDB1 Target / Biomarker
DDB1
Other Name(s): UV-DDB 1 | XPCe | damage specific DNA binding protein 1 | DNA damage-binding protein 1 | Xeroderma pigmentosum group E complementing protein | XPCE | XPE | DDB1_HUMAN | UV-damaged DNA-binding protein 1 | damage-specific DNA binding protein 1, 127kDa | UV-DDB1 | Damage specific DNA binding protein 1 | XPE-BF | DDBa | XPE-binding factor | XAP1 | Damage-specific DNA-binding protein 1 | Xeroderma pigmentosum group E-complementing protein | DNA damage binding protein 1 | Damage-specific DNA binding protein 1 (127kD) | xeroderma pigmentosum group E-complementing protein | HBV X-associated protein 1 | UV-damaged DNA-binding factor | DDB p127 subunit | DDBA | WHIKERS | XAP-1 | DNA damage-binding protein a

Introduction to DDB1, A Potential Drug Target

In the field of drug discovery and development, identifying potential drug targets or biomarkers is crucial for the development of effective therapies and diagnostic tools. One such target that has gained attention is DDB1 (DNA damage-binding protein 1). This article will explore the significance of DDB1 as a drug target and biomarker, its biological functions, and its potential implications in various diseases.

Understanding DDB1

DDB1 is a protein encoded by the DDB1 gene, which is found in humans. It belongs to the WD40 repeat family of proteins and plays a critical role in DNA repair mechanisms. DDB1 forms a core component of the CUL4A-RING ubiquitin ligase complex, along with CUL4A and RBX1. This complex is responsible for targeting various proteins for ubiquitination and subsequent degradation.

Biological Functions

The primary function of DDB1 is related to its involvement in the DNA repair pathway. It recognizes DNA lesions caused by ultraviolet (UV) radiation and forms a complex with DDB2, known as the UV-damaged DNA-binding complex. This complex recruits other proteins involved in nucleotide excision repair and efficiently removes the DNA damage.

Additionally, DDB1 is implicated in other cellular processes, including cell cycle regulation, transcriptional activation, and chromatin remodeling. It interacts with a range of proteins involved in these processes, highlighting its multifunctional role in cellular homeostasis.

Role of DDB1 in Cancer

Due to its association with the DNA repair pathway, DDB1 has been extensively studied in the context of cancer development and progression. Alterations in DDB1 expression or function have been observed in various cancer types, including lung, breast, and ovarian cancers. These alterations can result from gene mutations, deletions, or epigenetic modifications.

Research has shown that impaired DDB1 function leads to compromised DNA repair mechanisms, making cancer cells more susceptible to accumulating DNA damage. This build-up of DNA damage can further contribute to genomic instability, promoting cancer initiation and progression. Therefore, targeting DDB1 may hold therapeutic potential for developing anti-cancer strategies.

DDB1 as a Drug Target

Given its significant role in DNA repair and cancer development, DDB1 has emerged as a potential drug target. Strategies aimed at modulating DDB1 expression, activity, or protein-protein interactions could provide therapeutic benefits in different disease contexts. For example, inhibiting the CUL4A-DDB1 interaction with small molecules or peptides could disrupt the formation of the ubiquitin ligase complex, leading to increased DNA damage and selective killing of cancer cells.

Moreover, the development of DDB1-specific inhibitors may provide a complementary approach to enhance the efficacy of existing DNA-damaging therapies. By suppressing the repair mechanisms mediated by DDB1, cancer cells could become more vulnerable to DNA-damaging agents, leading to improved treatment outcomes.

DDB1 as a Biomarker

Apart from being a drug target, DDB1 also holds potential as a biomarker. Biomarkers are molecular indicators that can be measured to assess certain biological processes or disease states. In the case of DDB1, aberrant expression or activity levels can indicate a dysfunctional DNA repair pathway, which is characteristic of numerous diseases, including cancer and neurodegenerative disorders.

Detecting DDB1 levels in patient samples, such as blood or tissue, could provide valuable diagnostic and prognostic information. It may help predict treatment response, identify patients who would benefit from DNA-damaging therapies, and monitor the effectiveness of therapeutic interventions.

Conclusion

DDB1 plays a vital role in DNA repair mechanisms and is implicated in various cellular processes. Its dysregulation has been linked to cancer development and progression, making it a promising drug target for anti-cancer therapies. Additionally, DDB1 can serve as a biomarker, providing valuable insights into disease states and treatment strategies. Further research and development efforts are necessary to fully exploit the therapeutic and diagnostic potential of targeting DDB1 in various diseases.

Protein Name: Damage Specific DNA Binding Protein 1

Functions: Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively (PubMed:15448697, PubMed:14739464, PubMed:16260596, PubMed:16482215, PubMed:17079684, PubMed:16407242, PubMed:16407252, PubMed:16940174). Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair (PubMed:15448697, PubMed:16260596, PubMed:16407242, PubMed:16940174). The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches (PubMed:15448697, PubMed:16260596, PubMed:16407242, PubMed:16940174). Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:14739464, PubMed:16407252, PubMed:16482215, PubMed:17079684, PubMed:25043012, PubMed:25108355, PubMed:18332868, PubMed:18381890, PubMed:19966799, PubMed:22118460, PubMed:28886238). The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1 (PubMed:14739464, PubMed:16407252, PubMed:16482215, PubMed:17079684, PubMed:25043012, PubMed:25108355, PubMed:18332868, PubMed:18381890, PubMed:19966799, PubMed:22118460). DCX(DDB2) (also known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage (PubMed:16678110, PubMed:17041588, PubMed:16473935, PubMed:18593899). The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair (PubMed:16678110, PubMed:17041588, PubMed:16473935, PubMed:18593899). DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER (PubMed:15882621). DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication (PubMed:17041588). DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR) (PubMed:12732143). The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (PubMed:26431207). DDB1-mediated CRY1 degradation promotes FOXO1 protein stability and FOXO1-mediated gluconeogenesis in the liver (By similarity). By acting on TET dioxygenses, essential for oocyte maintenance at the primordial follicle stage, hence essential for female fertility (By similarity). Maternal factor required for proper zygotic genome activation and genome reprogramming (By similarity)

The "DDB1 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about DDB1 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

More Common Targets

DDB2 | DDC | DDC-AS1 | DDD core complex | DDHD1 | DDHD2 | DDI1 | DDI2 | DDIAS | DDIT3 | DDIT4 | DDIT4L | DDN | DDO | DDOST | DDR1 | DDR2 | DDRGK1 | DDT | DDTL | DDX1 | DDX10 | DDX11 | DDX11-AS1 | DDX11L1 | DDX11L10 | DDX11L2 | DDX11L8 | DDX11L9 | DDX12P | DDX17 | DDX18 | DDX18P1 | DDX19A | DDX19A-DT | DDX19B | DDX20 | DDX21 | DDX23 | DDX24 | DDX25 | DDX27 | DDX28 | DDX31 | DDX39A | DDX39B | DDX39B-AS1 | DDX3P1 | DDX3X | DDX3Y | DDX4 | DDX41 | DDX42 | DDX43 | DDX46 | DDX47 | DDX49 | DDX5 | DDX50 | DDX50P1 | DDX51 | DDX52 | DDX53 | DDX54 | DDX55 | DDX56 | DDX59 | DDX59-AS1 | DDX6 | DDX60 | DDX60L | DDX6P1 | DEAF1 | Death-associated protein kinase | Decapping Complex | DECR1 | DECR2 | DEDD | DEDD2 | Dedicator of cytokinesis protein | DEF6 | DEF8 | DEFA1 | DEFA10P | DEFA11P | DEFA1B | DEFA3 | DEFA4 | DEFA5 | DEFA6 | DEFA7P | DEFA8P | DEFA9P | DEFB1 | DEFB103A | DEFB103B | DEFB104A | DEFB104B | DEFB105A | DEFB105B