Rad23B Protein is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
--- [@rad2018] title: RAD23B Protein [@radb2019] --- [@xpcrad2017]
Rad23B Protein is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
--- [@rad2018] title: RAD23B Protein [@radb2019] --- [@xpcrad2017]
:: infobox .infobox-protein [@radb2020] ::
Overview
RAD23 Homolog B (RAD23B) is a paralog of RAD23A with overlapping and distinct functions in nucleotide excision repair (NER) and the [ubiquitin-proteasome system](/mechanisms/ubiquitin-proteasome-system). Like RAD23A, RAD23B serves as a molecular adaptor that bridges DNA damage recognition proteins with the NER machinery and delivers polyubiquitinated substrates to the proteasome. While RAD23A and RAD23B share functional domains, they exhibit tissue-specific expression patterns and may have partially redundant yet distinct physiological roles.
Structure
RAD23B is a 409-amino acid protein with multiple functional domains. It contains an N-terminal ubiquitin-like (Ubl) domain that interacts with the proteasome, and two C-terminal ubiquitin-binding (UBA) domains that bind polyubiquitinated proteins. RAD23B also has an XPC-binding domain that recruits it to DNA damage sites.
Normal Function
RAD23B has dual functions in nucleotide excision repair (NER) and the ubiquitin-proteasome system. As an XPC cofactor, RAD23B helps recruit the TFIIH complex to DNA damage sites for NER. As a proteasome-interacting protein, it helps deliver ubiquitinated substrates for degradation.
In [neurons](/entities/neurons), RAD23B's roles in DNA repair and protein quality control are both critical. The protein is expressed in various brain regions and may compensate for RAD23A deficiency in certain contexts.
Role in Disease
Alzheimer's Disease
RAD23B helps clear damaged proteins via the proteasome. Impaired function may contribute to protein aggregation in AD.
Parkinson's Disease
RAD23B-mediated protein quality control may be relevant to [alpha-synuclein](/proteins/alpha-synuclein) clearance and mitochondrial protein quality control.
Therapeutic Targeting
No RAD23B-targeted therapies exist. The RAD23 family proteins represent potential therapeutic targets for enhancing protein clearance in neurodegenerative diseases.
Key Publications
[RAD23B structure and function (2004)](https://doi.org/10.1074/jbc.M401917200)
[RAD23 proteins in DNA repair (2018)](https://pubmed.ncbi.nlm.nih.gov/29446774/)
[RAD23B in proteasomal degradation (2019)](https://pubmed.ncbi.nlm.nih.gov/31141792/)
[XPC-RAD23 complex in damage recognition (2017)](https://pubmed.ncbi.nlm.nih.gov/29150379/)
[RAD23B expression in brain (2020)](https://pubmed.ncbi.nlm.nih.gov/32845567/)
Background
The study of Rad23B Protein has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.
External Links
[PubMed](https://pubmed.ncbi.nlm.nih.gov/) - Biomedical literature
[Alzheimer's Disease Neuroimaging Initiative](https://adni.loni.usc.edu/) - Research data
[Allen Brain Atlas](https://brain-map.org/) - Brain gene expression data