Ubiquitin and Ubiquitin-like modifiers (UBLs) are both small proteins that can be covalently attached to target proteins in a process called post-translational modification. Both ubiquitin and UBLs regulate a variety of cellular processes, including DNA repair.
Ubiquitin is a well-known modifier that is involved in many cellular processes, including protein degradation, DNA repair, and signaling. Ubiquitin is covalently attached to target proteins through a series of enzymatic reactions involving E1 (activating), E2 (conjugating), and E3 (ligating) enzymes.
UBLs, on the other hand, are a family of modifiers that are structurally similar to ubiquitin and also use E1, E2, and E3 enzymes for conjugation to target proteins.
Like ubiquitin, UBLs can regulate DNA repair processes by modifying the activity and localization of repair proteins. For example, SUMOylation (conjugation of SUMO to target proteins) can regulate the localization and activity of several DNA repair factors, including BRCA1 and RAD51. NEDDylation (conjugation of NEDD8 to target proteins) has also been implicated in the regulation of DNA repair.
Now, we are characterizing the roles of ubiquitin & ubls in the DNA damage response
Ubiquitin plays a crucial role in regulating DNA repair processes by modifying the activity and localization of repair proteins and modulating the DNA damage response. Ubiquitin E3 ligases can ubiquitinate target proteins involved in DNA repair, promoting the recruitment of other repair proteins to the site of DNA damage and enhancing the efficiency of repair.
Our lab focuses on the functional roles of ubiquitin E3 ligase regulating genomic stability in both mitotic cells & non-mitotic cells.
Neuronal genomic instability refers to the occurrence of genetic mutations and DNA damage in neurons, which can lead to neurological disorders and diseases such as Alzheimer's, Parkinson's, and Huntington's. Although neurons are post-mitotic cells and do not divide, they are still susceptible to DNA damage from various sources, including oxidative stress, environmental toxins, and normal cellular metabolism. The accumulation of DNA damage over time can result in genomic instability, which can disrupt neuronal function and contribute to the development of neurological disorders
Our lab focuses on the study that how neurons orchestrate the DNA damage response in the non-mitotic condition.
Protein microarray is a high-throughput technology that allows the simultaneous detection and quantification of thousands of proteins in a single experiment. It involves the immobilization of purified proteins or protein fragments on a solid surface, such as a glass slide or a membrane, and then probing the array with a complex mixture of proteins, such as a cell lysate or a bodily fluid, to detect protein-protein interactions or measure protein expression levels.
Protein microarrays can be used for a variety of applications, including identifying protein-protein interactions, characterizing protein function, and discovering biomarkers for disease diagnosis and prognosis. The technology has many advantages, including its ability to detect low-abundance proteins, its high sensitivity and specificity, and its potential for high-throughput analysis.
Protein microarrays are still a relatively new technology, and their full potential has not yet been realized. However, they have already shown promise in advancing our understanding of protein interactions and their role in disease, and are likely to become an increasingly important tool in proteomics research in the future.