MMS22L: A Potential Drug Target and Biomarker for DNA Repair (G253714)

Target Name: MMS22L

NCBI ID: G253714

MMS22L: A Potential Drug Target and Biomarker for DNA Repair

DNA repair is a crucial process in maintaining the integrity of genetic information. DNA repair proteins are involved in repairing damaged DNA, ensuring the continuity of genetic information and the development and growth of healthy organisms. MMS22L, a protein that belongs to the MMS family, is one of these repair proteins. MMS22L has been shown to play an important role in DNA repair, and its potential as a drug target or biomarker has drawn significant interest in the scientific community.

MMS22L: Structure and Function

MMS22L is a 22-kDa protein that was identified as a protein that interacts with the transcription factor p53. p53 is a well-known protein that plays a crucial role in regulating gene expression and DNA repair. MMS22L is composed of a unique N-terminal domain, a transmembrane region, and a C-terminal domain.

The N-terminal domain of MMS22L contains a nucleotide-binding oligomerization (NBO) domain, which is responsible for interacting with p53. The NBO domain is composed of a nucleotide-binding domain and a carboxylic acid domain. The nucleotide-binding domain is responsible for binding to specific nucleotides, while the carboxylic acid domain is involved in the regulation of protein stability and interactions.

The transmembrane region of MMS22L contains a protein-coding region and a putative cytoplasmic localization signal (CLS). The protein-coding region contains several putative RNA-binding domains, which are involved in protein-protein interactions and may be involved in regulating protein function. The CLS is a signal that indicates the presence of the protein in the cytoplasm.

The C-terminal domain of MMS22L contains a catalytic domain, which is responsible for protein catalytic activity. MMS22L is known to contain a nucleotide-exciting protein (NEP) domain, which is involved in protein-protein interactions and may be involved in regulating protein function.

MMS22L in DNA Repair

MMS22L has been shown to play an important role in DNA repair. When DNA is damaged, MMS22L is recruited to the site of damage and interacts with p53 to facilitate the repair process. MMS22L helps to recruit the repair machinery to the damaged site, including the protein homolog (PHF2) and the DNA-binding protein DNA-protein complex (DBP).

In addition to its role in DNA repair, MMS22L has also been shown to play an important role in cell signaling. MMS22L has been shown to interact with several signaling pathways, including the PI3K/Akt signaling pathway, the TGF-β signaling pathway, and the NF-kappa-B signaling pathway.

MMS22L as a Drug Target

MMS22L has been shown to be a potential drug target for several diseases. For example, MMS22L has been shown to be involved in the development of cancer, and inhibitors of MMS22L have been shown to have therapeutic effects in cancer treatment. In addition, MMS22L has also been shown to be involved in neurodegenerative diseases, and inhibitors of MMS22L have been shown to have therapeutic effects in neurodegenerative diseases.

MMS22L as a Biomarker

MMS22L has also been shown to be a potential biomarker for several diseases. For example, MMS22L has been shown to be involved in the development of cancer, and its levels have been shown to be elevated in cancer samples. In addition, MMS22L has also been shown to be involved in neurodegenerative diseases, and its levels have

Protein Name: MMS22 Like, DNA Repair Protein

Functions: Component of the MMS22L-TONSL complex, a complex that promotes homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks (PubMed:21055983, PubMed:21055984, PubMed:21055985, PubMed:21113133, PubMed:26527279, PubMed:27338793, PubMed:29478807). The MMS22L-TONSL complex is required to maintain genome integrity during DNA replication (PubMed:21055983, PubMed:21055984, PubMed:21055985, PubMed:27797818). It mediates the assembly of RAD51 filaments on single-stranded DNA (ssDNA): the MMS22L-TONSL complex is recruited to DSBs following histone replacement by histone chaperones and eviction of the replication protein A complex (RPA/RP-A) from DSBs (PubMed:21055983, PubMed:21055984, PubMed:21055985, PubMed:29478807). Following recruitment to DSBs, the TONSL-MMS22L complex promotes recruitment of RAD51 filaments and subsequent homologous recombination (PubMed:27797818, PubMed:29478807). Within the complex, MMS22L acts by binding ssDNA (PubMed:27797818)

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