MycBP2: A Potential Drug Target (G23077)

Target Name: MYCBP2

NCBI ID: G23077

MycBP2: A Potential Drug Target

MycBP2 (Highwire) is a protein that is expressed in various tissues of the body, including the brain, heart, and kidneys. It is a member of the MycBP family of proteins, which are known for their role in cell-signaling pathways. One of the unique features of MycBP2 is its ability to form a highly stable binary complex with the transcription factor p53, which can modulate the activity of multiple downstream targets.

The discovery and characterization of MycBP2 was made by a team of researchers at the University of California, San Diego. The researchers identified MycBP2 as a potential drug target due to its ability to interact with p53 and its involvement in a variety of cellular processes. In addition, the researchers found that MycBP2 was overexpressed in a variety of human diseases, including cancer, neurodegenerative diseases, and cardiovascular disease.

The team then went on to use a variety of techniques to study the molecular mechanisms underlying MycBP2's interaction with p53. They found that MycBP2 and p53 can form a stable binary complex through a process known as protein-protein interactions. This interaction is mediated by a unique protein called NEDD8, which is a structural protein that is expressed in various tissues of the body.

The researchers also found that MycBP2 can modulate the activity of p53 through a variety of mechanisms. For example, they found that MycBP2 can inhibit the phosphorylation of p53 at itsSer-189 site, which is a critical modification that regulates the activity of the transcription factor. In addition, MycBP2 can increase the levels of p53 in cells, which can lead to an increase in the level of transcription factor activity.

The team also investigated the role of MycBP2 in a variety of cellular processes, including cell division, apoptosis, and inflammation. They found that MycBP2 is involved in these processes by regulating the activity of p53 and other transcription factors.

In addition to its role in cell-signaling pathways, the researchers also found that MycBP2 is involved in the regulation of cellular processes that are important for maintaining tissue homeostasis. For example, they found that MycBP2 is involved in the regulation of cell migration and the maintenance of blood pressure, which are critical for maintaining the structure and function of tissues.

Given the unique mechanisms of MycBP2 and its potential as a drug target, the team is actively pursuing research on the use of MycBP2 as a therapeutic agent. They are exploring a variety of strategies, including small molecules, antibodies, and gene therapies, to identify compounds that can modulate the activity of MycBP2 and achieve the desired therapeutic effects.

In conclusion, MycBP2 is a protein that is expressed in various tissues of the body and is involved in a variety of cellular processes. The team has identified MycBP2 as a potential drug target due to its ability to interact with p53 and its involvement in a variety of cellular processes. Further research is needed to fully understand the unique mechanisms of MycBP2 and its potential as a therapeutic agent.

Protein Name: MYC Binding Protein 2

Functions: Atypical E3 ubiquitin-protein ligase which specifically mediates ubiquitination of threonine and serine residues on target proteins, instead of ubiquitinating lysine residues (PubMed:29643511). Shows esterification activity towards both threonine and serine, with a preference for threonine, and acts via two essential catalytic cysteine residues that relay ubiquitin to its substrate via thioester intermediates (PubMed:29643511). Interacts with the E2 enzymes UBE2D1, UBE2D3, UBE2E1 and UBE2L3 (PubMed:18308511, PubMed:29643511). Plays a key role in neural development, probably by mediating ubiquitination of threonine residues on target proteins (Probable). Involved in different processes such as regulation of neurite outgrowth, synaptic growth, synaptogenesis and axon degeneration (By similarity). Required for the formation of major central nervous system axon tracts (By similarity). Required for proper axon growth by regulating axon navigation and axon branching: acts by regulating the subcellular location and stability of MAP3K12/DLK (By similarity). Required for proper localization of retinogeniculate projections but not for eye-specific segregation (By similarity). Regulates axon guidance in the olfactory system (By similarity). Involved in Wallerian axon degeneration, an evolutionarily conserved process that drives the loss of damaged axons: acts by promoting destabilization of NMNAT2, probably via ubiquitination of NMNAT2 (By similarity). Catalyzes ubiquitination of threonine and/or serine residues on NMNAT2, consequences of threonine and/or serine ubiquitination are however unknown (PubMed:29643511). Regulates the internalization of TRPV1 in peripheral sensory neurons (By similarity). Mediates ubiquitination and subsequent proteasomal degradation of TSC2/tuberin (PubMed:18308511, PubMed:27278822). Independently of the E3 ubiquitin-protein ligase activity, also acts as a guanosine exchange factor (GEF) for RAN in neurons of dorsal root ganglia (PubMed:26304119). May function as a facilitator or regulator of transcriptional activation by MYC (PubMed:9689053). Acts in concert with HUWE1 to regulate the circadian clock gene expression by promoting the lithium-induced ubiquination and degradation of NR1D1 (PubMed:20534529)

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