DNMBP (Scaffold Protein TUBA): A Potential Drug Target and Biomarker
DNMBP (Scaffold Protein TUBA): A Potential Drug Target and Biomarker
Dna-binding proteins play a crucial role in various cellular processes, including DNA replication, repair, and transcription. Among them, scaffold proteins are unique in their ability to physically hold onto DNA and facilitate its accessible to transcription factors for gene expression. The protein TUBA (Tubulin-associated protein B), a key component of microtubules, is a well-established scaffold protein that has been implicated in various diseases, including neurodegenerative disorders, cancer, and developmental defects. In this article, we discuss the potential drug target and biomarker properties of TUBA, focusing on its involvement in the context of neurodegenerative diseases.
The Scaffold Protein TUBA: Structure, Functions, and Interactions
TUBA is a 25 kDa protein that is highly homogeneous with a molecular weight of approximately 30 kDa. It is composed of a 155 amino acid residue and is primarily localized to the cytoskeleton, where it interacts with microtubules and other proteins. TUBA has a unique feature that consists of a 100 amino acid alpha-helical region that is involved in the formation of a covalent complex with microtubules. This interaction between TUBA and microtubules plays a crucial role in the regulation of microtubule dynamics and functions, including the transport of organelles, vesicles, and molecules to the cell surface and the control of mechanical forces that arise from the cytoskeleton.
In addition to its role in microtubule dynamics, TUBA is also involved in various cellular processes that are crucial for cell survival and growth, including cell division, apoptosis, angiogenesis, and inflammation. TUBA has been implicated in the regulation of cell proliferation, differentiation, and survival, and its expression has been observed in various types of cancer, including breast, ovarian, and prostate cancers.
Drug Targeting Strategies for TUBA
TUBA has been identified as a potential drug target due to its unique structure and its involvement in various cellular processes that are associated with the development and progression of diseases. Several drug targeting strategies have been proposed to target TUBA, including:
1. Small Interfering RNA (siRNA) Therapies:siRNA is a naturally occurring RNA molecule that can be used to knockdown gene expression in a variety of organisms, including humans. TUBA is a target gene that can be effectively knockdown using siRNA-based therapies.
2. Monoclonal Antibodies: Monoclonal antibodies (MRAs) are laboratory-produced antibodies that can be used to target specific proteins with high affinity. TUBA is a potential target protein that can be effectively targeted using MRAs.
3. chimeric antibodies: Chimeric antibodies are antibodies that consist of two distinct constant (C1) regions and an variable (C2) region. TUBA is a target protein that can be effectively targeted using chimeric antibodies.
4. Domain-Enrichment: Domain-enrichment is a technique that involves the addition of specific domains or motifs to the protein of interest to enhance its stability, solubility, or activity. TUBA can be domain-enriched using various techniques to increase its activity or stability.
Biomarker Properties of TUBA
TUBA has been suggested as a potential biomarker for various diseases, including neurodegenerative disorders, cancer, and developmental defects. Several studies have demonstrated the utility of TUBA as a biomarker in these conditions, including:
1. Neurodegenerative Disorders: TUBA has been shown to be involved in the development and progression of neurodegenerative disorders, including Alzheimer's disease, Parkinson's disease, and Huntington's disease.
2. Cancer: TUBA has been implicated in the development
Protein Name: Dynamin Binding Protein
Functions: Plays a critical role as a guanine nucleotide exchange factor (GEF) for CDC42 in several intracellular processes associated with the actin and microtubule cytoskeleton. Regulates the structure of apical junctions through F-actin organization in epithelial cells (PubMed:19767742, PubMed:17015620). Participates in the normal lumenogenesis of epithelial cell cysts by regulating spindle orientation (PubMed:20479467). Plays a role in ciliogenesis (By similarity). May play a role in membrane trafficking between the cell surface and the Golgi (By similarity)
More Common Targets
DNMBP-AS1 | DNMT1 | DNMT1-G9a-PCNA complex | DNMT1-HDAC2-DMAP1 complex | DNMT1-Rb-E2F1-HDAC1 complex | DNMT3A | DNMT3AP1 | DNMT3B | DNMT3L | DNPEP | DNPH1 | DNTT | DNTTIP1 | DNTTIP2 | DOC2A | DOC2B | DOC2GP | DOCK1 | DOCK10 | DOCK11 | DOCK2 | DOCK3 | DOCK4 | DOCK4-AS1 | DOCK5 | DOCK6 | DOCK7 | DOCK8 | DOCK8-AS1 | DOCK9 | DOCK9-DT | DOHH | DOK1 | DOK2 | DOK3 | DOK4 | DOK5 | DOK6 | DOK7 | Dolichol-phosphate-mannose synthase complex | DOLK | DOLPP1 | DONSON | DOP1A | DOP1B | Dopamine receptor | DOT1L | Double homeobox protein 4 | DP2-E2F4 complex | DPAGT1 | DPCD | DPEP1 | DPEP2 | DPEP3 | DPF1 | DPF2 | DPF3 | DPH1 | DPH2 | DPH3 | DPH3P1 | DPH5 | DPH5-DT | DPH6 | DPH6-DT | DPH7 | DPM1 | DPM2 | DPM3 | DPP10 | DPP10-AS1 | DPP3 | DPP3-DT | DPP4 | DPP6 | DPP7 | DPP8 | DPP9 | DPP9-AS1 | DPPA2 | DPPA2P3 | DPPA3 | DPPA3P1 | DPPA3P2 | DPPA4 | DPPA4P3 | DPPA5 | DPPA5P4 | DPRX | DPRXP2 | DPRXP4 | DPT | DPY19L1 | DPY19L1P1 | DPY19L2 | DPY19L2P1 | DPY19L2P2 | DPY19L2P3 | DPY19L2P4 | DPY19L3