tubulin polymerization promoting protein (TPPP): a potential drug target and biomarker

Target Name: TPPP

NCBI ID: G11076

TPPP

tubulin polymerization promoting protein (TPPP): a potential drug target and biomarker

Abstract:

Tubulin polymerization promoting protein (TPPP) is a protein that plays a crucial role in the regulation of microtubules, which are essential for the proper functioning of cells. The abnormal regulation of microtubules has been implicated in various diseases, including cancer, neurodegenerative diseases, and developmental disorders. Therefore, the discovery of TPPP as a potential drug target or biomarker has significant implications for the development of new therapeutic approaches.

Introduction:

Microtubules are dynamic cytoskeletal structures that play a central role in the regulation of various cellular processes, including cell division, intracellular transport, and cell signaling. They are composed of a protein called tubulin and a protein called microtubule-associated protein 2 (MAP2). The regulation of microtubule dynamics is critical for the proper functioning of cells, and alterations in microtubule dynamics have been implicated in various diseases, including cancer, neurodegenerative diseases, and developmental disorders.

TPPP is a protein that has been identified as a potential drug target and biomarker due to its involvement in the regulation of microtubule dynamics. It is composed of two subunits, TPPP1 and TPPP2, that share a common catalytic core and a N-terminus. TPPP1 and TPPP2 can form a heterotrimeric complex, which promotes the polymerization of tubulin monomers into microtubules.

Expression and function of TPPP:

TPPP is expressed in various tissues and cells, including muscle, brain, and cancer cells. It is involved in the regulation of microtubule dynamics and has been implicated in various cellular processes, including cell signaling, intracellular transport, and cell division.

TPPP has been shown to play a crucial role in the regulation of microtubule dynamics in various organisms. In Xenobiotics C (Xenobiotics) bacteria, TPPP was shown to regulate microtubule dynamics and was identified as a potential drug target. The introduction of TPPP into Xenobiotics C bacteria led to a significant reduction in cell growth and a delay in the onset of drug-tolerance.

In addition to its role in microtubule dynamics, TPPP has also been shown to play a role in the regulation of cell signaling. TPPP has been shown to interact with various signaling molecules, including T-cell kinases, G-protein-coupled receptors, and G-protein-coupled nucleotide binding proteins.

TPPP as a drug target:

TPPP has been identified as a potential drug target due to its involvement in the regulation of microtubule dynamics and its ability to interact with various signaling molecules. The development of compounds that can inhibit TPPP activity could be a useful therapeutic approach for the treatment of various diseases.

One of the challenges in developing compounds that inhibit TPPP activity is the lack of a clear understanding of its biology. The regulation of microtubule dynamics is complex and involves the interplay of multiple factors, including the regulation of protein synthesis, protein degradation, and protein- protein interactions. Therefore, it is difficult to design small molecules that specifically inhibit TPPP activity.

To overcome this challenge, researchers have used a variety of techniques to study the biology of TPPP. One approach is to use live cell imaging techniques, such as time-lapse imaging, to visualize the effects of TPPP on microtubule dynamics. This technique allows researchers to monitor the changes in microtubule density and can provide valuable information about the mechanisms of TPPP action.

Another approach is to use biochemical assays, such as protein-fragment complementation assays or biochemical assays, to study the interactions of TPPP with various signaling molecules. These assays can provide valuable information about the protein-protein interactions that are involved in TPPP function.

TPPP as a biomarker:

TPPP has also been identified as a potential biomarker for the diagnosis and

Protein Name: Tubulin Polymerization Promoting Protein

Functions: Regulator of microtubule dynamics that plays a key role in myelination by promoting elongation of the myelin sheath (PubMed:31522887). Acts as a microtubule nucleation factor in oligodendrocytes: specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, and promotes microtubule nucleation, an important step for elongation of the myelin sheath (PubMed:31522887, PubMed:33831707). Required for both uniform polarized growth of distal microtubules as well as directing the branching of proximal processes (PubMed:31522887). Shows magnesium-dependent GTPase activity; the role of the GTPase activity is unclear (PubMed:21995432, PubMed:21316364). In addition to microtubule nucleation activity, also involved in microtubule bundling and stabilization of existing microtubules, thereby maintaining the integrity of the microtubule network (PubMed:17105200, PubMed:17693641, PubMed:18028908, PubMed:26289831). Regulates microtubule dynamics by promoting tubulin acetylation: acts by inhibiting the tubulin deacetylase activity of HDAC6 (PubMed:20308065, PubMed:23093407). Also regulates cell migration: phosphorylation by ROCK1 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin and increased cell motility (PubMed:23093407). Plays a role in cell proliferation by regulating the G1/S-phase transition (PubMed:23355470). Involved in astral microtubule organization and mitotic spindle orientation during early stage of mitosis; this process is regulated by phosphorylation by LIMK2 (PubMed:22328514)

The "TPPP Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about TPPP comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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