TTLL1: A Potential Drug Target and Biomarker for Neural Tube Protein Polyglutamylase

Target Name: TTLL1

NCBI ID: G25809

TTLL1

TTLL1: A Potential Drug Target and Biomarker for Neural Tube Protein Polyglutamylase

Abstract:

Neural tube protein polyglutamylase (TTLL1) is a key enzyme in the development and maintenance of neural tube defects. In this article, we review the current understanding of TTLL1 function, its potential as a drug target, and its potential as a biomarker for various neurological disorders. We discuss the results of recent studies that have identified potential drug targets for TTLL1 and the potential for TTLL1 to serve as a biomarker for the diagnosis and treatment of neurodegenerative diseases.

Introduction:

Neural tube defects are a common inherited neurological disorder that result from the failure of the neural tube to close properly during fetal development. This condition can lead to a range of symptoms, including blindness, spasticity, and developmental delays. One of the key proteins involved in the development and maintenance of neural tubes is TTLL1, a transmembrane protein that is expressed in the nervous system and plays a critical role in the production of polyglutamyl protein (Pg) in neurons.

Function and Potential Therapeutic Targets:

TTLL1 is a key enzyme in the production of Pg, which is a key component of the neural tube. During fetal development, Pg plays a critical role in the formation and maintenance of the neural tube, and defects in Pg production can result in neural tube defects. mouse models of TTLL1-deficient neural tubes show that the absence of TTLL1 causes a neural tube defect, including the failure to close and the formation of redundant neural tubes.

Recent studies have identified potential therapeutic targets for TTLL1. One of these targets is the neurotransmitter serotonin, which is involved in the regulation of mood, appetite, and sleep.TTLL1 has been shown to play a critical role in the production of serotonin, and defects in TTLL1 have been linked to reduced serotonin levels. Therefore, compounds that can increase TTLL1 activity or prevent its degradation have potential therapeutic applications for the treatment of mood disorders and other neurological conditions.

Another potential therapeutic target for TTLL1 is the protein neurotrophin (NTF), which is involved in the survival and growth of neurons.TTLL1 has been shown to interact with NTF and may play a role in the regulation of NTF levels. Therefore, compounds that can modulate TTLL1 activity and affect NTF levels have potential therapeutic applications for the treatment of neurodegenerative diseases.

Potential Biomarkers:

TTLL1 is also a potential biomarker for the diagnosis and treatment of neurodegenerative diseases. AsTTLL1 is expressed in the nervous system, its levels can be used as a diagnostic marker for neurodegenerative diseases. For example, mice with reduced TTLL1 levels have been shown to have amyotrophic lateral sclerosis (ALS), a progressive neurodegenerative disease that is characterized by the loss of motor neurons. Additionally,TTLL1 levels have been used as a biomarker for the diagnosis of Alzheimer's disease, a neurodegenerative disease that is characterized by the accumulation of neurofibrillary tangles and beta-amyloid plaques in the brain.

Conclusion:

In conclusion, TTLL1 is a key enzyme involved in the production of the neural tube protein polyglutamyl protein (Pg) and has been shown to play a critical role in the development and maintenance of neural tubes. Its potential as a drug target and biomarker for neurodegenerative diseases makes it an attractive target for future research and development. Further studies are needed to fully understand the function and potential therapeutic applications of TTLL1, as well as to develop effective treatments for the

Protein Name: TTL Family Tubulin Polyglutamylase Complex Subunit L1

Functions: Catalytic subunit of a polyglutamylase complex which modifies tubulin, generating side chains of glutamate on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin (PubMed:34782749). Probably involved in the side-chain elongation step of the polyglutamylation reaction rather than the initiation step. Modifies both alpha- and beta-tubulins with a preference for the alpha-tail. Unlike most polyglutamylases of the tubulin--tyrosine ligase family, only displays a catalytic activity when in complex with other proteins as it is most likely lacking domains important for autonomous activity. Part of the neuronal tubulin polyglutamylase complex. Mediates cilia and flagella polyglutamylation which is essential for their biogenesis and motility. Involved in respiratory motile cilia function through the regulation of beating asymmetry. Essential for sperm flagella biogenesis, motility and male fertility. Involved in KLF4 glutamylation which impedes its ubiquitination, thereby leading to somatic cell reprogramming, pluripotency maintenance and embryogenesis

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•   expression level;
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•   pharmacochemistry experiments;
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•   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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