Target Name: MASTL
NCBI ID: G84930
Review Report on MASTL Target / Biomarker Content of Review Report on MASTL Target / Biomarker
MASTL
Other Name(s): Microtubule-associated serine/threonine-protein kinase-like | microtubule associated serine/threonine kinase like | RP11-85G18.2 | Serine/threonine-protein kinase greatwall | GWL_HUMAN | Microtubule associated serine/threonine kinase like, transcript variant 2 | MAST-L | FLJ14813 | greatwall protein kinase | greatwall kinase homolog | GWL | hGWL | Serine/threonine-protein kinase greatwall (isoform 2) | MASTL variant 2 | GW | THC2 | GREATWALL

MASTL: A Potential Drug Target for Disordered Cell Signaling

MASTL (Microtubule-associated serine/threonine-protein kinase-like) is a protein that is expressed in various tissues and cells throughout the body. It is a key regulator of microtubules, which are dynamic cytoskeletal structures that play a crucial role in the proper functioning of cells. MASTL is a protein that is known to interact with and regulate the activity of other proteins, including the protein tau. This suggests that MASTL may be a drug target or biomarker for the development of various diseases, including neurodegenerative disorders.

The structure and function of MASTL are closely related to the protein tau. Both proteins are composed of a unique catalytic domain and a unique transmembrane region. The catalytic domain of both proteins consists of a single transmembrane alpha-helices that contains a catalytic site. This catalytic site is the site where the proteins interact with other proteins and substrates, allowing them to perform their unique functions.

One of the key functions of MASTL is its ability to regulate the activity of microtubules. Microtubules are dynamic cytoskeletal structures that play a critical role in the proper functioning of cells. They are composed of a series of protein filaments that are organized in a specific pattern to create a highly defined structure that is essential for the cell's growth, division, and transport of various molecules.

MASTL is a key regulator of microtubule dynamics. It is known to interact with and regulate the activity of the protein tau, which is also a key regulator of microtubules. Tau is a protein that is composed of a unique transmembrane region and a catalytic domain. The transmembrane region of tau is responsible for the protein's ability to interact with other proteins and substrates, allowing it to perform its unique functions.

The catalytic domain of MASTL is responsible for its ability to regulate the activity of microtubules. It contains a unique site that is specific for the protein tau. This site allows MASTL to interact with tau and to regulate its activity. This interaction between MASTL and tau is important for the proper functioning of microtubules.

In addition to its role in regulating microtubule dynamics, MASTL is also known to play a role in the regulation of cell signaling pathways. It is a key regulator of the protein kinase pathway, which is responsible for the regulation of various cellular processes. This suggests that MASTL may be a drug target or biomarker for the development of various diseases, including neurodegenerative disorders.

The role of MASTL in the regulation of cell signaling pathways is closely related to its function in regulating microtubule dynamics. Both processes are critical for the proper functioning of cells, and MASTL plays a key role in regulating both processes.

MASTL is also known to play a role in the regulation of cellular processes related to cell adhesion. It is a key regulator of the protein cadherin, which is responsible for the regulation of cell adhesion. This suggests that MASTL may be a drug target or biomarker for the development of diseases that are characterized by disrupted cell adhesion, such as cancer.

In conclusion, MASTL is a protein that is known to interact with and regulate the activity of other proteins, including the protein tau. This suggests that MASTL may be a drug target or biomarker for the development of various diseases. Its role in regulating microtubule dynamics , cell signaling pathways, and cellular processes related to cell adhesion suggests that it may be a valuable target for the development of new therapeutic approaches for a variety of diseases.

Protein Name: Microtubule Associated Serine/threonine Kinase Like

Functions: Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of ARPP19 and ENSA at 'Ser-62' and 'Ser-67', respectively. ARPP19 and ENSA are phosphatase inhibitors that specifically inhibit the PPP2R2D (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved in checkpoint recovery by being inhibited. Phosphorylates histone protein in vitro; however such activity is unsure in vivo. May be involved in megakaryocyte differentiation

The "MASTL 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 MASTL 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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