Unlocking the Potential of MAGI2: A Drug Target and Biomarker for Membrane-Associated Guanylate Kinase Inverted 2

Target Name: MAGI2

NCBI ID: G9863

MAGI2

Unlocking the Potential of MAGI2: A Drug Target and Biomarker for Membrane-Associated Guanylate Kinase Inverted 2

Guanylate kinase (GK) is a family of enzymes that play a crucial role in various cellular processes, including signaling, intracellular signaling, and cell survival. The Membrane-Associated Guanylate Kinase Inverted 2 (MAGI2) is a GK enzyme that has been identified as a potential drug target and biomarker. In this article, we will explore the structure and function of MAGI2, its potential as a drug target, and its potential as a biomarker for various diseases.

Structure and Function

MAGI2 is a 21-kDa protein that is expressed in various tissues, including brain, heart, liver, and pancreas. It is localized to the endoplasmic reticulum (ER) and has been shown to be involved in the regulation of intracellular signaling pathways, including the cAMP/cGMP signaling pathway, the sonic hedgehog pathway, and the TGF-β pathway.

MAGI2 is a GK enzyme that is characterized by its catalytic activity and its ability to induce protein-protein interactions. The catalytic active site of MAGI2 is located at the N-terminus and consists of a catalytic core and a regulatory loop. The catalytic core consists of a catalytic loop and a hyperbolic loop, while the regulatory loop consists of a series of conserved amino acids that form a binding site for the regulatory protein.

MAGI2 has been shown to play a role in the regulation of intracellular signaling pathways, including the cAMP/cGMP signaling pathway, the sonic hedgehog pathway, and the TGF-β pathway. For instance, MAGI2 has been shown to regulate the activity of the cAMP/cGMP signaling pathway in smooth muscle cells, which is involved in the regulation of muscle contractions and blood pressure.

In addition to its role in intracellular signaling pathways, MAGI2 has also been shown to play a role in the regulation of cell survival. For instance, MAGI2 has been shown to play a role in the regulation of cell apoptosis, which is a critical mechanism that regulates cell death and homeostasis.

Potential Drug Target

MAGI2 has been identified as a potential drug target due to its unique structure and function. The catalytic activity of MAGI2 and its ability to induce protein-protein interactions make it an attractive target for small molecules. In addition, MAGI2 has been shown to play a role in the regulation of intracellular signaling pathways, making it an attractive target for drugs that can modulate these pathways.

MAGI2 has been shown to be involved in the regulation of the cAMP/cGMP signaling pathway, which is involved in the regulation of muscle contractions and blood pressure. Therefore, drugs that can modulate this pathway, such as dihydroorotropic factor (DHF), a protein that can activate MAGI2, may be useful in treating cardiovascular diseases.

In addition to its role in the cAMP/cGMP signaling pathway, MAGI2 has also been shown to play a role in the regulation of cell apoptosis. Therefore, drugs that can induce cell apoptosis in MAGI2-mediated signaling pathways may be useful in treating diseases that are characterized by uncontrolled cell growth, such as cancer.

Potential Biomarker

MAGI2 has been shown to have potential as a biomarker for various diseases. For instance, MAGI2 has been shown to be involved in the regulation of the cAMP/cGMP signaling pathway, which is involved in the regulation of inflammation. Therefore, drugs that

Protein Name: Membrane Associated Guanylate Kinase, WW And PDZ Domain Containing 2

Functions: Seems to act as a scaffold molecule at synaptic junctions by assembling neurotransmitter receptors and cell adhesion proteins (By similarity). Plays a role in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and neurite outgrowth (By similarity). May play a role in regulating activin-mediated signaling in neuronal cells (By similarity). Enhances the ability of PTEN to suppress AKT1 activation (PubMed:10760291). Plays a role in receptor-mediated clathrin-dependent endocytosis which is required for ciliogenesis (By similarity)

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•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   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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