JUP: A Protein Involved in Cell Signaling, Tissue Repair and Cancer Progression

Target Name: JUP

NCBI ID: G3728

Content of Review Report on JUP Target / Biomarker

JUP

JUP: A Protein Involved in Cell Signaling, Tissue Repair and Cancer Progression

JUP (Catenin, associated with cadherin) is a protein that is expressed in various tissues throughout the body, including epithelial, mesenchymal, and neural cells. Its primary function is to interact with cadherins, a transmembrane protein that plays a crucial role in cell- cell adhesion. JUP has been identified as a potential drug target or biomarker due to its unique structure and its involvement in several cellular processes, including cell signaling, tissue repair, and cancer progression.

JUP is a 120-kDa protein that consists of an N-terminus, a unique D/T-rich region, a middle T/C-rich region, and a C-terminus. The N-terminus of JUP contains a putative N- acyl transferase (NAT) domain, which is responsible for the transfer of negatively charged amino acids to the N-terminus of the protein. The D/T-rich region of JUP is composed of 21 amino acids, and it is known as the \"D arm\". The middle T/C-rich region of JUP is also rich in amino acids, and it is considered the \"core\" of the protein. The C-terminus of JUP contains a conserved glycine residue that is involved in the formation of a disulfide bond.

JUP has been shown to play a critical role in several cellular processes, including cell signaling, tissue repair, and cancer progression. In the context of cell signaling, JUP has been shown to be involved in several signaling pathways, including TGF-β, Wnt , and Hedgehog. For example, JUP has been shown to be a negative regulator of the TGF-β pathway, and it has been shown to interact with the transcription factor Smad. In the context of tissue repair, JUP has been shown to be involved in the regulation of cell proliferation, apoptosis, and angiogenesis. For example, JUP has been shown to be a negative regulator of the KLF gene, which encodes a nuclear factor that regulates cell proliferation. In the context of cancer progression, JUP has been shown to be involved in the regulation of cell migration, invasion, and metastasis. For example, JUP has been shown to be a positive regulator of the protein destimulating gene (10) , which encodes a protein that can inhibit the migration and invasion of cancer cells.

Due to its unique structure and its involvement in several cellular processes, JUP has been identified as a potential drug target or biomarker. Several studies have shown that JUP can be targeted by small molecules, including inhibitors of the NAT activity of JUP (11) and inhibitors of the N-acyl transferase domain of JUP. In addition, several studies have shown that JUP is involved in several diseases, including cancer, neurodegenerative diseases, and autoimmune diseases. Therefore, JUP is considered as a potential drug target or biomarker for the development of new therapeutic strategies for these diseases.

In conclusion, JUP is a 120-kDa protein that consists of an N-terminus, a unique D/T-rich region, a middle T/C-rich region, and a C-terminus. It has been shown to play a critical role in several cellular processes, including cell signaling, tissue repair, and cancer progression. Its unique structure and its involvement in several processes make JUP an attractive target for small molecules and therapeutic strategies. Further research is needed to fully understand the role of JUP in cellular processes and its potential as a drug target or biomarker.

Protein Name: Junction Plakoglobin

Functions: Common junctional plaque protein. The membrane-associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctions suggests that it plays a central role in the structure and function of submembranous plaques. Acts as a substrate for VE-PTP and is required by it to stimulate VE-cadherin function in endothelial cells. Can replace beta-catenin in E-cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton (By similarity)

The "JUP 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 JUP 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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