JMY: A Protein That Regulates TGF-? and Cell Signaling (G133746)

Target Name: JMY

NCBI ID: G133746

Content of Review Report on JMY Target / Biomarker

JMY

JMY: A Protein That Regulates TGF-? and Cell Signaling

JMY, or Junction-mediating and -regulatory protein, is a protein that plays a crucial role in various cellular processes. It is a transmembrane protein that is expressed in various tissues and cells throughout the body. It is involved in many different cellular processes, including cell signaling, cell adhesion, and cell survival.

One of the key functions of JMY is its role as a negative regulator of the TGF-β pathway. The TGF-β pathway is a well-known signaling pathway that is involved in many different cellular processes, including cell growth, differentiation, and survival. This pathway is activated by the presence of TGF-β signaling proteins, which include TGF-β1, TGF-β2, and TGF-β3.

JMY is involved in the regulation of TGF-β pathway by blocking the activity of the TGF-β1 receptor, which is a protein that plays a key role in the TGF-β pathway. The TGF-β1 receptor is a transmembrane protein that is involved in cell signaling and growth. It is expressed in various tissues and cells throughout the body, including the brain, heart, and liver.

JMY is also involved in the regulation of TGF-β pathway by blocking the activity of the TGF-β2 receptor, which is a protein that is also involved in the TGF-β pathway. The TGF-β2 receptor is a transmembrane protein that is expressed in various tissues and cells throughout the body, including the skin, heart, and liver.

In addition to its role as a negative regulator of the TGF-β pathway, JMY is also involved in the regulation of cell signaling and cell adhesion. It is a member of the JNK signaling pathway, which is a well-known signaling pathway that is involved in cellular stress and survival. JMY is involved in the regulation of this pathway by activating the activity of the JNK signaling pathway, which is a protein that is involved in the regulation of cellular stress and survival.

JMY is also involved in the regulation of cell signaling and cell adhesion by blocking the activity of the PDGFR signaling pathway. The PDGFR signaling pathway is a well-known signaling pathway that is involved in cell signaling and growth. It is expressed in various tissues and cells throughout the body, including the brain, heart, and liver.

In addition to its role in cell signaling and cell adhesion, JMY is also involved in the regulation of cell survival. It is a member of the NF-kappa-B signaling pathway, which is a well-known signaling pathway that is involved in cellular stress and survival. JMY is involved in the regulation of this pathway by activating the activity of the NF-kappa-B signaling pathway, which is a protein that is involved in the regulation of cellular stress and survival.

JMY is also involved in the regulation of cell survival by blocking the activity of the AP-1 signaling pathway. The AP-1 signaling pathway is a well-known signaling pathway that is involved in cellular growth and differentiation. It is expressed in various tissues and cells throughout the body, including the brain, heart and liver.

Given its involvement in so many different cellular processes, JMY is a potential drug target and biomarker. Many studies have investigated the role of JMY in various cellular processes, including its role as a negative regulator of the TGF-β pathway and its involvement in cell signaling, cell adhesion, and cell survival.

In conclusion, JMY, or Junction-mediating and -regulatory protein, is a protein that plays a crucial role in various cellular processes. It is a transmembrane protein that is involved in cell signaling, cell adhesion, and cell survival. JMY is also involved in the regulation of the TGF-β pathway by blocking the activity of the TGF-β1 receptor, the TGF-β2 receptor and the PDGFR signaling pathway. It is also involved in the regulation of cell signaling and cell adhesion by blocking the activity of the

Protein Name: Junction Mediating And Regulatory Protein, P53 Cofactor

Functions: Acts both as a nuclear p53/TP53-cofactor and a cytoplasmic regulator of actin dynamics depending on conditions (PubMed:30420355). In nucleus, acts as a cofactor that increases p53/TP53 response via its interaction with p300/EP300. Increases p53/TP53-dependent transcription and apoptosis, suggesting an important role in p53/TP53 stress response such as DNA damage. In cytoplasm, acts as a nucleation-promoting factor for both branched and unbranched actin filaments (PubMed:30420355). Activates the Arp2/3 complex to induce branched actin filament networks. Also catalyzes actin polymerization in the absence of Arp2/3, creating unbranched filaments (PubMed:30420355). Contributes to cell motility by controlling actin dynamics. May promote the rapid formation of a branched actin network by first nucleating new mother filaments and then activating Arp2/3 to branch off these filaments. Upon nutrient stress, directly recruited by MAP1LC3B to the phagophore membrane surfaces to promote actin assembly during autophagy (PubMed:30420355). The p53/TP53-cofactor and actin activator activities are regulated via its subcellular location (By similarity)

The "JMY 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 JMY 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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