PAN3: A Potential Drug Target for Pancreatic Cancer (G255967)

Target Name: PAN3

NCBI ID: G255967

PAN3

PAN3: A Potential Drug Target for Pancreatic Cancer

Pancreatic cancer is a leading cause of cancer-related deaths worldwide, with a five-year survival rate of only 12%. Despite advances in treatment, the standard of care for pancreatic cancer remains limited. There is a need for new treatments and approaches that can improve outcomes for patients.

One potential drug target for pancreatic cancer is PAN3 (OTTHUMP00000018180), a protein that is expressed in various tissues and has been shown to be involved in pancreatic cancer development. In this article, we will discuss the potential implications of PAN3 as a drug target for pancreatic cancer.

PAN3: Expression and Functions

PAN3 is a protein that is expressed in various tissues, including pancreas, spleen, and lymph nodes. It is a member of the Tetraspan family, which includes proteins that are involved in the regulation of protein interactions and quality control. PAN3 is characterized by a unique N-terminal domain that consists of a long alpha-helices and a C-terminal domain that consists of a short alpha-helices and a C-terminal domain.

PAN3 functions as a negative regulator of the microtubule dynamics in pancreatic cancer cells. Microtubules are cytoskeletal structures that play a critical role in cell division, migration, and intracellular transport. PAN3 is shown to regulate the stability of microtubules by interacting with the protein T-tubulin. This interaction between PAN3 and T-tubulin has been shown to inhibit microtubule dynamics and disrupt the ability of cancer cells to divide and migrate.

PAN3 is also involved in the regulation of the actinin complex, which is a complex of actinin filaments that are involved in the regulation of cell shape and mechanical forces. The actinin complex is a critical component of the cytoskeleton and is involved in many cellular processes, including cell division, migration, and intracellular transport. PAN3 is shown to regulate the actinin complex by interacting with the protein Myosin. This interaction between PAN3 and Myosin has been shown to affect the stability of the actinin complex and disrupt its ability to regulate cell shape and mechanical forces.

PAN3 as a Drug Target

PAN3 is a potential drug target for pancreatic cancer because of its involvement in the regulation of microtubule dynamics and the actinin complex. Drugs that can inhibit PAN3 function have the potential to treat pancreatic cancer by disrupting the regulation of microtubule dynamics and the actinin complex.

One class of drugs that have been shown to inhibit PAN3 function is the taxanes. Taxanes are a class of drugs that are commonly used to treat breast and ovarian cancers, and have also been shown to be effective in treating pancreatic cancer. Taxanes work by inhibiting the activity of tubulin, which is a protein that is involved in the regulation of microtubule dynamics.

Several studies have shown that taxanes can inhibit the activity of PAN3 by binding to its N-terminus. This binding causes PAN3 to enter a state of hyperactivity, which can disrupt the regulation of microtubule dynamics and the actinin complex.

Another class of drugs that have been shown to inhibit PAN3 function are the PI3K inhibitors. PI3K (Phosphatidylinositol 3-kinase) is a protein that is involved in the regulation of cellular signaling pathways, including the regulation of microtubule dynamics and the actinin complex. PI3K inhibitors have been shown to inhibit the activity of PAN3 by binding to its C-terminus. This binding causes PAN3 to enter a state of hyperactivity, which can disrupt

Protein Name: Poly(A) Specific Ribonuclease Subunit PAN3

Functions: Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and PABP, and to miRNA targets via its interaction with GW182 family proteins

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•   the target screening and validation;
•   expression level;
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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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