TPX2 (DIL-2): A Potent Drug Target and Potential Biomarker for Various Diseases

Target Name: TPX2

NCBI ID: G22974

TPX2 (DIL-2): A Potent Drug Target and Potential Biomarker for Various Diseases

Introduction

TPX2 (double-stranded RNA-protein hybrid), also known as DIL-2, is a non-coding RNA molecule that plays a crucial role in various cellular processes, including cell growth, differentiation, and inflammation. TPX2 has been identified as a potential drug target and biomarker for several diseases, including cancer, neurodegenerative disorders, and autoimmune diseases.

Structure and Function

TPX2 is a 22-kDa RNA molecule that consists of two distinct regions: the first region is a double-stranded RNA, and the second region is a protein that is derived from the gene ZNF2. The double-stranded RNA region encodes a unique RNA structure that is highly conserved in various species, including humans. The protein region of TPX2 is a 191-kDa protein that contains four conserved cysteine 鈥嬧?媟esidues, which are involved in protein-protein interactions and other cellular processes.

TPX2 is a potent drug target because it can interact with multiple protein molecules, including the oncogene transforming growth factor-尾1 (TGF-β1) and the tumor suppressor protein, p53. TGF-β1 is a key mediator of cellular processes that promote cell growth , including the regulation of cell adhesion, differentiation, and survival. TPX2 has been shown to interact with TGF-β1 and has been proposed as a potential inhibitor of TGF-β1-mediated signaling pathways.

In addition to its potential impact on TGF-β1, TPX2 has also been shown to interact with several other proteins, including the transcription factor, NF-kappa-B. NF-kappa-B is a protein that plays a role in the regulation of inflammation, immune responses , and cell survival. TPX2 has been shown to interact with NF-kappa-B and has been proposed as a potential NF-kappa-B inhibitor.

TPX2 has also been shown to have a role in the regulation of cell apoptosis, which is the process by which cells die when they have reached their lifespan. Apoptosis is a natural process that helps the body eliminate damaged or dysfunctional cells. TPX2 has also been shown to play a role in the regulation of cell apoptosis by activating the B-cell apoptosis pathway.

In addition to its potential impact on cell apoptosis, TPX2 has also been shown to have a role in the regulation of cell signaling pathways, including the TGF-β1 signaling pathway. TPX2 has also been shown to regulate the translation of mRNAs in the TGF-β1 signaling pathway by binding to the RNA-protein interface of the TGF-β1 complex.

Drug Target Interactions

TPX2 has been shown to interact with multiple drug targets, including the oncogene transforming growth factor-尾1 (TGF-β1), the tumor suppressor protein, p53, the transcription factor, NF-kappa-B, and the B-cell apoptosis pathway. TPX2 has has been shown to inhibit the activity of TGF-β1 by binding to its RNA-protein interface, which results in the inhibition of TGF-β1-mediated signaling pathways.

TPX2 has also been shown to inhibit the activity of NF-kappa-B by binding to its nuclear localization domain. NF-kappa-B is a protein that plays a role in the regulation of inflammation, immune responses, and cell survival, and its activity is regulated by several factors, including the protein

Protein Name: TPX2 Microtubule Nucleation Factor

Functions: Spindle assembly factor required for normal assembly of mitotic spindles. Required for normal assembly of microtubules during apoptosis. Required for chromatin and/or kinetochore dependent microtubule nucleation. Mediates AURKA localization to spindle microtubules (PubMed:18663142, PubMed:19208764). Activates AURKA by promoting its autophosphorylation at 'Thr-288' and protects this residue against dephosphorylation (PubMed:18663142, PubMed:19208764). TPX2 is inactivated upon binding to importin-alpha (PubMed:26165940). At the onset of mitosis, GOLGA2 interacts with importin-alpha, liberating TPX2 from importin-alpha, allowing TPX2 to activates AURKA kinase and stimulates local microtubule nucleation (PubMed:26165940)

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