TPR: A Potential Drug Target and Biomarker for Nuclear Pore Complex-Associated Protein

Target Name: TPR

NCBI ID: G7175

TPR: A Potential Drug Target and Biomarker for Nuclear Pore Complex-Associated Protein

Nuclear pore complex (NPC) is a protein complex that plays a critical role in the regulation of nuclear traffic, including the transport of proteins involved in various cellular processes. One of the proteins associated with the NPC is TPR (TPr, TP73), a nuclear-resident protein that is expressed in various cell types. TPR has been shown to play a key role in regulating nuclear pore complex stability and has been implicated in various cellular processes, including DNA replication, gene expression, and stress responses.

Despite the importance of TPR in cellular processes, its role in the regulation of nuclear traffic is not well understood. Although TPR has been shown to interact with various nuclear proteins, including the transcription factor TFp1, the precise mechanisms by which TPR regulates nuclear traffic are not clear.

Targeting TPR: A Potential Approach

The identification of potential drug targets and biomarkers for TPR has significant implications for the development of new therapeutic strategies. One approach to targeting TPR is to use small molecules that can modulate its activity. One such approach is the use of inhibitors of the protein synthesis pathway, which would reduce the amount of TPR available for its various cellular functions.

One potential inhibitor of protein synthesis is the drug tirapiravir, which is currently being investigated as a potential treatment for various human diseases, including HIV-1 infection and cancer. Tirapiravir works by inhibiting the activity of the protein synthesis enzyme fMet, which is essential for protein synthesis. By inhibiting fMet activity, Tirapiravir can reduce the amount of protein available for various cellular functions, including the regulation of nuclear traffic.

Another potential inhibitor of protein synthesis is the drug curacilin, which is a small molecule that has been shown to inhibit the activity of the protein synthesis enzyme tryptophan synthase. Curacilin works by binding to the active site of tryptophan synthase and inhibiting its activity. This inhibition of protein synthesis can also affect the regulation of nuclear traffic, as the synthesis of certain proteins involved in nuclear traffic is dependent on the activity of tryptophan synthase.

Another approach to targeting TPR is to use antibodies that can specifically recognize and label TPR, in order to study its localization and stability in the nucleoplasm. One such approach is the use of an anti-TPR monoclonal antibody, which can be used to study the distribution of TPR in the nucleoplasm and its stability under various cellular conditions.

Conclusion

In conclusion, TPR is a protein that plays a critical role in the regulation of nuclear traffic and has been implicated in various cellular processes. While the precise mechanisms by which TPR regulates nuclear traffic are not well understood, the identification of potential drug targets and biomarkers for TPR has significant implications for the development of new therapeutic strategies. The use of small molecules and antibodies that can modulate TPR activity could lead to new insights into the regulation of nuclear traffic and the development of new treatments for various diseases.

Protein Name: Translocated Promoter Region, Nuclear Basket Protein

Functions: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase, and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with NUP153, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Negatively regulates both the association of CTE-containing mRNA with large polyribosomes and translation initiation. Does not play any role in Rev response element (RRE)-mediated export of unspliced mRNAs. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters; associates both with chromatin in the HSP70 promoter and with mRNAs transcribed from this promoter under stress-induced conditions. Modulates the nucleocytoplasmic transport of activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the XPO1/CRM1-mediated nuclear export complex. According to some authors, plays a limited role in the regulation of nuclear protein export (PubMed:22253824, PubMed:11952838). Also plays a role as a structural and functional element of the perinuclear chromatin distribution; involved in the formation and/or maintenance of NPC-associated perinuclear heterochromatin exclusion zones (HEZs). Finally, acts as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression. Its N-terminus is involved in activation of oncogenic kinases

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