PIAS2: A Zinc Finger MIZ-Type Containing G protein-Coupled Receptor with Potential as a Drug Target

Target Name: PIAS2

NCBI ID: G9063

PIAS2

PIAS2: A Zinc Finger MIZ-Type Containing G protein-Coupled Receptor with Potential as a Drug Target

Phosphatidylinositol (PI) and inositol (IN) are essential nutrients for cell signaling, and their levels have been linked to various physiological processes, including cell adhesion, migration, and signaling pathways. PIAS2, a zinc finger protein belonging to the MIZ (Mammalian Imprinted Zinc Finger) family, has been identified as a potential drug target or biomarker due to its unique structure and function. In this article, we will provide an overview of PIAS2, its function, and potential as a drug target.

Structure and Function

PIAS2 is a 21-kDa protein that contains a zinc finger and a N-terminal transmembrane domain (TMD). The N-terminal region of PIAS2 contains a unique farnesylated cysteine residue, which is important for its stability and localization to the endoplasmic reticulum (ER) and for its potential interaction with various signaling pathways. The zinc finger region consists of four conserved zinc finger motifs (ZNFs), which are involved in protein-protein interactions and are crucial for protein stability.

PIAS2 is a member of the MIZ family, which includes several other zinc finger proteins, including ZNF2, ZNF3, ZNF4, and ZNF5. These proteins share a similar structure and function, including the presence of a N-terminal TMD and a C-terminal ZNF-like domain. The MIZ family has been implicated in various signaling pathways, including cell growth, differentiation, and survival.

PIAS2 has been shown to play a crucial role in various physiological processes, including cell adhesion, migration, and signaling pathways. For example, PIAS2 has been shown to be involved in cell-cell adhesion, as it has been shown to interact with various adhesion molecules, including cadherins and integrins. Additionally, PIAS2 has been shown to be involved in cell migration, as it has been shown to regulate the migration of various cell types, including cancer cells.

In addition to its role in cell signaling, PIAS2 has also been shown to have potential as a drug target. The farnesylated cysteine residue in the N-terminal region of PIAS2 has been shown to be modifiable, and various studies have suggested that modifying this residue could potentially lead to the development of drug resistance. Additionally, the zinc finger region of PIAS2 has been shown to be involved in protein-protein interactions, and the interaction with other proteins could potentially lead to the modulation of various cellular processes.

Molecular Mechanisms

The molecular mechanisms underlying PIAS2 function are still being fully understood. However, several studies have provided insights into the molecular mechanisms that regulate PIAS2 function.

One of the main mechanisms by which PIAS2 is regulated is through its phosphorylation. Studies have shown that PIAS2 can be phosphorylated by various enzymes, including casein kinase (CK) 2. The phosphorylation of PIAS2 has been shown to modulate its stability and localization to the ER, as well as its interaction with various signaling pathways.

Another mechanism by which PIAS2 is regulated is through its stability. Studies have shown that PIAS2 can be stability modified by various factors, including reactive oxygen species (ROS). The stability modification of PIAS2 has been shown to play a crucial role in its regulation of cellular processes, including cell adhesion, migration, and signaling pathways.

Drug Treatment

Several studies have investigated the potential of drugs to target PIAS2, with a focus on modifying its farnesylated cysteine residue and its interaction with various signaling pathways.

One of the most promising drugs currently under investigation is eribulin, an inhibitor of PIAS2. Eribulin has been shown to modulate PIAS2 stability and localization to the ER, as well as its interaction with various signaling pathways.

Another drug that is being investigated is sunitinib, an inhibitor of the tyrosine kinase TKT. Studies have shown that sunitinib can modulate PIAS2 stability and localization to the ER, as well as its interaction with various signaling pathways.

Conclusion

PIAS2 is a unique zinc finger protein that has been shown to play a crucial role in various physiological processes, including cell adhesion, migration, and signaling pathways. Its function is regulated through various mechanisms, including phosphorylation, stability modification, and interaction with various signaling pathways. The potential of drugs to target PIAS2, particularly those that can modulate its farnesylated cysteine residue and its interaction with various signaling pathways, make it an attractive target for future research.

Protein Name: Protein Inhibitor Of Activated STAT 2

Functions: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulator in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing may vary depending upon the biological context and the PIAS2 isoform studied. However, it seems to be mostly involved in gene silencing. Binds to sumoylated ELK1 and enhances its transcriptional activity by preventing recruitment of HDAC2 by ELK1, thus reversing SUMO-mediated repression of ELK1 transactivation activity. Isoform PIAS2-beta, but not isoform PIAS2-alpha, promotes MDM2 sumoylation. Isoform PIAS2-alpha promotes PARK7 sumoylation. Isoform PIAS2-beta promotes NCOA2 sumoylation more efficiently than isoform PIAS2-alpha. Isoform PIAS2-alpha sumoylates PML at'Lys-65' and 'Lys-160'

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