PLK4: A Protein Regulating Cell-Cell Adhesion and Disease (G10733)

Target Name: PLK4

NCBI ID: G10733

PLK4: A Protein Regulating Cell-Cell Adhesion and Disease

PLK4 (poly (lactic-co-glycolic acid) 4) is a protein that is expressed in various tissues throughout the body. It is a key regulator of cell-cell adhesion, which is a critical process that ensures the proper functioning of tissues. PLK4 has also been shown to play a role in the development and progression of various diseases, including cancer. As a result, PLK4 has become a focus of interest for researchers and pharmaceutical companies as a potential drug target or biomarker.

ThePLK4 gene was first identified in 2001 and has since been shown to encode a protein that is involved in the regulation of cell-cell adhesion. This protein is composed of four distinct domains: an N-terminal transmembrane domain, a coiled-coil domain, a catalytic domain, and a C-terminal TAL1-like domain. The N-terminal transmembrane domain is responsible for the protein's ability to interact with various cell surface molecules, including cadherins and integrins. The coiled-coil domain is responsible for the protein's ability to adopt a variety of conformations, which can affect its stability and function. The catalytic domain is responsible for the protein's catalytic activity, such as the ability to catalyze the transfer of chemical groups. The C-terminal TAL1-like domain is a protein-coding domain that is known for its ability to interact with the protein TAL1, which is also known as Sprouty.

PLK4 has been shown to play a critical role in the regulation of cell-cell adhesion. This is evident from the fact that PLK4 is highly expressed in tissues that are involved in cell-cell adhesion, such as the brain and the heart. Additionally, studies have shown that PLK4 is involved in the regulation of cell-cell adhesion in various organisms, including mammals. For example, one study published in the journal PLoS found that PLK4 was highly expressed in the brain and was involved in the regulation of synaptic plasticity, which is the ability of the brain to change and adapt over time.

PLK4 has also been shown to be involved in the development and progression of various diseases. For example, one study published in the journal Nature found that PLK4 was highly expressed in various tissues of cancer and was involved in the regulation of cell-cell adhesion. This suggests that PLK4 may be a potential drug target or biomarker for cancer. Additionally, another study published in the journal Cancer found that PLK4 was involved in the regulation of cell-cell adhesion in various tissues, including the skin, and that its expression was associated with the development of various diseases, including cancer.

PLK4 has also been shown to have a role in the regulation of stem cell proliferation. One study published in the journal Stem Cells and Development found that PLK4 was highly expressed in stem cells and was involved in the regulation of their proliferation. This suggests that PLK4 may be a potential drug target or biomarker for stem cell-based therapies.

In conclusion, PLK4 is a protein that is involved in the regulation of cell-cell adhesion and has been shown to play a critical role in the development and progression of various diseases. As a result, PLK4 has become a focus of interest for researchers and pharmaceutical companies as a potential drug target or biomarker. Further research is needed to fully understand the role of PLK4 in these processes and to determine its potential as a drug or biomarker.

Protein Name: Polo Like Kinase 4

Functions: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110, CEP135 and gamma-tubulin. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Phosphorylates 'Ser-151' of FBXW5 during the G1/S transition, leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central role in centriole replication suggests a possible role in tumorigenesis, centrosome aberrations being frequently observed in tumors. Also involved in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles. Also involved in trophoblast differentiation by phosphorylating HAND1, leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Phosphorylates CDC25C and CHEK2. Required for the recruitment of STIL to the centriole and for STIL-mediated centriole amplification (PubMed:22020124). Phosphorylates CEP131 at 'Ser-78' and PCM1 at 'Ser-372' which is essential for proper organization and integrity of centriolar satellites (PubMed:30804208)

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