PRKCQ: Key Regulator of Cell Adhesion, Migration and Inflammation

Target Name: PRKCQ

NCBI ID: G5588

PRKCQ

PRKCQ: Key Regulator of Cell Adhesion, Migration and Inflammation

PRKCQ, also known as PRKCQ variant 1, is a protein that is expressed in various tissues throughout the body. It is a member of the PRKCQ gene family, which is known for its role in cell signaling pathways. PRKCQ has been shown to play a role in the regulation of several cellular processes, including cell adhesion, migration, and inflammation.

One of the key functions of PRKCQ is its role in cell adhesion. PRKCQ is a critical regulator of tight junctions, which are a type of cell-cell adhesion that helps to maintain the integrity of tissues. tight junctions are composed of Transmembrane proteins that span the cell membrane and allow the exchange of nutrients, waste products, and other molecules between cells. They are also involved in the regulation of cell signaling pathways, including the TGF-β pathway.

In addition to its role in cell adhesion, PRKCQ is also involved in the regulation of cell migration. PRKCQ has been shown to play a role in the regulation of cell migration, which is the process by which cells move from one location to another in the body. This process is critical for the development and maintenance of tissues and organs, and is often regulated by signaling pathways that involve the signaling of genes.

PRKCQ is also involved in the regulation of inflammation. Inflammation is a critical response of the immune system to harmful stimuli, and it is often characterized by the production of pro-inflammatory cytokines. PRKCQ has been shown to play a role in the regulation of pro -inflammatory responses, and it is involved in the regulation of the production of these cytokines.

Another function of PRKCQ is its role in cell signaling pathways. PRKCQ is involved in the regulation of several signaling pathways, including the PI3K/Akt signaling pathway. This pathway is involved in the regulation of cellular processes that are important for the survival and growth of cells, including the regulation of cell survival, angiogenesis, and inflammation.

In addition to its role in cell signaling pathways, PRKCQ is also involved in the regulation of cellular processes that are important for the development and maintenance of tissues. PRKCQ is involved in the regulation of cell proliferation, which is the process by which cells grow and divide, and it is also involved in the regulation of cell differentiation.

PRKCQ is also involved in the regulation of cellular processes that are important for the regulation of cellular interactions. PRKCQ is involved in the regulation of cell-cell interactions, including the regulation of cell-cell adhesion, and it is also involved in the regulation of cell-extracellular matrix interactions.

In conclusion, PRKCQ is a protein that is involved in several critical cellular processes that are important for the development and maintenance of tissues. Its role in cell adhesion, migration, and inflammation, as well as its involvement in cell signaling pathways and cellular processes that are important for the development and maintenance of tissues make PRKCQ an attractive drug target and biomarker. Further studies are needed to fully understand the role of PRKCQ in these processes and to develop effective therapies that target this protein.

Protein Name: Protein Kinase C Theta

Functions: Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that mediates non-redundant functions in T-cell receptor (TCR) signaling, including T-cells activation, proliferation, differentiation and survival, by mediating activation of multiple transcription factors such as NF-kappa-B, JUN, NFATC1 and NFATC2. In TCR-CD3/CD28-co-stimulated T-cells, is required for the activation of NF-kappa-B and JUN, which in turn are essential for IL2 production, and participates in the calcium-dependent NFATC1 and NFATC2 transactivation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11 on several serine residues, inducing CARD11 association with lipid rafts and recruitment of the BCL10-MALT1 complex, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. May also play an indirect role in activation of the non-canonical NF-kappa-B (NFKB2) pathway. In the signaling pathway leading to JUN activation, acts by phosphorylating the mediator STK39/SPAK and may not act through MAP kinases signaling. Plays a critical role in TCR/CD28-induced NFATC1 and NFATC2 transactivation by participating in the regulation of reduced inositol 1,4,5-trisphosphate generation and intracellular calcium mobilization. After costimulation of T-cells through CD28 can phosphorylate CBLB and is required for the ubiquitination and subsequent degradation of CBLB, which is a prerequisite for the activation of TCR. During T-cells differentiation, plays an important role in the development of T-helper 2 (Th2) cells following immune and inflammatory responses, and, in the development of inflammatory autoimmune diseases, is necessary for the activation of IL17-producing Th17 cells. May play a minor role in Th1 response. Upon TCR stimulation, mediates T-cell protective survival signal by phosphorylating BAD, thus protecting T-cells from BAD-induced apoptosis, and by up-regulating BCL-X(L)/BCL2L1 levels through NF-kappa-B and JUN pathways. In platelets, regulates signal transduction downstream of the ITGA2B, CD36/GP4, F2R/PAR1 and F2RL3/PAR4 receptors, playing a positive role in 'outside-in' signaling and granule secretion signal transduction. May relay signals from the activated ITGA2B receptor by regulating the uncoupling of WASP and WIPF1, thereby permitting the regulation of actin filament nucleation and branching activity of the Arp2/3 complex. May mediate inhibitory effects of free fatty acids on insulin signaling by phosphorylating IRS1, which in turn blocks IRS1 tyrosine phosphorylation and downstream activation of the PI3K/AKT pathway. Phosphorylates MSN (moesin) in the presence of phosphatidylglycerol or phosphatidylinositol. Phosphorylates PDPK1 at 'Ser-504' and 'Ser-532' and negatively regulates its ability to phosphorylate PKB/AKT1. Phosphorylates CCDC88A/GIV and inhibits its guanine nucleotide exchange factor activity (PubMed:23509302)

The "PRKCQ Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about PRKCQ comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   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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