PRKACA: A Protein Targeted for Therapeutic Intervention (G5566)

Target Name: PRKACA

NCBI ID: G5566

PRKACA

PRKACA: A Protein Targeted for Therapeutic Intervention

PRKACA (PR interleukin-1 receptor kinase-activating protein) is a protein that is expressed in various tissues throughout the body, including the lungs, heart, kidneys, and intestines. It is a key regulator of cell signaling pathways that play a role in the development and maintenance of tissues and organs.

PRKACA is a protein that is known to be involved in the regulation of several different signaling pathways, including the TGF-β pathway and the NF-kappa-B pathway. The TGF-β pathway is a well-established pathway that is involved in the regulation of cell growth, differentiation, and survival, while the NF-kappa-B pathway is involved in the regulation of inflammation and inflammation-related processes.

Recent studies have identified PRKACA as a potential drug target for several different diseases, including cancer, fibrosis, and autoimmune disorders. PRKACA has also been shown to be involved in the regulation of several different biological processes that are relevant to a wide range of diseases, including inflammation, fibrosis, and aging.

One of the key benefits of PRKACA as a drug target is its widespread expression in a variety of tissues and organs, which makes it an attractive target for therapeutic intervention. PRKACA is also known to be involved in the regulation of several different signaling pathways, which makes it a potentially versatile target for therapeutic intervention.

In addition to its potential as a drug target, PRKACA is also a potential biomarker for several different diseases. The TGF-β pathway is involved in the regulation of cell growth and differentiation, and changes in TGF-β signaling have been associated with a wide range of diseases, including cancer, fibrosis, and autoimmune disorders. Similarly, the NF-kappa-B pathway is involved in the regulation of inflammation and inflammation-related processes, and changes in NF-kappa-B signaling have been associated with a wide range of diseases, including cancer, fibrosis, and autoimmune disorders.

Recent studies have shown that PRKACA is involved in the regulation of several different biological processes that are relevant to a wide range of diseases, including inflammation, fibrosis, and aging. For example, PRKACA has been shown to be involved in the regulation of inflammation, as demonstrated by studies that have shown that PRKACA is involved in the production of pro-inflammatory cytokines.

In addition to its potential as a drug target and biomarker, PRKACA is also of interest as a potential therapeutic intervention for a wide range of diseases. PRKACA has been shown to play a role in the regulation of several different signaling pathways that are involved in the development and maintenance of tissues and organs, and therapeutic intervention that targets these signaling pathways may be effective in treating a wide range of diseases.

In conclusion, PRKACA is a protein that is known to be involved in the regulation of several different signaling pathways that play a role in the development and maintenance of tissues and organs. Its widespread expression in a variety of tissues and organs makes it an attractive target for therapeutic intervention, and its potential as a drug target and biomarker make it an important area of research for the development of new treatments for a wide range of diseases. Further studies are needed to fully understand the role of PRKACA in the regulation of cell signaling pathways and its potential as a therapeutic intervention.

Protein Name: Protein Kinase CAMP-activated Catalytic Subunit Alpha

Functions: Phosphorylates a large number of substrates in the cytoplasm and the nucleus (PubMed:15642694, PubMed:15905176, PubMed:16387847, PubMed:17333334, PubMed:17565987, PubMed:17693412, PubMed:18836454, PubMed:19949837, PubMed:20356841, PubMed:21085490, PubMed:21514275, PubMed:21812984). Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA, SOX9 and VASP (PubMed:15642694, PubMed:15905176, PubMed:16387847, PubMed:17333334, PubMed:17565987, PubMed:17693412, PubMed:18836454, PubMed:19949837, PubMed:20356841, PubMed:21085490, PubMed:21514275, PubMed:21812984). Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis (PubMed:21423175). RORA is activated by phosphorylation (PubMed:21514275). Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts (PubMed:19949837). Involved in chondrogenesis by mediating phosphorylation of SOX9 (By similarity). Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP (PubMed:15642694, PubMed:20356841). Prevents the antiproliferative and anti-invasive effects of alpha-difluoromethylornithine in breast cancer cells when activated (PubMed:17333334). RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca(2+), leading to reduced amplitude and increased frequency of store overload-induced Ca(2+) release (SOICR) characterized by an increased rate of Ca(2+) release and propagation velocity of spontaneous Ca(2+) waves, despite reduced wave amplitude and resting cytosolic Ca(2+) (PubMed:17693412). PSMC5/RPT6 activation by phosphorylation stimulates proteasome (PubMed:17565987). Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation (PubMed:15905176). NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding (PubMed:15642694). Required for phosphorylation of GLI transcription factors which inhibits them and prevents transcriptional activation of Hedgehog signaling pathway target genes (By similarity). GLI transcription factor phosphorylation is inhibited by interaction of PRKACA with SMO which sequesters PRKACA at the cell membrane (By similarity). Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis most probably through the regulation of OFD1 in ciliogenesis (PubMed:33934390). Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation (By similarity). May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT) (By similarity). Phosphorylates APOBEC3G and AICDA (PubMed:16387847, PubMed:18836454). Phosphorylates HSF1; this phosphorylation promotes HSF1 nuclear localization and transcriptional activity upon heat shock (PubMed:21085490)

The "PRKACA 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 PRKACA 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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