PRKCA
GeneName
PRKCA
Summary
PRKCA, also known as PKC, PKC alpha, or PRKACA, is a 77 kDa serine/threonine kinase that plays a vital role in various cellular processes. It is expressed in multiple tissues and localised to various cellular compartments including the cytoplasm, plasma membrane, endoplasmic reticulum, and mitochondria. PRKCA is involved in intracellular signal transduction and is activated by diacylglycerol and calcium. It participates in processes such as angiogenesis, cell adhesion, and apoptotic signalling, and has been implicated in the regulation of various signalling pathways, including those related to inflammation and cell migration.
Importance
PRKCA is relevant to: - Angiogenesis and vascular biology, influencing blood vessel formation and endothelial cell behaviour. - Neurobiology, particularly in central nervous system neuron axonogenesis and learning or memory processes. - Cancer research, due to its role in cell proliferation and survival signalling pathways. - Inflammatory responses, as it negatively regulates cytokine production and influences glial cell apoptosis.
Top Products
For researchers investigating PRKCA, we highly recommend the top-selling recombinant antibody, Anti-PKC alpha antibody [Y124] (ab32376). This antibody has been validated in knockout models, ensuring reliable performance in various applications, including Western blotting (WB), immunohistochemistry (IHC), immunocytochemistry (ICC), flow cytometry (FC), and immunoprecipitation (IP). With 150 citations, it is well-regarded in the research community, making it an excellent choice for those seeking dependable detection of PKC alpha.
Abcam Product Citation Summary
The use of Abcam antibodies targeting PRKCA in various studies highlights its role in significant biological processes such as cAMP accumulation, PKA localisation, and cell motility. The studies involve both human and pig cell lines, indicating the relevance of PRKCA in different species and contexts.
Abcam Product Citation Table
Function
Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, tumorigenesis, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascade involving MAPK1/3 (ERK1/2) and RAP1GAP. Involved in cell proliferation and cell growth arrest by positive and negative regulation of the cell cycle. Can promote cell growth by phosphorylating and activating RAF1, which mediates the activation of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A, which facilitates active cyclin-dependent kinase (CDK) complex formation in glioma cells. In intestinal cells stimulated by the phorbol ester PMA, can trigger a cell cycle arrest program which is associated with the accumulation of the hyper-phosphorylated growth-suppressive form of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B. Exhibits anti-apoptotic function in glioma cells and protects them from apoptosis by suppressing the p53/TP53-mediated activation of IGFBP3, and in leukemia cells mediates anti-apoptotic action by phosphorylating BCL2. During macrophage differentiation induced by macrophage colony-stimulating factor (CSF1), is translocated to the nucleus and is associated with macrophage development. After wounding, translocates from focal contacts to lamellipodia and participates in the modulation of desmosomal adhesion. Plays a role in cell motility by phosphorylating CSPG4, which induces association of CSPG4 with extensive lamellipodia at the cell periphery and polarization of the cell accompanied by increases in cell motility. During chemokine-induced CD4(+) T cell migration, phosphorylates CDC42-guanine exchange factor DOCK8 resulting in its dissociation from LRCH1 and the activation of GTPase CDC42 (PubMed:28028151). Is highly expressed in a number of cancer cells where it can act as a tumor promoter and is implicated in malignant phenotypes of several tumors such as gliomas and breast cancers. Negatively regulates myocardial contractility and positively regulates angiogenesis, platelet aggregation and thrombus formation in arteries. Mediates hypertrophic growth of neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-dependent signaling pathway, and upon PMA treatment, is required to induce cardiomyocyte hypertrophy up to heart failure and death, by increasing protein synthesis, protein-DNA ratio and cell surface area. Regulates cardiomyocyte function by phosphorylating cardiac troponin T (TNNT2/CTNT), which induces significant reduction in actomyosin ATPase activity, myofilament calcium sensitivity and myocardial contractility. In angiogenesis, is required for full endothelial cell migration, adhesion to vitronectin (VTN), and vascular endothelial growth factor A (VEGFA)-dependent regulation of kinase activation and vascular tube formation. Involved in the stabilization of VEGFA mRNA at post-transcriptional level and mediates VEGFA-induced cell proliferation. In the regulation of calcium-induced platelet aggregation, mediates signals from the CD36/GP4 receptor for granule release, and activates the integrin heterodimer ITGA2B-ITGB3 through the RAP1GAP pathway for adhesion. During response to lipopolysaccharides (LPS), may regulate selective LPS-induced macrophage functions involved in host defense and inflammation. But in some inflammatory responses, may negatively regulate NF-kappa-B-induced genes, through IL1A-dependent induction of NF-kappa-B inhibitor alpha (NFKBIA/IKBA). Upon stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and may be involved in the regulation of EIF4E phosphorylation. Phosphorylates KIT, leading to inhibition of KIT activity. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription. Phosphorylates SOCS2 at 'Ser-52' facilitating its ubiquitination and proteasomal degradation (By similarity). Phosphorylates KLHL3 in response to angiotensin II signaling, decreasing the interaction between KLHL3 and WNK4 (PubMed:25313067). Phosphorylates and activates LRRK1, which phosphorylates RAB proteins involved in intracellular trafficking (PubMed:36040231).
Post-translational modifications
In response to growth factors, phosphorylated at Thr-631 and Ser-657 by the mTORC2 complex, promoting autophosphorylation and activation of PRKCA.
Sequence Similarities
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.
Cellular localization
- Cytoplasm
- Cell membrane
- Peripheral membrane protein
- Mitochondrion membrane
- Peripheral membrane protein
- Nucleus
Alternative names
PKCA, PRKACA, PRKCA, Protein kinase C alpha type, PKC-A, PKC-alpha