MAPKAPK2 Kinase: Regulation of Cell Signaling and Tumorigenesis

Target Name: MAPKAPK2

NCBI ID: G9261

MAPKAPK2

MAPKAPK2 Kinase: Regulation of Cell Signaling and Tumorigenesis

MAPKAPK2, also known as MAPKAPK2 kinase 2, is a protein that is expressed in various tissues throughout the body. It is a member of the MAPKAPK2 family, which includes several related proteins that play important roles in cellular signaling pathways. One of the most well -studied of these proteins is the MAPKAPK2 kinase, which is involved in the regulation of various cellular processes, including cell growth, differentiation, and survival.

MAPKAPK2 kinase is a kinase involved in regulating many cellular processes, including cell growth, differentiation, and survival. Its function can be inhibited, leading to a variety of diseases, including neurodegenerative diseases, tumors, and metabolic disorders.

The activity of MAPKAPK2 kinase is closely related to its substrate specificity. The catalytic activity of MAPKAPK2 kinase is affected by multiple factors, including substrate structure, substrate concentration, and substrate exposure site. These factors can change the activity of MAPKAPK2 kinase, thereby affecting the intracellular signaling pathway.

The substrates of MAPKAPK2 kinase include a variety of proteins that perform different biological functions in cells. For example, MAPKAPK2 kinase can catalyze the binding of PDGF receptors to substrates, thereby promoting cell proliferation and survival. MAPKAPK2 kinase can also catalyze the phosphorylation of substrates such as P21 and FAK, thereby increasing the activity of the substrate and promoting intracellular signaling pathways.

The activity of MAPKAPK2 kinase can also be inhibited by a variety of drugs. For example, antihypertensive and anti-inflammatory drugs can inhibit the activity of MAPKAPK2 kinase, thereby reducing the effects of hypertension and inflammatory diseases. In addition, some studies have shown that inhibiting the activity of MAPKAPK2 kinase can treat certain cancers, such as lung and prostate cancer.

However, MAPKAPK2 kinase is also involved in the occurrence and development of various diseases. For example, MAPKAPK2 kinase activity can be increased by certain neurodegenerative diseases, such as Parkinson's disease and Alzheimer's disease. These diseases are often associated with overactivation of MAPKAPK2 kinase, which may lead to neuronal death and neurological tissue damage.

In addition, MAPKAPK2 kinase is also closely related to the occurrence and development of tumors. Studies have shown that the activity of MAPKAPK2 kinase can increase the growth and viability of tumor cells. In addition, MAPKAPK2 kinase can also promote the invasion and metastasis of tumor cells. These findings provide new ideas for tumor treatment.

In conclusion, MAPKAPK2 kinase plays an important role in cell signaling and tumorigenesis. Although it is closely related to the occurrence and development of many diseases, there are also some drugs that can inhibit its activity. Future research will continue to explore the biological functions of MAPKAPK2 kinase and develop new drugs to treat diseases related to this protein.

Protein Name: MAPK Activated Protein Kinase 2

Functions: Stress-activated serine/threonine-protein kinase involved in cytokine production, endocytosis, reorganization of the cytoskeleton, cell migration, cell cycle control, chromatin remodeling, DNA damage response and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. Phosphorylates ALOX5, CDC25B, CDC25C, CEP131, ELAVL1, HNRNPA0, HSP27/HSPB1, KRT18, KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Phosphorylates HSF1; leading to the interaction with HSP90 proteins and inhibiting HSF1 homotrimerization, DNA-binding and transactivation activities (PubMed:16278218). Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to the dissociation of HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impairment of their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins ELAVL1, HNRNPA0, PABPC1 and TTP/ZFP36, leading to the regulation of the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity, leading to inhibition of dependent degradation of ARE-containing transcripts. Phosphorylates CEP131 in response to cellular stress induced by ultraviolet irradiation which promotes binding of CEP131 to 14-3-3 proteins and inhibits formation of novel centriolar satellites (PubMed:26616734). Also involved in late G2/M checkpoint following DNA damage through a process of post-transcriptional mRNA stabilization: following DNA damage, relocalizes from nucleus to cytoplasm and phosphorylates HNRNPA0 and PARN, leading to stabilization of GADD45A mRNA. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3

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