ERK phosphorylation is a cell signaling pathway involved in cell survival and apoptosis. Malfunction can lead to abnormal and cancerous cells. ERK regulates cell survival and death, and its activation requires double phosphorylation by Tys and Thr. Pharmaceutical companies target ERK proteins in cancer treatment and use an ERK test to measure GPCR activation.
In cell biology, extracellular signal-regulated kinase (ERK) phosphorylation refers to a signaling pathway composed of proteins and enzymes involved in cellular processes, namely cell survival and apoptosis. Phosphorylation of ERK is one of four mitogen-activated protein kinase (MAPK) signaling pathways. The ERK phosphorylation cascade is activated when a tyrosine (Tys) and/or threonine (Thr) kinase receptor molecule activates a protein kinase on the surface of a cell. When the ERK phosphorylation cycle malfunctions, inappropriate activation of ERK can occur and abnormal and cancerous cells can develop.
The fundamental role of ERK phosphorylation is cell survival; however, there is evidence for a death-promoting role under certain conditions in the cell. Evidence has shown that ERK regulates cell survival and cell death, or apoptosis, at various points along the signaling pathway. The exact mechanism of ERK-induced apoptosis can occur at different levels, both upstream and downstream of the phosphorylation cascade. Scientists have suggested a relationship between the cell death role of ERK and effects related to injury or stroke.
Defining ERK phosphorylation requires an explanation of the phosphorylation cascade, which involves a handful of highly specific enzymes and proteins. There are two ERK pathways: kinase-1 (ERK1) and kinase-2 (ERK2), also known as MAPK3 and MAPK1, respectively. The activation of ERK requires a double phosphorylation by Tys and Thr, starting with the phosphorylation of Tys. Phosphorylation involves the transfer of a phosphate molecule from an active protein kinase to an inactive protein kinase; an energy-providing adenosine triphosphate (ATP) molecule donates the phosphate molecule. Activation of one protein kinase results in the phosphorylation of each successive protein kinase along the pathway until one protein is activated and a cellular response is elicited.
Cells of different origins require different proteins and/or enzymes to drive the phosphorylation cascade. For every activating protein, there must be an inactivating protein. Activating and deactivating molecules essentially regulate the signaling cascade by binding to receptor sites until the appropriate cellular response is completed. Several proteins involved in the ERK phosphorylation cycle have been targeted in cancer treatment therapies because atypical activation of ERK has been shown to cause cancer.
In the pharmaceutical industry, therapeutic drugs have been developed to target specific protein receptors, namely G-coupled protein receptors (GCPR). G proteins (Ras, Rac, Rho, Cdc42, etc.) are involved in many physiological processes at the cellular level. Researchers developed an ERK test as a tool to measure GCPR activation. An ERK test like this enables ERK detection and provides clear and consistent results for drug developers.
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