Introduction
Introduction
ERK protein kinase was isolated and identified in the early 1990s as a signal transduction protein that transmits mitogen signals. It is often found in the cytosol and is rapidly translocated into the nucleus of the cell when it is activated by mitogens such as various growth factors. The phosphoric acid ERK1/2 acts on transcription factors such as c-Jun, NF-AT, and NF-κB to exert biological effects. ERK is the first MAPK member to be discovered. It is the most widely studied and plays an important role in the development of tumors. The ERK-associated intracellular signaling pathway is thought to be the classical MAPK pathway, an important part of a series of kinase enzymatic cascades that transduce extracellular stimuli from the cell membrane into the nucleus.
ERK family
ERK is a silk/threonine protein kinase belonging to the members of Mitogen-Activated Protein Kinases (MAPKs). ERK is an important transduction protein that transmits mitogen signals in the body and is expressed in most cells. The current study found that ERK includes several subfamilies of ERK1/ERK2, ERK3/ERK4, and ERK5. Among them, ERK1/ERK2 is the earliest cloned member of the MAPKs family, collectively referred to as ERK1/2, with relative molecular masses of 42 kd and 44 kd, respectively. ERK1/2 is primarily activated by mitogen stimuli and subsequently leads to activation of a range of transcription factors that ultimately regulate cell proliferation and differentiation. ERK1/2 has up to 90% homology and is a proline-directed serine/threonine kinase. Like other MAPKs family kinases, activation of ERK1/2 requires the phosphorylation of serine (Y) and threonine (T) sites to be active.
The RAS/RAF/MEK/ERK pathway is the most mature in the MAPK pathway and plays an important role in the cell signaling regulatory network. ERK is an important member of this pathway, and the activation process of the ERK cascade has been confirmed. Under external stimulation, Ras protein is activated by cell membrane enrichment, Raf protein is activated by Ras phosphorylation, and then its C-terminal catalytic domain binds to MAPK kinase (MEK), further phosphorylating and activating MEK1/2. MEK1/2 has dual specificity and is activated by phosphorylation of two regulatory sites of threonine and tyrosine at the active site of ERK protein. Activated ERK transfers to the nucleus and phosphorylates transcription factors (CREB), cytoskeleton-associated protein (CAP), and enzymes (RSK) to regulate related gene expression. In addition, it is involved in various physiological processes such as cell growth, development, division, migration, metabolism, and apoptosis.
Figure 1. The RAS/RAF/MEK/MAPK pathways
ERK includes two subtypes with up to 90% homology: ERK1 and ERK2. Although the two subtype sequences are similar, they all have their own independent functions, and ERK2 can well compensate for the functional defects of ERK1. For example, mice that are knocked out ERK2 cause embryo death. Like many kinases, ERK contains a long chain of polypeptides whose N-terminus and C-terminus are mutually curled to form a typical bilobal structure. When MEK activates ERK, phosphorylation of its N-terminal Thr183 and Tyr185 sites results in a conformational change near the N-terminus and ATP-binding site. This effect is transmitted to the C-terminus such that the C-terminal active site binds to the substrate protein to phosphorylate its serine/threonine residue. The special property of ERK diphosphorylation is determined by a cyclic structure called Loop 12 in its molecule. The ring is located on the surface of the molecule and adjacent to the active site, some of which form a lip-like structure called the "phosphorylated lip." This region is considered to be a key structure that determines the activity of ERK protein kinases.
In neuronal apoptosis, the ERK pathway has a dual role. Although most studies have demonstrated that the ERK pathway has an anti-apoptotic effect in neurons, ERK signaling-induced pro-apoptotic effects have also been observed. The different effects of the ERK pathway may result from the different types of neurons, stimuli, interactions with other MAPK pathways used in these studies, and factors that may not be known.
Return to Signaling Pathway
Research Areas Related Targets Featured Products
Cancer ERK CAL-101 (GS-1101)
Infection PI3K TG100-115
Alzheimer's disease MEK GDC0941
Neurological Disease Akt XL147
Cancer Immunotherapy NF-κB Duvelisib
Inflammation/Immunology Ras Quercetin
Cardiovascular and blood system Raf Copanlisib
Endocrinology and Metabolic Disease mTOR TIC-10
ERK protein kinase was isolated and identified in the early 1990s as a signal transduction protein that transmits mitogen signals. It is often found in the cytosol and is rapidly translocated into the nucleus of the cell when it is activated by mitogens such as various growth factors. The phosphoric acid ERK1/2 acts on transcription factors such as c-Jun, NF-AT, and NF-κB to exert biological effects. ERK is the first MAPK member to be discovered. It is the most widely studied and plays an important role in the development of tumors. The ERK-associated intracellular signaling pathway is thought to be the classical MAPK pathway, an important part of a series of kinase enzymatic cascades that transduce extracellular stimuli from the cell membrane into the nucleus.
ERK family
ERK is a silk/threonine protein kinase belonging to the members of Mitogen-Activated Protein Kinases (MAPKs). ERK is an important transduction protein that transmits mitogen signals in the body and is expressed in most cells. The current study found that ERK includes several subfamilies of ERK1/ERK2, ERK3/ERK4, and ERK5. Among them, ERK1/ERK2 is the earliest cloned member of the MAPKs family, collectively referred to as ERK1/2, with relative molecular masses of 42 kd and 44 kd, respectively. ERK1/2 is primarily activated by mitogen stimuli and subsequently leads to activation of a range of transcription factors that ultimately regulate cell proliferation and differentiation. ERK1/2 has up to 90% homology and is a proline-directed serine/threonine kinase. Like other MAPKs family kinases, activation of ERK1/2 requires the phosphorylation of serine (Y) and threonine (T) sites to be active.
The RAS/RAF/MEK/ERK pathway is the most mature in the MAPK pathway and plays an important role in the cell signaling regulatory network. ERK is an important member of this pathway, and the activation process of the ERK cascade has been confirmed. Under external stimulation, Ras protein is activated by cell membrane enrichment, Raf protein is activated by Ras phosphorylation, and then its C-terminal catalytic domain binds to MAPK kinase (MEK), further phosphorylating and activating MEK1/2. MEK1/2 has dual specificity and is activated by phosphorylation of two regulatory sites of threonine and tyrosine at the active site of ERK protein. Activated ERK transfers to the nucleus and phosphorylates transcription factors (CREB), cytoskeleton-associated protein (CAP), and enzymes (RSK) to regulate related gene expression. In addition, it is involved in various physiological processes such as cell growth, development, division, migration, metabolism, and apoptosis.
Figure 1. The RAS/RAF/MEK/MAPK pathways
ERK includes two subtypes with up to 90% homology: ERK1 and ERK2. Although the two subtype sequences are similar, they all have their own independent functions, and ERK2 can well compensate for the functional defects of ERK1. For example, mice that are knocked out ERK2 cause embryo death. Like many kinases, ERK contains a long chain of polypeptides whose N-terminus and C-terminus are mutually curled to form a typical bilobal structure. When MEK activates ERK, phosphorylation of its N-terminal Thr183 and Tyr185 sites results in a conformational change near the N-terminus and ATP-binding site. This effect is transmitted to the C-terminus such that the C-terminal active site binds to the substrate protein to phosphorylate its serine/threonine residue. The special property of ERK diphosphorylation is determined by a cyclic structure called Loop 12 in its molecule. The ring is located on the surface of the molecule and adjacent to the active site, some of which form a lip-like structure called the "phosphorylated lip." This region is considered to be a key structure that determines the activity of ERK protein kinases.
In neuronal apoptosis, the ERK pathway has a dual role. Although most studies have demonstrated that the ERK pathway has an anti-apoptotic effect in neurons, ERK signaling-induced pro-apoptotic effects have also been observed. The different effects of the ERK pathway may result from the different types of neurons, stimuli, interactions with other MAPK pathways used in these studies, and factors that may not be known.
Return to Signaling Pathway
Research Areas Related Targets Featured Products
Cancer ERK CAL-101 (GS-1101)
Infection PI3K TG100-115
Alzheimer's disease MEK GDC0941
Neurological Disease Akt XL147
Cancer Immunotherapy NF-κB Duvelisib
Inflammation/Immunology Ras Quercetin
Cardiovascular and blood system Raf Copanlisib
Endocrinology and Metabolic Disease mTOR TIC-10
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