Abstract
The extracellular signal-regulated kinases ERK1 and ERK2 are 43- and 41-kd enzymes activated by many extracellular cues. They lie within a protein kinase cascade that is used to achieve many cellular responses. In addition to the wide variety of regulatory contexts in which they are activated, they phosphorylate important regulatory proteins, including receptors, transcription factors, cytoskeletal proteins, and other protein kinases. Thus, the stimulation of this kinase cascade is thought to have a pleiotropic action. ERK1 and ERK2 are controlled by phosphorylation on threonine and tyrosine. To understand the regulatory mechanisms, wild-type and mutant ERKs were expressed in bacteria and phosphorylated with MEK, the enzyme that is upstream of ERKs. Wildtype proteins could be activated 500- to 1,000-fold In vitro by MEK. ERK3, an enzyme of 62 kd and only 50% identical to ERK1 and ERK2 in the catalytic core, was also phosphorylated by MEK in vitro. This suggests that all three of these enzymes are targets of common signaling pathways.
| Original language | English |
|---|---|
| Pages (from-to) | 1104-1110 |
| Number of pages | 7 |
| Journal | Journal of the American Society of Nephrology |
| Volume | 4 |
| Issue number | 5 |
| State | Published - Nov 1 1993 |
| Externally published | Yes |
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Keywords
- ERK
- MAP kinases
- Protein kinases
- Signal transduction
ASJC Scopus subject areas
- Nephrology
Cite this
Regulation and properties of extracellular signal-regulated protein kinases 1, 2, and 3. / Robbins, David J; Zhen, Erzhen; Cheng, Mangeng; Xu, Shuichan; Vanderbilt, Colleen A.; Ebert, Douglas; Garcia, Clark; Dang, Alphonsus; Cobb, Melanie H.
In: Journal of the American Society of Nephrology, Vol. 4, No. 5, 01.11.1993, p. 1104-1110.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Regulation and properties of extracellular signal-regulated protein kinases 1, 2, and 3
AU - Robbins, David J
AU - Zhen, Erzhen
AU - Cheng, Mangeng
AU - Xu, Shuichan
AU - Vanderbilt, Colleen A.
AU - Ebert, Douglas
AU - Garcia, Clark
AU - Dang, Alphonsus
AU - Cobb, Melanie H.
PY - 1993/11/1
Y1 - 1993/11/1
N2 - The extracellular signal-regulated kinases ERK1 and ERK2 are 43- and 41-kd enzymes activated by many extracellular cues. They lie within a protein kinase cascade that is used to achieve many cellular responses. In addition to the wide variety of regulatory contexts in which they are activated, they phosphorylate important regulatory proteins, including receptors, transcription factors, cytoskeletal proteins, and other protein kinases. Thus, the stimulation of this kinase cascade is thought to have a pleiotropic action. ERK1 and ERK2 are controlled by phosphorylation on threonine and tyrosine. To understand the regulatory mechanisms, wild-type and mutant ERKs were expressed in bacteria and phosphorylated with MEK, the enzyme that is upstream of ERKs. Wildtype proteins could be activated 500- to 1,000-fold In vitro by MEK. ERK3, an enzyme of 62 kd and only 50% identical to ERK1 and ERK2 in the catalytic core, was also phosphorylated by MEK in vitro. This suggests that all three of these enzymes are targets of common signaling pathways.
AB - The extracellular signal-regulated kinases ERK1 and ERK2 are 43- and 41-kd enzymes activated by many extracellular cues. They lie within a protein kinase cascade that is used to achieve many cellular responses. In addition to the wide variety of regulatory contexts in which they are activated, they phosphorylate important regulatory proteins, including receptors, transcription factors, cytoskeletal proteins, and other protein kinases. Thus, the stimulation of this kinase cascade is thought to have a pleiotropic action. ERK1 and ERK2 are controlled by phosphorylation on threonine and tyrosine. To understand the regulatory mechanisms, wild-type and mutant ERKs were expressed in bacteria and phosphorylated with MEK, the enzyme that is upstream of ERKs. Wildtype proteins could be activated 500- to 1,000-fold In vitro by MEK. ERK3, an enzyme of 62 kd and only 50% identical to ERK1 and ERK2 in the catalytic core, was also phosphorylated by MEK in vitro. This suggests that all three of these enzymes are targets of common signaling pathways.
KW - ERK
KW - MAP kinases
KW - Protein kinases
KW - Signal transduction
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M3 - Article
C2 - 8305637
AN - SCOPUS:0027688457
VL - 4
SP - 1104
EP - 1110
JO - Journal of the American Society of Nephrology
JF - Journal of the American Society of Nephrology
SN - 1046-6673
IS - 5
ER -