Regulation and properties of extracellular signal-regulated protein kinases 1, 2, and 3

David J. Robbins, Erzhen Zhen, Mangeng Cheng, Shuichan Xu, Colleen A. Vanderbilt, Douglas Ebert, Clark Garcia, Alphonsus Dang, Melanie H. Cobb

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


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 languageEnglish (US)
Pages (from-to)1104-1110
Number of pages7
JournalJournal of the American Society of Nephrology
Issue number5
StatePublished - Nov 1993


  • ERK
  • MAP kinases
  • Protein kinases
  • Signal transduction

ASJC Scopus subject areas

  • Nephrology


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