Enzyme Research

Report summarizes enzyme research study findings from Babraham Institute

Published in Gene Therapy Weekly, May 8th, 2008

New research, 'DUSP6/MKP-3 inactivates ERK1/2 but fails to bind and inactivate ERK5,' is the subject of a report. "Extracellular signal-regulated kinase-1 and -2 (ERK1/2) are activated by dual threonine and tyrosine phosphorylation of a TEY motif. The highly related kinase ERK5 is also activated by phosphorylation at a TEY motif," scientists in Cambridge, the United Kingdom report.

"Inactivation of ERK1/2 is achieved by distinct members of the dual-specificity protein phosphatase (DUSP) family, which are responsible for the specific, regulated de-phosphorylation of the TEY motif. These include both nuclear (DUSP5) and cytoplasmic (DUSP6) enzymes. DUSP6, a candidate...

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Source: Gene Therapy Weekly (2008-05-08)

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