TY - JOUR
T1 - Phosphorylation of MAP kinases by MAP/ERK involves multiple regions of MAP kinases
AU - Wilsbacher, Julie L.
AU - Goldsmith, Elizabeth J.
AU - Cobb, Melanie H.
PY - 1999/6/11
Y1 - 1999/6/11
N2 - Mitogen-activated protein (MAP) kinases are activated with great specificity by MAP/ERK kinases (MEKs). The basis for the specific activation is not understood. In this study chimeras composed of two MAP kinases, extracellular signal-regulated protein kinase 2 and p38, were assayed in vitro for phosphorylation and activation by different MEK isoforms to probe the requirements for productive interaction of MAP kinases with MEKs. Experimental results and modeling support the conclusion that the specificity of MEK/MAP kinase phosphorylation results from multiple contacts, including surfaces in both the N- and C-terminal domains.
AB - Mitogen-activated protein (MAP) kinases are activated with great specificity by MAP/ERK kinases (MEKs). The basis for the specific activation is not understood. In this study chimeras composed of two MAP kinases, extracellular signal-regulated protein kinase 2 and p38, were assayed in vitro for phosphorylation and activation by different MEK isoforms to probe the requirements for productive interaction of MAP kinases with MEKs. Experimental results and modeling support the conclusion that the specificity of MEK/MAP kinase phosphorylation results from multiple contacts, including surfaces in both the N- and C-terminal domains.
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U2 - 10.1074/jbc.274.24.16988
DO - 10.1074/jbc.274.24.16988
M3 - Article
C2 - 10358048
AN - SCOPUS:0033546188
SN - 0021-9258
VL - 274
SP - 16988
EP - 16994
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 24
ER -