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Molecular and Cellular Biology, February 1999, p. 1301-1312, Vol. 19, No. 2
Department of
Pediatrics1 and
Ben May Institute for
Cancer Research and Department of Pharmacological and Physiological
Sciences,2 University of Chicago, Chicago,
Illinois 60637
Received 22 July 1998/Returned for modification 31 August
1998/Accepted 27 October 1998
Mitogen-activated protein (MAP) kinases play distinct roles in a
variety of cellular signaling pathways and are regulated through
multiple mechanisms. In this study, a novel 61-kDa member of the MAP
kinase family, termed extracellular signal-regulated kinase 7 (ERK7),
has been cloned and characterized. Although it has the signature TEY
activation motif of ERK1 and ERK2, ERK7 is not activated by
extracellular stimuli that typically activate ERK1 and ERK2 or by
common activators of c-Jun N-terminal kinase (JNK) and p38 kinase.
Instead, ERK7 has appreciable constitutive activity in serum-starved
cells that is dependent on the presence of its C-terminal domain.
Interestingly, the C-terminal tail, not the kinase domain, of ERK7
regulates its nuclear localization and inhibition of growth. Taken
together, these results elucidate a novel type of MAP kinase whereby
interactions via its C-terminal tail, rather than extracellular
signal-mediated activation cascades, regulate its activity,
localization, and function.
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Extracellular Signal-Regulated Kinase 7 (ERK7), a
Novel ERK with a C-Terminal Domain That Regulates Its Activity, Its
Cellular Localization, and Cell Growth
*
Corresponding author. Mailing address: Ben May
Institute for Cancer Research, University of Chicago, 5841 S. Maryland
Ave., MC 6027, Chicago, IL 60637-1470. Phone: (773) 702-0380. Fax:
(773) 702-4634. E-mail:
mrosner{at}ben-may.bsd.uchicago.edu.
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