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Papers In Press, published online ahead of print January 3, 2001
J. Biol. Chem, 10.1074/jbc.M009286200
Submitted on October 11, 2000
Revised on December 21, 2000
Accepted on January 3, 2001

Molecular Cloning of Mouse ERK5/BMK1 Splice Variants and Characterization of ERK5 Functional Domains

Chen Yan, Honglin Luo, Jiing-Dwan Lee, Jun-ichi Abe, and Bradford C. Berk

Center for Cardiovascular Research, University of Rochester, Rochester, NY 14642

Corresponding Author: bradford_berk{at}urmc.rochester.edu

The Mitogen-activated protein kinases (MAPKs) play important roles in regulation of cell growth and survival. Human MAPK 5 (ERK5) or big MAP kinase 1 (BMK1) is a recently cloned member of the MAPK family. To identify ERK5-related kinases, we searched the GenBank expressed sequence tag (EST) database for mouse cDNAs with homology to human ERK5. A full-length mouse cDNA that was highly homologous to the human ERK5 was identified. Further analysis of ERK5 PCR products generated from mouse embryo cDNA yielded three mouse ERK5 cDNAs (mERK5a, mERK5b and mERK5c). Sequence analysis showed that these cDNAs are alternative splice products of the mouse ERK5 gene. Interestingly, expressed mERK5b and mERK5c act as dominant-negative inhibitors based on inhibition of mERK5a kinase activity and mERK5a-mediated MEF2C transactivation. However, the physiological significance of mERK5b and mERK5c is not fully understood. Further investigation using these mouse ERK5 splice variants and other constructed mutants identified functional roles of several regions of mERK5 which appear to be important for protein-protein interaction and intracellular localization. Specifically, we found that the long C-terminal tail, which contains a putative NLS, is not required for activation and kinase activity, but is responsible for the activation of nuclear transcription factor MEF2C due to nuclear targeting. In addition, the N-terminal domain (AA1-77) is important for cytoplasmic targeting; domain (AA78-139) is required for association with the upstream kinase MEK5; and domain (AA140-406) is necessary for oligomerization. Taken together, these observations indicate that ERK5 is regulated by distinct mechanisms determined by its unique structure and presumably the presence of multiple splice variants.


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