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Differential targeting of MAP kinases to the ETS‐domain transcription factor Elk‐1
Author(s) -
Yang ShenHsi,
Whitmarsh Alan J.,
Davis Roger J.,
Sharrocks Andrew D.
Publication year - 1998
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/17.6.1740
Subject(s) - biology , transcription factor , kinase , protein serine threonine kinases , microbiology and biotechnology , computational biology , genetics , gene , protein kinase a
The activation of MAP kinase (MAPK) signal transduction pathways results in the phosphorylation of transcription factors by the terminal kinases in these cascades. Different pathways are activated by mitogenic and stress stimuli, which lead to the activation of distinct groups of target proteins. The ETS‐domain transcription factor Elk‐1 is a substrate for three distinct classes of MAPKs. Elk‐1 contains a targeting domain, the D‐domain, which is distinct from the phosphoacceptor motifs and is required for efficient phosphorylation and activation by the ERK MAPKs. In this study, we demonstrate that members of the JNK subfamily of MAPKs are also targeted to Elk‐1 by this domain. Targeting via this domain is essential for the efficient and rapid phosphorylation and activation of Elk‐1 both in vitro and in vivo . The ERK and JNK MAPKs use overlapping yet distinct determinants in the D‐domain for targeting to Elk‐1. In contrast, members of the p38 subfamily of MAPKs are not targeted to Elk‐1 via this domain. Our data therefore demonstrate that different classes of MAPKs exhibit differential requirements for targeting to Elk‐1.