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Rac‐1 and Raf‐1 kinases, components of distinct signaling pathways, activate myotonic dystrophy protein kinase
Author(s) -
Shimizu Miho,
Wang Wenfu,
Walch E.Timothy,
Dunne Patrick W.,
Epstein Henry F.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01692-6
Subject(s) - myotonic dystrophy , biology , kinase , c raf , microbiology and biotechnology , gtpase , map2k7 , signal transduction , map kinase kinase kinase , protein kinase a , cyclin dependent kinase 2 , genetics
Myotonic dystrophy protein kinase (DMPK) is a serine–threonine protein kinase encoded by the myotonic dystrophy (DM) locus on human chromosome 19q13.3. It is a close relative of other kinases that interact with members of the Rho family of small GTPases. We show here that the actin cytoskeleton‐linked GTPase Rac‐1 binds to DMPK, and coexpression of Rac‐1 and DMPK activates its transphosphorylation activity in a GTP‐sensitive manner. DMPK can also bind Raf‐1 kinase, the Ras‐activated molecule of the MAP kinase pathway. Purified Raf‐1 kinase phosphorylates and activates DMPK. The interaction of DMPK with these distinct signals suggests that it may play a role as a nexus for cross‐talk between their respective pathways and may partially explain the remarkable pleiotropy of DM.