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The polo‐like protein kinases Fnk and Snk associate with a Ca 2+ ‐ and integrin‐binding protein and are regulated dynamically with synaptic plasticity
Author(s) -
Kauselmann Gunther,
Weiler Markus,
Wulff Peer,
Jessberger Sebastian,
Konietzko Uwe,
Scafidi Joey,
Staubli Ursula,
BereiterHahn Jürgen,
Strebhardt Klaus,
Kuhl Dietmar
Publication year - 1999
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/18.20.5528
Subject(s) - biology , long term potentiation , synaptic plasticity , kinase , integrin linked kinase , microbiology and biotechnology , phosphorylation , cyclin dependent kinase 5 , protein kinase a , cyclin dependent kinase 2 , biochemistry , receptor
In order to stabilize changes in synaptic strength, neurons activate a program of gene expression that results in alterations of their molecular composition and structure. Here we demonstrate that Fnk and Snk , two members of the polo family of cell cycle associated kinases, are co‐opted by the brain to serve in this program. Stimuli that produce synaptic plasticity, including those that evoke long‐term potentiation (LTP), dramatically increase levels of both kinase mRNAs. Induced Fnk and Snk proteins are targeted to the dendrites of activated neurons, suggesting that they mediate phosphorylation of proteins in this compartment. Moreover, a conserved C‐terminal domain in these kinases is shown to interact specifically with Cib, a Ca 2+ ‐ and integrin‐binding protein. Together, these studies suggest a novel signal transduction mechanism in the stabilization of long‐term synaptic plasticity.