title: MoniTORing neuronal excitability at the synapse.
abstract: Mammalian target of rapamycin (mTOR) is a key player at the synapse regulating local translation and long-lasting synaptic plasticity. Now, a new study by Sosanya et al. (2013. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201212089) investigates the molecular mechanism of how mTOR suppresses local protein synthesis of a key potassium channel at activated synapses.
authors.affiliation: Department for Anatomy and Cell Biology, Ludwig Maximilian University, D-80336 Munich, Germany.
authors.forename: Inge
authors.initials: I
authors.lastname: Kepert
authors.forename: Michael A
authors.initials: MA
authors.lastname: Kiebler
mesh_terms: D000818:Animals; D051959:ELAV Proteins / Q000378:metabolism*; D000067779:ELAV-Like Protein 4; D006801:Humans; D051662:Kv1.1 Potassium Channel / Q000378:metabolism*; D000076222:Mechanistic Target of Rapamycin Complex 1; D035683:MicroRNAs / Q000378:metabolism*; D046912:Multiprotein Complexes; D011506:Proteins / Q000378:metabolism*; D059748:Proteolysis; D012333:RNA, Messenger / Q000378:metabolism*; D058570:TOR Serine-Threonine Kinases
chemical_list: D051959:ELAV Proteins; D000067779:ELAV-Like Protein 4; C000594136:Elavl4 protein, rat; C489293:Kcna1 protein, rat; D035683:MicroRNAs; D046912:Multiprotein Complexes; D011506:Proteins; D012333:RNA, Messenger; D051662:Kv1.1 Potassium Channel; D000076222:Mechanistic Target of Rapamycin Complex 1; D058570:TOR Serine-Threonine Kinases