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Comment
. 2013 Jul 8;202(1):7-9.
doi: 10.1083/jcb.201304183.

MoniTORing neuronal excitability at the synapse

Inge Kepert  1 , Michael A Kiebler
Affiliations
Comment

MoniTORing neuronal excitability at the synapse

Inge Kepert et al. J Cell Biol. .

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.

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Figures

Figure 1.
Figure 1.
mTOR-mediated translational control of the Kv1.1 potassium channel at the synapse. This cartoon summarizes a hypothetical model based on the work by Sosanya et al. (2013) linking neuronal receptors, e.g., the NMDAR, with both intracellular mTOR signaling as well as translational control at the synapse (Hoeffer and Klann, 2010). When mTOR is active (right), miR-129 binds to Kv1.1 mRNA, repressing its translation at the synapse. When mTOR is inactivated by adding the mTOR inhibitor rapamycin or by inhibiting the NMDAR (left), HuD displaces miR-129 to relieve translational repression of Kv1.1.
See this image and copyright information in PMC

Comment on

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